{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T20:38:33Z","timestamp":1792615113078,"version":"4.5.0"},"reference-count":249,"publisher":"Springer Science and Business Media LLC","issue":"10","license":[{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["World J Microbiol Biotechnol"],"published-print":{"date-parts":[[2025,10]]},"DOI":"10.1007\/s11274-025-04614-1","type":"journal-article","created":{"date-parts":[[2025,10,16]],"date-time":"2025-10-16T09:36:38Z","timestamp":1760607398000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["L-asparaginase: a review of microbial production and protein engineering with translational applications for oncology and food safety"],"prefix":"10.1007","volume":"41","author":[{"given":"Manisha","family":"Thakur","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sanjiv Kumar","family":"Tiwari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0574-4063","authenticated-orcid":false,"given":"Saurabh","family":"Bansal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,10,16]]},"reference":[{"key":"4614_CR1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jgeb.2024.100450","volume":"23","author":"H Abd El Baky","year":"2025","unstructured":"Abd El Baky H, El Baroty G (2025) Algal l\u2013 asparaginase: antioxidant activity, mitigation of acrylamide in fried potato chips, sensory quality and immobilization. J Genet Eng Biotechnol 23:100450. https:\/\/doi.org\/10.1016\/j.jgeb.2024.100450","journal-title":"J Genet Eng Biotechnol"},{"key":"4614_CR2","doi-asserted-by":"publisher","DOI":"10.1186\/s13568-020-01005-7","volume":"10","author":"NA Abdelrazek","year":"2020","unstructured":"Abdelrazek NA, Elkhatib WF, Raafat MM, Aboulwafa MM (2020) Production, characterization and bioinformatics analysis of L-asparaginase from a new Stenotrophomonas maltophilia EMCC2297 soil isolate. AMB Express 10:71. https:\/\/doi.org\/10.1186\/s13568-020-01005-7","journal-title":"AMB Express"},{"key":"4614_CR3","doi-asserted-by":"publisher","DOI":"10.1186\/s13568-024-01700-9","volume":"14","author":"NA Abdelrazek","year":"2024","unstructured":"Abdelrazek NA, Saleh SE, Raafat MM et al (2024) Production of highly cytotoxic and low immunogenic L-asparaginase from Stenotrophomonas maltophilia EMCC2297. AMB Express 14:51. https:\/\/doi.org\/10.1186\/s13568-024-01700-9","journal-title":"AMB Express"},{"key":"4614_CR4","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2024.135458","volume":"279","author":"EM Abdullah","year":"2024","unstructured":"Abdullah EM, Khan MS, Aziz IM et al (2024) Expression, characterization and cytotoxicity of recombinant L-asparaginase II from Salmonella paratyphi cloned in Escherichia coli. Int J Biol Macromol 279:135458. https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.135458","journal-title":"Int J Biol Macromol"},{"key":"4614_CR5","doi-asserted-by":"publisher","DOI":"10.1186\/s43141-022-00309-4","volume":"20","author":"KN Abhini","year":"2022","unstructured":"Abhini KN, Rajan AB, Fathimathu Zuhara K, Sebastian D (2022) Response surface methodological optimization of l-asparaginase production from the medicinal plant endophyte Acinetobacter baumannii ZAS1. J Genet Eng Biotechnol 20:22. https:\/\/doi.org\/10.1186\/s43141-022-00309-4","journal-title":"J Genet Eng Biotechnol"},{"key":"4614_CR6","doi-asserted-by":"publisher","first-page":"5655","DOI":"10.1021\/bi0029595","volume":"40","author":"K Aghaiypour","year":"2001","unstructured":"Aghaiypour K, Wlodawer A, Lubkowski J (2001) Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase. Biochemistry 40:5655\u20135664. https:\/\/doi.org\/10.1021\/bi0029595","journal-title":"Biochemistry"},{"key":"4614_CR7","doi-asserted-by":"publisher","first-page":"659","DOI":"10.31788\/RJC.2022.1516742","volume":"15","author":"A Ahmad","year":"2022","unstructured":"Ahmad A, Asmi N, Karim H et al (2022) Effect of substrate concentration and fecl2 addition on L-asparaginase activities of bacteria symbionts brown algae sargassum sp. and its potential as a new anti-dengue agents. Rasayan J Chem 15:659\u2013667. https:\/\/doi.org\/10.31788\/RJC.2022.1516742","journal-title":"Rasayan J Chem"},{"key":"4614_CR8","doi-asserted-by":"publisher","first-page":"155932582210923","DOI":"10.1177\/15593258221092379","volume":"20","author":"A Aisha","year":"2022","unstructured":"Aisha A, Zahra S, Tahir IM et al (2022) Anticancer L-asparaginase and phytoactive compounds from plant Solanum nigrum against MDR (methicillindrug resistant) Staphylococcus aureus and fungal isolates. Dose-Response 20:15593258221092380. https:\/\/doi.org\/10.1177\/15593258221092379","journal-title":"Dose-Response"},{"key":"4614_CR9","doi-asserted-by":"publisher","first-page":"313","DOI":"10.1007\/s12088-019-00806-0","volume":"59","author":"SS Aishwarya","year":"2019","unstructured":"Aishwarya SS, Selvarajan E, Iyappan S, Rajnish KN (2019) Recombinant l-asparaginase II from Lactobacillus casei subsp. casei ATCC 393 and its anticancer activity. Indian J Microbiol 59:313\u2013320. https:\/\/doi.org\/10.1007\/s12088-019-00806-0","journal-title":"Indian J Microbiol"},{"key":"4614_CR10","doi-asserted-by":"publisher","DOI":"10.1111\/jfpp.15486","volume":"45","author":"B Akg\u00fcn","year":"2021","unstructured":"Akg\u00fcn B, Ar\u0131c\u0131 M, \u00c7avu\u015f F (2021) Application of L-asparaginase to produce high-quality Turkish coffee and the role of precursors in acrylamide formation. J Food Process Preserv 45:e15486. https:\/\/doi.org\/10.1111\/jfpp.15486","journal-title":"J Food Process Preserv"},{"key":"4614_CR11","doi-asserted-by":"publisher","DOI":"10.1002\/biot.202400507","volume":"19","author":"BY Aktar","year":"2024","unstructured":"Aktar BY, Aysan A, Turunen O (2024) L-asparaginase from Lachancea thermotolerans: effect of Lys99Ala on enzyme performance and in vitro antileukemic efficacy. Biotechnol J 19:e202400507. https:\/\/doi.org\/10.1002\/biot.202400507","journal-title":"Biotechnol J"},{"key":"4614_CR12","doi-asserted-by":"publisher","DOI":"10.3390\/md23050194","volume":"23","author":"GM Al-Harbi","year":"2025","unstructured":"Al-Harbi GM, Kotb E, Almiman AA et al (2025) Isolation and characterization of L-asparaginase-producing bacteria from the Arabian-Persian Gulf region: first report on Bacillus xiamenensis ASP-J1-4 as a producer and its potential application. Mar Drugs 23:194. https:\/\/doi.org\/10.3390\/md23050194","journal-title":"Mar Drugs"},{"key":"4614_CR13","doi-asserted-by":"publisher","first-page":"27283","DOI":"10.1007\/s11356-021-17925-1","volume":"29","author":"NE Al-Hazmi","year":"2022","unstructured":"Al-Hazmi NE, Naguib DM (2022) Plant asparaginase versus microbial asparaginase as anticancer agent. Environ Sci Pollut Res 29:27283\u201327293. https:\/\/doi.org\/10.1007\/s11356-021-17925-1","journal-title":"Environ Sci Pollut Res"},{"key":"4614_CR14","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1134\/S1990750822030027","volume":"16","author":"SS Alexandrova","year":"2022","unstructured":"Alexandrova SS, Gladilina YA, Pokrovskaya MV et al (2022) Mechanisms of development of side effects and drug resistance to Asparaginase and ways to overcome them. Biochemistry (Moscow), Supplement Series b: Biomedical Chemistry 16:175\u2013186. https:\/\/doi.org\/10.1134\/S1990750822030027","journal-title":"Biochemistry (Moscow), Supplement Series b: Biomedical Chemistry"},{"key":"4614_CR15","doi-asserted-by":"publisher","DOI":"10.1016\/j.polymertesting.2020.106980","volume":"93","author":"SA Ali Noma","year":"2021","unstructured":"Ali Noma SA, Acet \u00d6, Ulu A et al (2021) L-asparaginase immobilized p(HEMA-GMA) cryogels: a recent study for biochemical, thermodynamic and kinetic parameters. Polym Test 93:106980. https:\/\/doi.org\/10.1016\/j.polymertesting.2020.106980","journal-title":"Polym Test"},{"key":"4614_CR16","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-021-00841-2","volume":"11","author":"MR Almeida","year":"2021","unstructured":"Almeida MR, Crist\u00f3v\u00e3o RO, Barros MA et al (2021) Superior operational stability of immobilized L-asparaginase over surface-modified carbon nanotubes. Sci Rep 11:21529. https:\/\/doi.org\/10.1038\/s41598-021-00841-2","journal-title":"Sci Rep"},{"key":"4614_CR17","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-019-40512-x","volume":"9","author":"SA Alrumman","year":"2019","unstructured":"Alrumman SA, Mostafa YS, Al-izran KA et al (2019) Production and anticancer activity of an L-asparaginase from Bacillus licheniformis isolated from the Red Sea, Saudi Arabia. Sci Rep 9:3756. https:\/\/doi.org\/10.1038\/s41598-019-40512-x","journal-title":"Sci Rep"},{"key":"4614_CR18","doi-asserted-by":"publisher","first-page":"617","DOI":"10.2174\/0113892010309260240624072408","volume":"26","author":"R Alshamy","year":"2025","unstructured":"Alshamy R, El-Nikhely N, Nematalla H et al (2025) Pseudomonas aeruginosa recombinant L-asparaginase: PEGylation with low molecular weight polyethylene glycol, molecular dynamics simulation, in vitro and in vivo serum half-life and biochemical characterization. Curr Pharm Biotechnol 26:617\u2013629. https:\/\/doi.org\/10.2174\/0113892010309260240624072408","journal-title":"Curr Pharm Biotechnol"},{"key":"4614_CR19","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1007\/s10930-020-09932-x","volume":"39","author":"N Aly","year":"2020","unstructured":"Aly N, El-Ahwany A, Ataya FS, Saeed H (2020) Bacillus sonorensis L. asparaginase: cloning, expression in E. coli and characterization. Protein J 39:717\u2013729. https:\/\/doi.org\/10.1007\/s10930-020-09932-x","journal-title":"Protein J"},{"key":"4614_CR20","doi-asserted-by":"publisher","first-page":"2867","DOI":"10.1016\/j.jmb.2015.06.017","volume":"427","author":"A Anishkin","year":"2015","unstructured":"Anishkin A, Vanegas JM, Rogers DM et al (2015) Catalytic role of the substrate defines specificity of therapeutic l-asparaginase. J Mol Biol 427:2867\u20132885. https:\/\/doi.org\/10.1016\/j.jmb.2015.06.017","journal-title":"J Mol Biol"},{"key":"4614_CR21","doi-asserted-by":"publisher","first-page":"1137","DOI":"10.31557\/APJCP.2021.22.4.1137","volume":"22","author":"N Ardalan","year":"2021","unstructured":"Ardalan N, Akhavan Sepahi A, Khavari-Nejad RA (2021) Development of Escherichia coli asparaginase II for the treatment of acute lymphocytic leukemia. In silico reduction of asparaginase II side effects by a novel mutant (V27F). Asian Pac J Cancer Prev 22:1137\u20131147. https:\/\/doi.org\/10.31557\/APJCP.2021.22.4.1137","journal-title":"Asian Pac J Cancer Prev"},{"key":"4614_CR22","doi-asserted-by":"publisher","DOI":"10.1016\/j.pep.2021.106006","volume":"190","author":"N Arumugam","year":"2022","unstructured":"Arumugam N, Thangavelu P (2022) Purification and anticancer activity of glutaminase and urease free intracellular l-asparaginase from Chaetomium sp. Protein Expr Purif 190:106006. https:\/\/doi.org\/10.1016\/j.pep.2021.106006","journal-title":"Protein Expr Purif"},{"key":"4614_CR23","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-018-38094-1","volume":"9","author":"A Ashok","year":"2019","unstructured":"Ashok A, Doriya K, Rao JV et al (2019) Microbes producing l-asparaginase free of glutaminase and urease isolated from extreme locations of Antarctic soil and moss. Sci Rep 9:1423. https:\/\/doi.org\/10.1038\/s41598-018-38094-1","journal-title":"Sci Rep"},{"key":"4614_CR24","doi-asserted-by":"publisher","first-page":"2273","DOI":"10.3109\/10428194.2014.1003056","volume":"56","author":"B Asselin","year":"2015","unstructured":"Asselin B, Rizzari C (2015) Asparaginase pharmacokinetics and implications of therapeutic drug monitoring. Leuk Lymphoma 56:2273\u20132280. https:\/\/doi.org\/10.3109\/10428194.2014.1003056","journal-title":"Leuk Lymphoma"},{"key":"4614_CR25","doi-asserted-by":"publisher","first-page":"1780","DOI":"10.1200\/JCO.1993.11.9.1780","volume":"11","author":"BL Asselin","year":"1993","unstructured":"Asselin BL, Whitin JC, Coppola DJ et al (1993) Comparative pharmacokinetic studies of three asparaginase preparations. J Clin Oncol 11:1780\u20131786. https:\/\/doi.org\/10.1200\/JCO.1993.11.9.1780","journal-title":"J Clin Oncol"},{"key":"4614_CR26","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1016\/S0167-4838(00)00179-5","volume":"1481","author":"H-P Aung","year":"2000","unstructured":"Aung H-P, Bocola M, Schleper S, R\u00f6hm K-H (2000) Dynamics of a mobile loop at the active site of Escherichia coli asparaginase. Biochimica et Biophysica Acta (BBA) 1481:349\u2013359. https:\/\/doi.org\/10.1016\/S0167-4838(00)00179-5","journal-title":"Biochimica et Biophysica Acta (BBA)"},{"key":"4614_CR27","doi-asserted-by":"publisher","first-page":"344","DOI":"10.22099\/ijvr.2024.49166.7208","volume":"25","author":"M Azizian","year":"2024","unstructured":"Azizian M, Tamaddon GH, Ashrafi M et al (2024) Impact of carboxymethyl dextran-asparaginase in NALM-6 cell apoptosis and autophagy. Iran J Vet Res 25:344\u2013352. https:\/\/doi.org\/10.22099\/ijvr.2024.49166.7208","journal-title":"Iran J Vet Res"},{"key":"4614_CR28","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2023.128655","volume":"257","author":"A Baluchi","year":"2024","unstructured":"Baluchi A, Homaei A (2024) Immobilization of l-asparaginase on chitosan nanoparticles for the purpose of long-term application. Int J Biol Macromol 257:128655. https:\/\/doi.org\/10.1016\/j.ijbiomac.2023.128655","journal-title":"Int J Biol Macromol"},{"key":"4614_CR29","doi-asserted-by":"publisher","first-page":"375","DOI":"10.1134\/S0006297910030144","volume":"75","author":"S Bansal","year":"2010","unstructured":"Bansal S, Gnaneswari D, Mishra P, Kundu B (2010) Structural stability and functional analysis of L-asparaginase from Pyrococcus furiosus. Biochemistry (Moscow) 75:375\u2013381. https:\/\/doi.org\/10.1134\/S0006297910030144","journal-title":"Biochemistry (Moscow)"},{"key":"4614_CR30","doi-asserted-by":"publisher","first-page":"1161","DOI":"10.1096\/fj.11-191254","volume":"26","author":"S Bansal","year":"2012","unstructured":"Bansal S, Srivastava A, Mukherjee G et al (2012) Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action. FASEB J 26:1161\u20131171. https:\/\/doi.org\/10.1096\/fj.11-191254","journal-title":"FASEB J"},{"key":"4614_CR31","doi-asserted-by":"publisher","unstructured":"Bansal S, Kundu B (2022) Chapter 39 - Protein engineering: Methods and applications. In: Tripathi T, Dubey VK (eds) Advances in Protein Molecular and Structural Biology Methods. Academic Press, pp 641\u2013668. https:\/\/doi.org\/10.1016\/B978-0-323-90264-9.00039-8","DOI":"10.1016\/B978-0-323-90264-9.00039-8"},{"key":"4614_CR32","doi-asserted-by":"publisher","DOI":"10.3390\/biotech11020010","volume":"11","author":"RAM Barros","year":"2022","unstructured":"Barros RAM, Crist\u00f3v\u00e3o RO, Carabineiro SAC et al (2022) Immobilization and characterization of L-asparaginase over carbon xerogels. Biotech 11:10. https:\/\/doi.org\/10.3390\/biotech11020010","journal-title":"Biotech"},{"key":"4614_CR33","doi-asserted-by":"publisher","DOI":"10.1002\/cplu.202400025","volume":"89","author":"RAM Barros","year":"2024","unstructured":"Barros RAM, Crist\u00f3v\u00e3o RO, Carneiro IG et al (2024) Improved L-asparaginase properties and reusability by immobilization onto functionalized carbon xerogels. ChemPlusChem 89:e202400025. https:\/\/doi.org\/10.1002\/cplu.202400025","journal-title":"ChemPlusChem"},{"key":"4614_CR34","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s40995-017-0359-x","volume":"43","author":"K Beulah","year":"2019","unstructured":"Beulah K, Hemalatha KPJ (2019) Screening of medicinal plants for potential source of L-asparaginase and optimization of conditions for maximum extraction and assay of L-asparaginase from Asparagus racemosus. Iran J Sci Technol Trans Sci 43:1\u20136. https:\/\/doi.org\/10.1007\/s40995-017-0359-x","journal-title":"Iran J Sci Technol Trans Sci"},{"key":"4614_CR35","doi-asserted-by":"publisher","first-page":"222","DOI":"10.1016\/j.fbp.2016.05.010","volume":"99","author":"J Bhagat","year":"2016","unstructured":"Bhagat J, Kaur A, Chadha BS (2016) Single step purification of asparaginase from endophytic bacteria Pseudomonas oryzihabitans exhibiting high potential to reduce acrylamide in processed potato chips. Food Bioprod Process 99:222\u2013230. https:\/\/doi.org\/10.1016\/j.fbp.2016.05.010","journal-title":"Food Bioprod Process"},{"key":"4614_CR36","doi-asserted-by":"publisher","first-page":"919","DOI":"10.1007\/s41208-022-00428-2","volume":"38","author":"M Bhargavi","year":"2022","unstructured":"Bhargavi M, Madhuri RJ (2022) Bio potential of a marine fungus Sarocladium kiliense in fermentative production of anti-cancer enzyme l-asparaginase using solid waste substrates and evaluation of its cytotoxic role against Jurkat J6 and PA1 cell lines. Thalassas 38:919\u2013927. https:\/\/doi.org\/10.1007\/s41208-022-00428-2","journal-title":"Thalassas"},{"key":"4614_CR37","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41417-024-00865-6","volume":"32","author":"M Biswas","year":"2025","unstructured":"Biswas M, Sengupta S, Gandhi KA et al (2025) Engineered L-asparaginase variants with enhanced therapeutic properties to improve treatment of childhood acute lymphatic leukemia. Cancer Gene Ther 32:1\u201314. https:\/\/doi.org\/10.1038\/s41417-024-00865-6","journal-title":"Cancer Gene Ther"},{"key":"4614_CR38","doi-asserted-by":"publisher","first-page":"4097","DOI":"10.1111\/febs.12906","volume":"281","author":"D Borek","year":"2014","unstructured":"Borek D, Kozak M, Pei J, Jaskolski M (2014) Crystal structure of active site mutant of antileukemic L-asparaginase reveals conserved zinc-binding site. FEBS J 281:4097\u20134111. https:\/\/doi.org\/10.1111\/febs.12906","journal-title":"FEBS J"},{"key":"4614_CR39","doi-asserted-by":"publisher","DOI":"10.1186\/s44356-024-00010-3","volume":"1","author":"V Botta","year":"2024","unstructured":"Botta V, Camerino M, Bicanov\u00e1 L (2024) Pilot study investigating the intravenous administration of monomeric L-asparaginase to dogs with multicentric lymphoma. Vet Oncol 1:10. https:\/\/doi.org\/10.1186\/s44356-024-00010-3","journal-title":"Vet Oncol"},{"key":"4614_CR40","doi-asserted-by":"publisher","first-page":"1114","DOI":"10.1038\/1911114a0","volume":"191","author":"JD Broome","year":"1961","unstructured":"Broome JD (1961) Evidence that the L-asparaginase activity of Guinea pig serum is responsible for its antilymphoma effects. Nature 191:1114\u20131115. https:\/\/doi.org\/10.1038\/1911114a0","journal-title":"Nature"},{"issue":"1","key":"4614_CR41","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1084\/jem.118.1.121","volume":"118","author":"JD Broome","year":"1963","unstructured":"Broome JD (1963) Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects. II. Lymphoma 6C3HED cells cultured in a medium devoid of L-asparagine lose their susceptibility to the effects of guinea pig serum in vivo. J Exp Med 118(1):99\u2013120. https:\/\/doi.org\/10.1084\/jem.118.1.121","journal-title":"J Exp Med"},{"key":"4614_CR42","doi-asserted-by":"publisher","DOI":"10.3389\/fbioe.2018.00212","author":"LP Brumano","year":"2019","unstructured":"Brumano LP, da Silva FVS, Costa-Silva TA (2019) Development of L-asparaginase biobetters: current research status and review of the desirable quality profiles. Front Bioeng Biotechnol. https:\/\/doi.org\/10.3389\/fbioe.2018.00212","journal-title":"Front Bioeng Biotechnol"},{"key":"4614_CR43","doi-asserted-by":"publisher","DOI":"10.1016\/j.lwt.2024.116770","volume":"209","author":"M Calabrese","year":"2024","unstructured":"Calabrese M, De Luca L, Basile G (2024) Reducing the acrylamide concentration in homemade bread processed with L-asparaginase. LWT 209:116770. https:\/\/doi.org\/10.1016\/j.lwt.2024.116770","journal-title":"LWT"},{"key":"4614_CR44","doi-asserted-by":"publisher","first-page":"4515","DOI":"10.1007\/s00253-021-11359-y","volume":"105","author":"D Castro","year":"2021","unstructured":"Castro D, Marques ASC, Almeida MR et al (2021) L-asparaginase production review: bioprocess design and biochemical characteristics. Appl Microbiol Biotechnol 105:4515\u20134534. https:\/\/doi.org\/10.1007\/s00253-021-11359-y","journal-title":"Appl Microbiol Biotechnol"},{"key":"4614_CR45","doi-asserted-by":"publisher","DOI":"10.1016\/j.ab.2019.113537","volume":"591","author":"M Chahardahcherik","year":"2020","unstructured":"Chahardahcherik M, Ashrafi M, Ghasemi Y, Aminlari M (2020) Effect of chemical modification with carboxymethyl dextran on kinetic and structural properties of L-asparaginase. Anal Biochem 591:113537. https:\/\/doi.org\/10.1016\/j.ab.2019.113537","journal-title":"Anal Biochem"},{"key":"4614_CR46","doi-asserted-by":"publisher","first-page":"527","DOI":"10.1016\/j.ijbiomac.2021.01.130","volume":"174","author":"N Chakravarty","year":"2021","unstructured":"Chakravarty N, Priyanka SJ, Singh RP (2021) A potential type-II L-asparaginase from marine isolate Bacillus australimaris NJB19: Statistical optimization, in silico analysis and structural modeling. Int J Biol Macromol 174:527\u2013539. https:\/\/doi.org\/10.1016\/j.ijbiomac.2021.01.130","journal-title":"Int J Biol Macromol"},{"key":"4614_CR47","doi-asserted-by":"publisher","first-page":"619","DOI":"10.1002\/bab.1888","volume":"67","author":"S Chand","year":"2020","unstructured":"Chand S, Mahajan RV, Prasad JP et al (2020) A comprehensive review on microbial L-asparaginase: bioprocessing, characterization, and industrial applications. Biotechnol Appl Biochem 67:619\u2013647. https:\/\/doi.org\/10.1002\/bab.1888","journal-title":"Biotechnol Appl Biochem"},{"key":"4614_CR48","doi-asserted-by":"publisher","first-page":"416","DOI":"10.1134\/S0003683822040032","volume":"58","author":"S Chand","year":"2022","unstructured":"Chand S, Mihooliya KN, Sahoo DK et al (2022) L-asparaginase from Bacillus flexus strain SS: isolation, screening, production process optimization, purification, and anticancer activity. Appl Biochem Microbiol 58:416\u2013427. https:\/\/doi.org\/10.1134\/S0003683822040032","journal-title":"Appl Biochem Microbiol"},{"key":"4614_CR49","doi-asserted-by":"publisher","unstructured":"Rezende Corr\u00eaa P, Schwarz MGA, Antunes D, et al (2024) Characterization of Mycobacterium smegmatis Glutaminase-Free Asparaginase (MSMEG_3173). ACS Omega acsomega.4c06459. https:\/\/doi.org\/10.1021\/acsomega.4c06459","DOI":"10.1021\/acsomega.4c06459"},{"key":"4614_CR50","doi-asserted-by":"publisher","first-page":"2114","DOI":"10.1021\/acsomega.7b00110","volume":"2","author":"DM Charbonneau","year":"2017","unstructured":"Charbonneau DM, Aub\u00e9 A, Rachel NM et al (2017) Development of Escherichia coli asparaginase II for immunosensing: a trade-off between receptor density and sensing efficiency. ACS Omega 2:2114\u20132125. https:\/\/doi.org\/10.1021\/acsomega.7b00110","journal-title":"ACS Omega"},{"key":"4614_CR51","doi-asserted-by":"publisher","first-page":"1092","DOI":"10.1002\/cnma.201900245","volume":"5","author":"H Che","year":"2019","unstructured":"Che H, van Hest JCM (2019) Adaptive polymersome nanoreactors. Chemnanomat 5:1092\u20131109. https:\/\/doi.org\/10.1002\/cnma.201900245","journal-title":"Chemnanomat"},{"key":"4614_CR52","doi-asserted-by":"publisher","DOI":"10.1080\/13102818.2023.2281493","volume":"37","author":"A Chergui","year":"2023","unstructured":"Chergui A, Trabelsi L, Salem-Bekhit MM et al (2023) Optimization of intracellular l-asparaginase production by Streptomyces paulus CA01 isolated from wheat bran using the response surface methodology. Biotechnol Biotechnol Equip 37:2281493. https:\/\/doi.org\/10.1080\/13102818.2023.2281493","journal-title":"Biotechnol Biotechnol Equip"},{"key":"4614_CR53","doi-asserted-by":"publisher","first-page":"1384","DOI":"10.1016\/j.ijbiomac.2022.09.162","volume":"221","author":"H Chi","year":"2022","unstructured":"Chi H, Xia B, Shen J et al (2022) Characterization of a novel and glutaminase-free type II L-asparaginase from Corynebacterium glutamicum and its acrylamide alleviation efficiency in potato chips. Int J Biol Macromol 221:1384\u20131393. https:\/\/doi.org\/10.1016\/j.ijbiomac.2022.09.162","journal-title":"Int J Biol Macromol"},{"key":"4614_CR54","doi-asserted-by":"publisher","first-page":"2321","DOI":"10.1007\/s00253-023-12443-1","volume":"107","author":"H Chi","year":"2023","unstructured":"Chi H, Zhu X, Shen J et al (2023) Thermostability enhancement and insight of L-asparaginase from Mycobacterium sp. via consensus-guided engineering. Appl Microbiol Biotechnol 107:2321\u20132333. https:\/\/doi.org\/10.1007\/s00253-023-12443-1","journal-title":"Appl Microbiol Biotechnol"},{"key":"4614_CR55","doi-asserted-by":"publisher","DOI":"10.1016\/j.envres.2024.119543","volume":"259","author":"V Chinnadurai","year":"2024","unstructured":"Chinnadurai V, Govindasamy C (2024) L-asparaginase producing ability of Aspergillus species isolated from tapioca root soil and optimized ideal growth parameters for l-asparaginase production. Environ Res 259:119543. https:\/\/doi.org\/10.1016\/j.envres.2024.119543","journal-title":"Environ Res"},{"key":"4614_CR56","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/j.ijbiomac.2020.01.012","volume":"147","author":"SM Chohan","year":"2020","unstructured":"Chohan SM, Sajed M, Naeem S, Rashid N (2020) Heterologous gene expression and characterization of TK2246, a highly active and thermostable plant type l-asparaginase from Thermococcus kodakarensis. Int J Biol Macromol 147:131\u2013137. https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.01.012","journal-title":"Int J Biol Macromol"},{"key":"4614_CR57","doi-asserted-by":"publisher","first-page":"713","DOI":"10.1007\/s12223-023-01112-5","volume":"69","author":"RW Chua","year":"2024","unstructured":"Chua RW, Song KP, Ting ASY (2024) Antioxidant properties and L-asparaginase activities of endophytic fungi from Cymbidium orchids. Folia Microbiol (Praha) 69:713\u2013722. https:\/\/doi.org\/10.1007\/s12223-023-01112-5","journal-title":"Folia Microbiol (Praha)"},{"key":"4614_CR58","doi-asserted-by":"publisher","DOI":"10.1016\/j.ab.2020.114084","volume":"644","author":"AJL Cooper","year":"2022","unstructured":"Cooper AJL, Dorai T, Pinto JT, Denton TT (2022) The metabolic importance of the overlooked asparaginase II pathway. Anal Biochem 644:114084. https:\/\/doi.org\/10.1016\/j.ab.2020.114084","journal-title":"Anal Biochem"},{"key":"4614_CR59","doi-asserted-by":"publisher","DOI":"10.1016\/j.foodchem.2020.128045","volume":"338","author":"CLO Corr\u00eaa","year":"2021","unstructured":"Corr\u00eaa CLO, das Merces Penha E, dos Anjos MR et al (2021) Use of asparaginase for acrylamide mitigation in coffee and its influence on the content of caffeine, chlorogenic acid, and caffeic acid. Food Chem 338:128045. https:\/\/doi.org\/10.1016\/j.foodchem.2020.128045","journal-title":"Food Chem"},{"key":"4614_CR60","doi-asserted-by":"publisher","DOI":"10.1016\/j.focha.2023.100206","volume":"2","author":"C Covino","year":"2023","unstructured":"Covino C, Sorrentino A, Pierro PD et al (2023) Asparaginase enzyme reduces acrylamide levels in fried and wood oven baked pizza base. Food Chemistry Advances 2:100206. https:\/\/doi.org\/10.1016\/j.focha.2023.100206","journal-title":"Food Chemistry Advances"},{"key":"4614_CR61","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1016\/j.bcab.2018.07.018","volume":"16","author":"MC da Cunha","year":"2018","unstructured":"da Cunha MC, Silva LC, Sato HH, de Castro RJS (2018) Using response surface methodology to improve the L-asparaginase production by Aspergillus niger under solid-state fermentation. Biocatal Agric Biotechnol 16:31\u201336. https:\/\/doi.org\/10.1016\/j.bcab.2018.07.018","journal-title":"Biocatal Agric Biotechnol"},{"key":"4614_CR62","doi-asserted-by":"publisher","DOI":"10.1016\/j.foodres.2019.108658","volume":"126","author":"MC da Cunha","year":"2019","unstructured":"da Cunha MC, dos Santos Aguilar JG, de Melo RR et al (2019) Fungal L-asparaginase: strategies for production and food applications. Food Res Int 126:108658. https:\/\/doi.org\/10.1016\/j.foodres.2019.108658","journal-title":"Food Res Int"},{"key":"4614_CR63","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1080\/10826068.2021.1931881","volume":"52","author":"MC da Cunha","year":"2022","unstructured":"da Cunha MC, Aguilar JG, dos Santos O, Lindo SM, Ros\u00e1rio D et al (2022) L-asparaginase from Aspergillus oryzae spp.: effects of production process and biochemical parameters. Prep Biochem Biotechnol 52:253\u2013263. https:\/\/doi.org\/10.1080\/10826068.2021.1931881","journal-title":"Prep Biochem Biotechnol"},{"key":"4614_CR64","doi-asserted-by":"publisher","DOI":"10.1186\/s13568-023-01521-2","volume":"13","author":"S Darnal","year":"2023","unstructured":"Darnal S, Patial V, Kumar V et al (2023) Biochemical characterization of extremozyme L-asparaginase from Pseudomonas sp. PCH199 for therapeutics. AMB Express 13:22. https:\/\/doi.org\/10.1186\/s13568-023-01521-2","journal-title":"AMB Express"},{"key":"4614_CR65","doi-asserted-by":"publisher","first-page":"955","DOI":"10.1016\/j.ijbiomac.2018.12.162","volume":"125","author":"F Darvishi","year":"2019","unstructured":"Darvishi F, Faraji N, Shamsi F (2019) Production and structural modeling of a novel asparaginase in Yarrowia lipolytica. Int J Biol Macromol 125:955\u2013961. https:\/\/doi.org\/10.1016\/j.ijbiomac.2018.12.162","journal-title":"Int J Biol Macromol"},{"key":"4614_CR66","doi-asserted-by":"publisher","first-page":"5335","DOI":"10.1007\/s00253-022-12086-8","volume":"106","author":"F Darvishi","year":"2022","unstructured":"Darvishi F, Jahanafrooz Z, Mokhtarzadeh A (2022) Microbial l-asparaginase as a promising enzyme for treatment of various cancers. Appl Microbiol Biotechnol 106:5335\u20135347. https:\/\/doi.org\/10.1007\/s00253-022-12086-8","journal-title":"Appl Microbiol Biotechnol"},{"key":"4614_CR67","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2024.130312","volume":"263","author":"F Darvishi","year":"2024","unstructured":"Darvishi F, Beiranvand E, Kalhor H et al (2024) Homology modeling and molecular docking studies to decrease glutamine affinity of Yarrowia lipolytica l-asparaginase. Int J Biol Macromol 263:130312. https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.130312","journal-title":"Int J Biol Macromol"},{"key":"4614_CR68","doi-asserted-by":"publisher","first-page":"551","DOI":"10.4014\/jmb.2112.12050","volume":"32","author":"DB Darwesh","year":"2022","unstructured":"Darwesh DB, Al-Awthan YS, Elfaki I et al (2022) Anticancer activity of extremely effective recombinant L-asparaginase from Burkholderia pseudomallei. J Microbiol Biotechnol 32:551\u2013563. https:\/\/doi.org\/10.4014\/jmb.2112.12050","journal-title":"J Microbiol Biotechnol"},{"key":"4614_CR69","doi-asserted-by":"publisher","first-page":"675","DOI":"10.34172\/apb.2024.048","volume":"14","author":"M Dastmalchi","year":"2024","unstructured":"Dastmalchi M, Hamzeh-Mivehroud M, Rezazadeh H et al (2024) Investigating functional and folding stability of an engineered E. coli L-asparaginase harboring Y176F\/S241C mutations. Adv Pharm Bull 14:675\u2013685. https:\/\/doi.org\/10.34172\/apb.2024.048","journal-title":"Adv Pharm Bull"},{"key":"4614_CR70","doi-asserted-by":"publisher","first-page":"2009","DOI":"10.1110\/ps.9.10.2009","volume":"9","author":"C Derst","year":"2000","unstructured":"Derst C, Henseling J, R\u00f6hm K-H (2000) Engineering the substrate specificity of Escherichia coli asparaginase II. Selective reduction of glutaminase activity by amino acid replacements at position 248. Protein Sci 9:2009\u20132017. https:\/\/doi.org\/10.1110\/ps.9.10.2009","journal-title":"Protein Sci"},{"key":"4614_CR71","doi-asserted-by":"publisher","first-page":"604","DOI":"10.3390\/pharmaceutics13050604","volume":"13","author":"C D\u00edaz-Barriga","year":"2021","unstructured":"D\u00edaz-Barriga C, Villanueva-Flores F, Quester K et al (2021) L-asparaginase-phage P22 nanoreactors: toward a biobetter development for acute lymphoblastic leukemia treatment. Pharmaceutics 13:604. https:\/\/doi.org\/10.3390\/pharmaceutics13050604","journal-title":"Pharmaceutics"},{"key":"4614_CR72","doi-asserted-by":"publisher","DOI":"10.3390\/ph15040406","volume":"15","author":"NV Dobryakova","year":"2022","unstructured":"Dobryakova NV, Zhdanov DD, Sokolov NN et al (2022) Improvement of biocatalytic properties and cytotoxic activity of l-asparaginase from Rhodospirillum rubrum by conjugation with chitosan-based cationic polyelectrolytes. Pharmaceuticals 15:406. https:\/\/doi.org\/10.3390\/ph15040406","journal-title":"Pharmaceuticals"},{"key":"4614_CR73","doi-asserted-by":"publisher","DOI":"10.3390\/ijms25084174","volume":"25","author":"NV Dobryakova","year":"2024","unstructured":"Dobryakova NV, Dumina MV, Zhgun AA et al (2024) L-asparaginase conjugates from the hyperthermophilic Archaea Thermococcus sibiricus with improved biocatalytic properties. Int J Mol Sci 25:4174. https:\/\/doi.org\/10.3390\/ijms25084174","journal-title":"Int J Mol Sci"},{"key":"4614_CR74","doi-asserted-by":"publisher","first-page":"188","DOI":"10.1016\/j.bej.2018.07.024","volume":"138","author":"K Doriya","year":"2018","unstructured":"Doriya K, Kumar DS (2018a) Solid state fermentation of mixed substrate for L-asparaginase production using tray and in-house designed rotary bioreactor. Biochem Eng J 138:188\u2013196. https:\/\/doi.org\/10.1016\/j.bej.2018.07.024","journal-title":"Biochem Eng J"},{"key":"4614_CR75","doi-asserted-by":"publisher","first-page":"244","DOI":"10.1016\/j.bcab.2018.01.004","volume":"13","author":"K Doriya","year":"2018","unstructured":"Doriya K, Kumar DS (2018b) Optimization of solid substrate mixture and process parameters for the production of L-asparaginase and scale-up using tray bioreactor. Biocatal Agric Biotechnol 13:244\u2013250. https:\/\/doi.org\/10.1016\/j.bcab.2018.01.004","journal-title":"Biocatal Agric Biotechnol"},{"key":"4614_CR76","doi-asserted-by":"publisher","DOI":"10.3390\/fermentation11070410","volume":"11","author":"C Dudeja","year":"2025","unstructured":"Dudeja C, Mishra A, Ali A et al (2025) Microbial genome editing with CRISPR\u2013Cas9: recent advances and emerging applications across sectors. Fermentation 11:410. https:\/\/doi.org\/10.3390\/fermentation11070410","journal-title":"Fermentation"},{"key":"4614_CR77","doi-asserted-by":"publisher","DOI":"10.3390\/ijms222413632","volume":"22","author":"M Dumina","year":"2021","unstructured":"Dumina M, Zhgun A, Pokrovskaya M et al (2021) Highly active thermophilic L-asparaginase from Melioribacter roseus represents a novel large group of type II bacterial L-asparaginases from Chlorobi-Ignavibacteriae-Bacteroidetes clade. Int J Mol Sci 22:13632. https:\/\/doi.org\/10.3390\/ijms222413632","journal-title":"Int J Mol Sci"},{"key":"4614_CR78","doi-asserted-by":"publisher","DOI":"10.3390\/ijms26125437","volume":"26","author":"MV Dumina","year":"2025","unstructured":"Dumina MV, Zhdanov DD, Veselovsky AV et al (2025) Hyperthermophilic l-asparaginase from Thermococcus sibiricus and its double mutant with increased activity: insights into substrate specificity and structure. Int J Mol Sci 26:5437. https:\/\/doi.org\/10.3390\/ijms26125437","journal-title":"Int J Mol Sci"},{"key":"4614_CR79","doi-asserted-by":"publisher","first-page":"1205","DOI":"10.1007\/s12223-024-01163-2","volume":"69","author":"V Ebrahimi","year":"2024","unstructured":"Ebrahimi V, Hashemi A (2024) Optimizing recombinant production of L-asparaginase 1 from Saccharomyces cerevisiae using response surface methodology. Folia Microbiol (Praha) 69:1205\u20131219. https:\/\/doi.org\/10.1007\/s12223-024-01163-2","journal-title":"Folia Microbiol (Praha)"},{"key":"4614_CR80","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-38039-x","volume":"14","author":"SB Ebrahimi","year":"2023","unstructured":"Ebrahimi SB, Samanta D (2023) Engineering protein-based therapeutics through structural and chemical design. Nat Commun 14:2411. https:\/\/doi.org\/10.1038\/s41467-023-38039-x","journal-title":"Nat Commun"},{"key":"4614_CR81","doi-asserted-by":"publisher","first-page":"3837","DOI":"10.1080\/07391102.2020.1851300","volume":"40","author":"E El-Fakharany","year":"2022","unstructured":"El-Fakharany E, Orabi H, Abdelkhalek E, Sidkey N (2022) Purification and biotechnological applications of l-asparaginase from newly isolated Bacillus halotolerans OHEM18 as antitumor and antioxidant agent. J Biomol Struct Dyn 40:3837\u20133849. https:\/\/doi.org\/10.1080\/07391102.2020.1851300","journal-title":"J Biomol Struct Dyn"},{"key":"4614_CR82","doi-asserted-by":"publisher","first-page":"2540","DOI":"10.1016\/j.sjbs.2021.01.058","volume":"28","author":"MMAA El-Gendy","year":"2021","unstructured":"El-Gendy MMAA, Awad MF, El-Shenawy FS, El-Bondkly AMA (2021) Production, purification, characterization, antioxidant and antiproliferative activities of extracellular L-asparaginase produced by Fusarium equiseti AHMF4. Saudi J Biol Sci 28:2540\u20132548. https:\/\/doi.org\/10.1016\/j.sjbs.2021.01.058","journal-title":"Saudi J Biol Sci"},{"key":"4614_CR83","doi-asserted-by":"publisher","first-page":"7942","DOI":"10.1038\/s41598-020-64052-x","volume":"10","author":"NE-A El-Naggar","year":"2020","unstructured":"El-Naggar NE-A, El-Shweihy NM (2020) Bioprocess development for L-asparaginase production by Streptomyces rochei, purification and in-vitro efficacy against various human carcinoma cell lines. Sci Rep 10:7942. https:\/\/doi.org\/10.1038\/s41598-020-64052-x","journal-title":"Sci Rep"},{"key":"4614_CR84","doi-asserted-by":"publisher","first-page":"13571","DOI":"10.1038\/s41598-019-49709-6","volume":"9","author":"NE-A El-Naggar","year":"2019","unstructured":"El-Naggar NE-A, Moawad H, El-Shweihy NM et al (2019) Process development for scale-up production of a therapeutic L-asparaginase by Streptomyces brollosae NEAE-115 from shake flasks to bioreactor. Sci Rep 9:13571. https:\/\/doi.org\/10.1038\/s41598-019-49709-6","journal-title":"Sci Rep"},{"key":"4614_CR85","doi-asserted-by":"publisher","first-page":"29625","DOI":"10.1038\/s41598-024-77867-9","volume":"14","author":"NE-A El-Naggar","year":"2024","unstructured":"El-Naggar NE-A, Hamouda RA, Elshafey N (2024) Artificial intelligence-based optimization for extracellular L-glutaminase free L-asparaginase production by Streptomyces violaceoruber under solid state fermentation conditions. Sci Rep 14:29625. https:\/\/doi.org\/10.1038\/s41598-024-77867-9","journal-title":"Sci Rep"},{"key":"4614_CR86","doi-asserted-by":"publisher","first-page":"1169","DOI":"10.1007\/s00726-021-03052-1","volume":"53","author":"M Endicott","year":"2021","unstructured":"Endicott M, Jones M, Hull J (2021) Amino acid metabolism as a therapeutic target in cancer: a review. Amino Acids 53:1169\u20131179. https:\/\/doi.org\/10.1007\/s00726-021-03052-1","journal-title":"Amino Acids"},{"key":"4614_CR87","doi-asserted-by":"publisher","DOI":"10.1007\/s13205-023-03600-4","volume":"13","author":"F Erden-Karao\u011flan","year":"2023","unstructured":"Erden-Karao\u011flan F, Karao\u011flan M (2023) Improvement of recombinant L-asparaginase production in Pichia pastoris. 3 Biotech 13:164. https:\/\/doi.org\/10.1007\/s13205-023-03600-4","journal-title":"3 Biotech"},{"key":"4614_CR88","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1021\/acs.bioconjchem.4c00518","volume":"36","author":"P Erwardt","year":"2025","unstructured":"Erwardt P, Szymczak B, Wi\u015bniewski M et al (2025) L-asparaginase immobilized on nanographene oxide as an efficient nanobiocatalytic tool for asparagine depletion in leukemia cells. Bioconjug Chem 36:253\u2013262. https:\/\/doi.org\/10.1021\/acs.bioconjchem.4c00518","journal-title":"Bioconjug Chem"},{"key":"4614_CR89","doi-asserted-by":"publisher","first-page":"418","DOI":"10.1016\/j.jbiosc.2018.09.007","volume":"127","author":"Y Feng","year":"2019","unstructured":"Feng Y, Liu S, Jiao Y et al (2019) Gene cloning and expression of the L-asparaginase from Bacillus cereus BDRD-ST26 in Bacillus subtilis WB600. J Biosci Bioeng 127:418\u2013424. https:\/\/doi.org\/10.1016\/j.jbiosc.2018.09.007","journal-title":"J Biosci Bioeng"},{"key":"4614_CR90","doi-asserted-by":"publisher","first-page":"1307","DOI":"10.1007\/s00280-014-2464-2","volume":"73","author":"CA Fernandez","year":"2014","unstructured":"Fernandez CA, Stewart E, Panetta JC et al (2014) Successful challenges using native E. coli asparaginase after hypersensitivity reactions to PEGylated E. coli asparaginase. Cancer Chemother Pharmacol 73:1307\u20131313. https:\/\/doi.org\/10.1007\/s00280-014-2464-2","journal-title":"Cancer Chemother Pharmacol"},{"key":"4614_CR91","doi-asserted-by":"publisher","first-page":"719","DOI":"10.1039\/D2BM01237E","volume":"11","author":"NH Fischer","year":"2023","unstructured":"Fischer NH, Oliveira MT, Diness F (2023) Chemical modification of proteins \u2013 challenges and trends at the start of the 2020s. Biomater Sci 11:719\u2013748. https:\/\/doi.org\/10.1039\/D2BM01237E","journal-title":"Biomater Sci"},{"key":"4614_CR92","doi-asserted-by":"publisher","first-page":"111616","DOI":"10.1016\/j.biopha.2021.111616","volume":"139","author":"MHG Fonseca","year":"2021","unstructured":"Fonseca MHG, da Fi\u00faza TS, de Morais SB et al (2021) Circumventing the side effects of L-asparaginase. Biomed Pharmacother 139:111616. https:\/\/doi.org\/10.1016\/j.biopha.2021.111616","journal-title":"Biomed Pharmacother"},{"key":"4614_CR93","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1080\/10826068.2020.1815053","volume":"51","author":"RKB Freire","year":"2021","unstructured":"Freire RKB, Mendon\u00e7a CMN, Ferraro RB et al (2021) Glutaminase-free L-asparaginase production by Leucosporidium muscorum isolated from Antarctic marine-sediment. Prep Biochem Biotechnol 51:277\u2013288. https:\/\/doi.org\/10.1080\/10826068.2020.1815053","journal-title":"Prep Biochem Biotechnol"},{"key":"4614_CR94","doi-asserted-by":"publisher","first-page":"1977","DOI":"10.1517\/14656566.8.12.1977","volume":"8","author":"CH Fu","year":"2007","unstructured":"Fu CH, Sakamoto KM (2007) PEG-asparaginase. Expert Opin Pharmacother 8:1977\u20131984. https:\/\/doi.org\/10.1517\/14656566.8.12.1977","journal-title":"Expert Opin Pharmacother"},{"key":"4614_CR95","doi-asserted-by":"publisher","DOI":"10.1016\/j.foodchem.2022.134224","volume":"402","author":"S Gazi","year":"2023","unstructured":"Gazi S, G\u00f6nc\u00fco\u011flu Ta\u015f N, G\u00f6rg\u00fcl\u00fc A, G\u00f6kmen V (2023) Effectiveness of asparaginase on reducing acrylamide formation in bakery products according to their dough type and properties. Food Chem 402:134224. https:\/\/doi.org\/10.1016\/j.foodchem.2022.134224","journal-title":"Food Chem"},{"key":"4614_CR96","doi-asserted-by":"publisher","DOI":"10.1186\/2043-7129-1-9","volume":"1","author":"S Ghosh","year":"2013","unstructured":"Ghosh S, Murthy S, Govindasamy S, Chandrasekaran M (2013) Optimization of L-asparaginase production by Serratia marcescens (NCIM 2919) under solid state fermentation using coconut oil cake. Sustain Chem Process 1:9. https:\/\/doi.org\/10.1186\/2043-7129-1-9","journal-title":"Sustain Chem Process"},{"key":"4614_CR97","doi-asserted-by":"publisher","first-page":"133731","DOI":"10.1016\/j.ijbiomac.2024.133731","volume":"275","author":"JGS da Gomes","year":"2024","unstructured":"da Gomes JGS, Brand\u00e3o LC, Pinheiro DP et al (2024) Kinetics characterization of a low immunogenic recombinant l-asparaginase from Phaseolus vulgaris with cytotoxic activity against leukemia cells. Int J Biol Macromol 275:133731. https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.133731","journal-title":"Int J Biol Macromol"},{"key":"4614_CR98","doi-asserted-by":"publisher","first-page":"2186","DOI":"10.1038\/s41590-024-02015-4","volume":"25","author":"S Goswami","year":"2024","unstructured":"Goswami S, Pauken KE, Wang L, Sharma P (2024) Next-generation combination approaches for immune checkpoint therapy. Nat Immunol 25:2186\u20132199. https:\/\/doi.org\/10.1038\/s41590-024-02015-4","journal-title":"Nat Immunol"},{"key":"4614_CR99","doi-asserted-by":"publisher","first-page":"4168","DOI":"10.1021\/jf900174q","volume":"57","author":"HV Hendriksen","year":"2009","unstructured":"Hendriksen HV, Kornbrust BA, \u00d8stergaard PR, Stringer MA (2009) Evaluating the potential for enzymatic acrylamide mitigation in a range of food products using an asparaginase from Aspergillus oryzae. J Agric Food Chem 57:4168\u20134176. https:\/\/doi.org\/10.1021\/jf900174q","journal-title":"J Agric Food Chem"},{"key":"4614_CR100","doi-asserted-by":"publisher","first-page":"767","DOI":"10.1007\/s40265-019-01120-1","volume":"79","author":"Y-A Heo","year":"2019","unstructured":"Heo Y-A, Syed YY, Keam SJ (2019) Pegaspargase: a review in acute lymphoblastic leukaemia. Drugs 79:767\u2013777. https:\/\/doi.org\/10.1007\/s40265-019-01120-1","journal-title":"Drugs"},{"key":"4614_CR101","doi-asserted-by":"publisher","first-page":"599","DOI":"10.1134\/S0003683823602937","volume":"60","author":"K Hosseini","year":"2024","unstructured":"Hosseini K, Zivari-Ghader T, Akbarzadehlaleh P et al (2024) A comprehensive review of L-asparaginase: production, applications and therapeutic potential in cancer treatment. Appl Biochem Microbiol 60:599\u2013613. https:\/\/doi.org\/10.1134\/S0003683823602937","journal-title":"Appl Biochem Microbiol"},{"key":"4614_CR102","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1080\/10826068.2024.2449139","volume":"55","author":"K Hosseini","year":"2025","unstructured":"Hosseini K, Zivari-Ghader T, Dilmaghani A et al (2025) Review on up and downstream processing of L-asparaginase. Prep Biochem Biotechnol 55:1\u20139. https:\/\/doi.org\/10.1080\/10826068.2024.2449139","journal-title":"Prep Biochem Biotechnol"},{"key":"4614_CR103","doi-asserted-by":"publisher","first-page":"30","DOI":"10.4161\/bioe.21710","volume":"4","author":"A Huerta-Saquero","year":"2012","unstructured":"Huerta-Saquero A, Evangelista-Mart\u00ednez Z, Moreno-Enriquez A, Perez-Rueda E (2012) Rhizobium etli L- Asparaginase II: an alternative for acute lymphoblastic leukemia (ALL) treatment. Bioengineered 4:30\u201336. https:\/\/doi.org\/10.4161\/bioe.21710","journal-title":"Bioengineered"},{"key":"4614_CR104","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1007\/s12010-008-8438-2","volume":"159","author":"M Hymavathi","year":"2009","unstructured":"Hymavathi M, Sathish T, Rao ChS, Prakasham RS (2009) Enhancement of L-asparaginase production by isolated Bacillus circulans (MTCC 8574) using response surface methodology. Appl Biochem Biotechnol 159:191\u2013198. https:\/\/doi.org\/10.1007\/s12010-008-8438-2","journal-title":"Appl Biochem Biotechnol"},{"key":"4614_CR105","doi-asserted-by":"publisher","DOI":"10.1016\/j.pep.2024.106463","volume":"219","author":"\u0130 \u0130ncir","year":"2024","unstructured":"\u0130ncir \u0130, Kaplan \u00d6 (2024) Escherichia coli as a versatile cell factory: advances and challenges in recombinant protein production. Protein Expr Purif 219:106463. https:\/\/doi.org\/10.1016\/j.pep.2024.106463","journal-title":"Protein Expr Purif"},{"key":"4614_CR106","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.micres.2018.01.011","volume":"208","author":"F Izadpanah Qeshmi","year":"2018","unstructured":"Izadpanah Qeshmi F, Homaei A, Fernandes P, Javadpour S (2018) Marine microbial L-asparaginase: biochemistry, molecular approaches and applications in tumor therapy and in food industry. Microbiol Res 208:99\u2013112. https:\/\/doi.org\/10.1016\/j.micres.2018.01.011","journal-title":"Microbiol Res"},{"key":"4614_CR107","doi-asserted-by":"publisher","first-page":"599","DOI":"10.1007\/s10126-022-10129-9","volume":"24","author":"F Izadpanah Qeshmi","year":"2022","unstructured":"Izadpanah Qeshmi F, Homaei A, Khajeh K et al (2022) Production of a novel marine Pseudomonas aeruginosa recombinant L-asparaginase: insight on the structure and biochemical characterization. Mar Biotechnol 24:599\u2013613. https:\/\/doi.org\/10.1007\/s10126-022-10129-9","journal-title":"Mar Biotechnol"},{"key":"4614_CR108","doi-asserted-by":"publisher","DOI":"10.1016\/j.fochx.2024.102055","volume":"25","author":"A Jana","year":"2025","unstructured":"Jana A, Biswas S, Ghosh R, Modak R (2025) Recent advances in L-asparaginase enzyme production and formulation development for acrylamide reduction during food processing. Food Chemistry: X 25:102055. https:\/\/doi.org\/10.1016\/j.fochx.2024.102055","journal-title":"Food Chemistry: X"},{"key":"4614_CR109","doi-asserted-by":"publisher","DOI":"10.1002\/pro.4647","volume":"32","author":"M Janicki","year":"2023","unstructured":"Janicki M, \u015aciuk A, Zielezinski A et al (2023) The effects of nature-inspired amino acid substitutions on structural and biochemical properties of the E. coli l-asparaginase EcAIII. Protein Sci 32:e4647. https:\/\/doi.org\/10.1002\/pro.4647","journal-title":"Protein Sci"},{"key":"4614_CR110","doi-asserted-by":"publisher","DOI":"10.3390\/microorganisms9081659","volume":"9","author":"R Jia","year":"2021","unstructured":"Jia R, Wan X, Geng X (2021) Microbial L-asparaginase for application in acrylamide mitigation from food: current research status and future perspectives. Microorganisms 9:1659. https:\/\/doi.org\/10.3390\/microorganisms9081659","journal-title":"Microorganisms"},{"key":"4614_CR111","doi-asserted-by":"crossref","unstructured":"Jianhua C, Yujun W, Ruibo J, Min W, Wutong W (2006) Probing the antigenicity of E. coli L-asparaginase by mutational analysis. Mole Biotechnol 33:57\u201365. https:\/\/europepmc.org\/article\/MED\/16691007","DOI":"10.1385\/MB:33:1:57"},{"key":"4614_CR112","doi-asserted-by":"publisher","first-page":"672","DOI":"10.1016\/j.jbiosc.2020.01.007","volume":"129","author":"L Jiao","year":"2020","unstructured":"Jiao L, Chi H, Lu Z et al (2020) Characterization of a novel type I L-asparaginase from Acinetobacter soli and its ability to inhibit acrylamide formation in potato chips. J Biosci Bioeng 129:672\u2013678. https:\/\/doi.org\/10.1016\/j.jbiosc.2020.01.007","journal-title":"J Biosci Bioeng"},{"key":"4614_CR113","doi-asserted-by":"publisher","DOI":"10.3390\/molecules27196670","volume":"27","author":"L Jiao","year":"2022","unstructured":"Jiao L, Chi H, Xia B et al (2022) Thermostability improvement of L-asparaginase from Acinetobacter soli via consensus-designed cysteine residue substitution. Molecules 27:6670. https:\/\/doi.org\/10.3390\/molecules27196670","journal-title":"Molecules"},{"key":"4614_CR114","doi-asserted-by":"publisher","DOI":"10.1007\/s11274-024-03907-1","volume":"40","author":"D Joshi","year":"2024","unstructured":"Joshi D, Patel H, Suthar S et al (2024) Evaluation of the efficiency of thermostable l-asparaginase from B. licheniformis UDS-5 for acrylamide mitigation during preparation of French fries. World J Microbiol Biotechnol 40:92. https:\/\/doi.org\/10.1007\/s11274-024-03907-1","journal-title":"World J Microbiol Biotechnol"},{"key":"4614_CR115","doi-asserted-by":"publisher","first-page":"55","DOI":"10.2147\/BLCTT.S342052","volume":"12","author":"KR Juluri","year":"2022","unstructured":"Juluri KR, Siu C, Cassaday RD (2022) Asparaginase in the treatment of acute lymphoblastic leukemia in adults: current evidence and place in therapy. Blood Lymphat Cancer Targets Ther 12:55\u201379. https:\/\/doi.org\/10.2147\/BLCTT.S342052","journal-title":"Blood Lymphat Cancer Targets Ther"},{"key":"4614_CR116","doi-asserted-by":"publisher","first-page":"410","DOI":"10.1016\/S0022-3565(25)32435-3","volume":"216","author":"Y Kamisaki","year":"1981","unstructured":"Kamisaki Y, Wada H, Yagura T et al (1981) Reduction in immunogenicity and clearance rate of Escherichia coli l-asparaginase by modification with monomethoxypolyethylene glycol. J Pharmacol Exp Ther 216:410\u2013414","journal-title":"J Pharmacol Exp Ther"},{"key":"4614_CR117","doi-asserted-by":"crossref","first-page":"81","DOI":"10.7897\/2277-4572.04219","volume":"4","author":"M Kataria","year":"2015","unstructured":"Kataria M, Kaur N, Narula R et al (2015) L-Asparaginase from novel source-Solanum nigrum and development of asparagine biosensor. Pharma Innov 4:81","journal-title":"Pharma Innov"},{"key":"4614_CR118","doi-asserted-by":"publisher","first-page":"3616","DOI":"10.1021\/acsomega.3c07633","volume":"9","author":"SP Khabade","year":"2024","unstructured":"Khabade SP, Sirigiri DNR, Ram AB (2024) L-Asparaginase from Solanum lycopersicum as a nutraceutical for acute lymphoblastic leukemia. ACS Omega 9:3616\u20133624. https:\/\/doi.org\/10.1021\/acsomega.3c07633","journal-title":"ACS Omega"},{"key":"4614_CR119","doi-asserted-by":"publisher","first-page":"2625","DOI":"10.1007\/s00203-021-02198-6","volume":"203","author":"NM Khalil","year":"2021","unstructured":"Khalil NM, Rodr\u00edguez-Couto S, El-Ghany MNA (2021) Characterization of Penicillium crustosum L-asparaginase and its acrylamide alleviation efficiency in roasted coffee beans at non-cytotoxic levels. Arch Microbiol 203:2625\u20132637. https:\/\/doi.org\/10.1007\/s00203-021-02198-6","journal-title":"Arch Microbiol"},{"issue":"6","key":"4614_CR120","doi-asserted-by":"publisher","first-page":"565","DOI":"10.1084\/jem.98.6.565","volume":"98","author":"JG Kidd","year":"1953","unstructured":"Kidd JG (1953) Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum: I. Course of transplanted cancers of various kinds in mice and rats given guinea pig serum, horse serum, or rabbit serum. J Exp Med 98(6):565\u2013582. https:\/\/doi.org\/10.1084\/jem.98.6.565","journal-title":"J Exp Med"},{"key":"4614_CR121","doi-asserted-by":"publisher","DOI":"10.1007\/s13205-022-03224-0","volume":"12","author":"S Kumar","year":"2022","unstructured":"Kumar S, Darnal S, Patial V et al (2022) Molecular cloning, characterization, and in-silico analysis of l-asparaginase from Himalayan Pseudomonas sp. PCH44. 3 Biotech 12:162. https:\/\/doi.org\/10.1007\/s13205-022-03224-0","journal-title":"3 Biotech"},{"key":"4614_CR122","unstructured":"Kundu B, Bansal S, Mishra P (2016) Mutants of L-asparaginase. https:\/\/patents.google.com\/patent\/US9322008B2\/en"},{"key":"4614_CR123","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1016\/j.enzmictec.2016.06.013","volume":"92","author":"NE Labrou","year":"2016","unstructured":"Labrou NE, Muharram MM (2016) Biochemical characterization and immobilization of Erwinia carotovora l-asparaginase in a microplate for high-throughput biosensing of l-asparagine. Enzyme Microb Technol 92:86\u201393. https:\/\/doi.org\/10.1016\/j.enzmictec.2016.06.013","journal-title":"Enzyme Microb Technol"},{"key":"4614_CR124","doi-asserted-by":"publisher","first-page":"7055","DOI":"10.1007\/s00253-019-09967-w","volume":"103","author":"X Li","year":"2019","unstructured":"Li X, Zhang X, Xu S et al (2019) Insight into the thermostability of thermophilic L-asparaginase and non-thermophilic L-asparaginase II through bioinformatics and structural analysis. Appl Microbiol Biotechnol 103:7055\u20137070. https:\/\/doi.org\/10.1007\/s00253-019-09967-w","journal-title":"Appl Microbiol Biotechnol"},{"key":"4614_CR125","doi-asserted-by":"publisher","DOI":"10.3389\/fchem.2020.00647","author":"M Li","year":"2020","unstructured":"Li M, Zhao G, Su W-K, Shuai Q (2020a) Enzyme-responsive nanoparticles for anti-tumor drug delivery. Front Chem. https:\/\/doi.org\/10.3389\/fchem.2020.00647","journal-title":"Front Chem"},{"key":"4614_CR126","doi-asserted-by":"publisher","first-page":"328","DOI":"10.1158\/1078-0432.CCR-19-1255","volume":"26","author":"R-J Li","year":"2020","unstructured":"Li R-J, Jin R, Liu C et al (2020b) FDA approval summary: Calaspargase pegol-mknl for treatment of acute lymphoblastic leukemia in children and young adults. Clin Cancer Res 26:328\u2013331. https:\/\/doi.org\/10.1158\/1078-0432.CCR-19-1255","journal-title":"Clin Cancer Res"},{"key":"4614_CR127","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2024.138247","volume":"285","author":"Y Li","year":"2025","unstructured":"Li Y, Li Y, Lin Z et al (2025) Heterologous expression of a highly thermostable L-asparaginase from Thermococcus zilligii in Aspergillus niger for efficient reduction of acrylamide in French fries. Int J Biol Macromol 285:138247. https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.138247","journal-title":"Int J Biol Macromol"},{"key":"4614_CR128","doi-asserted-by":"publisher","first-page":"514","DOI":"10.1107\/S2052252521006011","volume":"8","author":"JI Loch","year":"2021","unstructured":"Loch JI, Jaskolski M (2021) Structural and biophysical aspects of L-asparaginases: a growing family with amazing diversity. IUCrJ 8:514\u2013531. https:\/\/doi.org\/10.1107\/S2052252521006011","journal-title":"IUCrJ"},{"key":"4614_CR129","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-27105-x","volume":"12","author":"JI Loch","year":"2021","unstructured":"Loch JI, Imiolczyk B, Sliwiak J (2021) Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site. Nat Commun 12:6717","journal-title":"Nat Commun"},{"key":"4614_CR130","doi-asserted-by":"publisher","first-page":"775","DOI":"10.1107\/S2059798323005648","volume":"79","author":"JI Loch","year":"2023","unstructured":"Loch JI, Worsztynowicz P, Sliwiak J et al (2023) Rhizobium etli has two L-asparaginases with low sequence identity but similar structure and catalytic center. Acta Crystallogr Sect D Struct Biol 79:775\u2013791. https:\/\/doi.org\/10.1107\/S2059798323005648","journal-title":"Acta Crystallogr Sect D Struct Biol"},{"key":"4614_CR131","doi-asserted-by":"publisher","first-page":"252","DOI":"10.1107\/S205979832500292X","volume":"81","author":"JI Loch","year":"2025","unstructured":"Loch JI, Pier\u00f3g I, Imio\u0142czyk B et al (2025) Unique double-helical packing of protein molecules in the crystal of potassium-independent L-asparaginase from common bean. Acta Crystallogr Sect D Struct Biol 81:252\u2013264. https:\/\/doi.org\/10.1107\/S205979832500292X","journal-title":"Acta Crystallogr Sect D Struct Biol"},{"key":"4614_CR132","doi-asserted-by":"publisher","first-page":"82","DOI":"10.3109\/07388551.2015.1120705","volume":"37","author":"AM Lopes","year":"2017","unstructured":"Lopes AM, Oliveira-Nascimento L, Ribeiro A (2017) Therapeutic l-asparaginase: upstream, downstream and beyond. Crit Rev Biotechnol 37:82\u201399. https:\/\/doi.org\/10.3109\/07388551.2015.1120705","journal-title":"Crit Rev Biotechnol"},{"key":"4614_CR133","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1016\/j.pep.2019.02.012","volume":"159","author":"W Lopes","year":"2019","unstructured":"Lopes W, dos Santos BAF, Sampaio ALF et al (2019) Expression, purification, and characterization of asparaginase II from Saccharomyces cerevisiae in Escherichia coli. Protein Expr Purif 159:21\u201326. https:\/\/doi.org\/10.1016\/j.pep.2019.02.012","journal-title":"Protein Expr Purif"},{"key":"4614_CR134","doi-asserted-by":"publisher","first-page":"1850","DOI":"10.1002\/pro.3709","volume":"28","author":"J Lubkowski","year":"2019","unstructured":"Lubkowski J, Wlodawer A (2019) Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase. Protein Sci 28:1850\u20131864. https:\/\/doi.org\/10.1002\/pro.3709","journal-title":"Protein Sci"},{"key":"4614_CR135","doi-asserted-by":"publisher","first-page":"4183","DOI":"10.1111\/febs.16042","volume":"288","author":"J Lubkowski","year":"2021","unstructured":"Lubkowski J, Wlodawer A (2021) Structural and biochemical properties of L-asparaginase. FEBS J 288:4183\u20134209. https:\/\/doi.org\/10.1111\/febs.16042","journal-title":"FEBS J"},{"key":"4614_CR136","doi-asserted-by":"publisher","first-page":"1927","DOI":"10.1021\/acs.biochem.0c00116","volume":"59","author":"J Lubkowski","year":"2020","unstructured":"Lubkowski J, Vanegas J, Chan W-K et al (2020) Mechanism of catalysis by L-asparaginase. Biochemistry 59:1927\u20131945. https:\/\/doi.org\/10.1021\/acs.biochem.0c00116","journal-title":"Biochemistry"},{"key":"4614_CR137","doi-asserted-by":"publisher","DOI":"10.3389\/fped.2022.902117","author":"L Maese","year":"2022","unstructured":"Maese L, Rau RE (2022) Current use of asparaginase in acute lymphoblastic leukemia\/lymphoblastic lymphoma. Front Pediatr. https:\/\/doi.org\/10.3389\/fped.2022.902117","journal-title":"Front Pediatr"},{"key":"4614_CR138","doi-asserted-by":"publisher","DOI":"10.1002\/pbc.29169","volume":"68","author":"L Maese","year":"2021","unstructured":"Maese L, Rizzari C, Coleman R et al (2021) Can recombinant technology address asparaginase Erwinia chrysanthemi shortages? Pediatr Blood Cancer 68:e29169. https:\/\/doi.org\/10.1002\/pbc.29169","journal-title":"Pediatr Blood Cancer"},{"key":"4614_CR139","doi-asserted-by":"publisher","first-page":"704","DOI":"10.1182\/blood.2022016923","volume":"141","author":"L Maese","year":"2023","unstructured":"Maese L, Loh ML, Choi MR (2023) Recombinant Erwinia asparaginase (JZP458) in acute lymphoblastic leukemia: results from the phase 2\/3 AALL1931 study. Blood 141:704\u2013712. https:\/\/doi.org\/10.1182\/blood.2022016923","journal-title":"Blood"},{"key":"4614_CR140","doi-asserted-by":"publisher","first-page":"1498","DOI":"10.1182\/blood-2023-172577","volume":"142","author":"L Maese","year":"2023","unstructured":"Maese L, Loh ML, Choi MR et al (2023b) Efficacy and safety of recombinant Erwinia Asparaginase (JZP458) in acute lymphoblastic leukemia (ALL) or lymphoblastic lymphoma (LBL): complete follow-up of the Children\u2019s Oncology Group (COG) AALL1931 study. Blood 142:1498. https:\/\/doi.org\/10.1182\/blood-2023-172577","journal-title":"Blood"},{"key":"4614_CR141","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-021-98455-1","volume":"11","author":"M Maggi","year":"2021","unstructured":"Maggi M, Meli M, Colombo G, Scotti C (2021) Revealing Escherichia coli type II l-asparaginase active site flexible loop in its open, ligand-free conformation. Sci Rep 11:18885. https:\/\/doi.org\/10.1038\/s41598-021-98455-1","journal-title":"Sci Rep"},{"key":"4614_CR142","doi-asserted-by":"publisher","first-page":"584","DOI":"10.1016\/j.ijbiomac.2020.02.246","volume":"152","author":"B Maqsood","year":"2020","unstructured":"Maqsood B, Basit A, Khurshid M, Bashir Q (2020) Characterization of a thermostable, allosteric l-asparaginase from Anoxybacillus flavithermus. Int J Biol Macromol 152:584\u2013592. https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.02.246","journal-title":"Int J Biol Macromol"},{"key":"4614_CR143","doi-asserted-by":"publisher","DOI":"10.1007\/s12223-025-01247-7","author":"A Marathe","year":"2025","unstructured":"Marathe A, Charya L (2025) Goan mangrove yeast: a source of therapeutic enzyme L-asparaginase. Folia Microbiol (Praha). https:\/\/doi.org\/10.1007\/s12223-025-01247-7","journal-title":"Folia Microbiol (Praha)"},{"key":"4614_CR144","doi-asserted-by":"publisher","DOI":"10.1111\/jfpp.16306","volume":"46","author":"M Masri","year":"2022","unstructured":"Masri M, Nur F, Widodo J et al (2022) A novel l\u2010asparaginase from the symbiotic Enterobacter aerogenes isolated from Eucheuma sp. J Food Process Preserv 46:e16306. https:\/\/doi.org\/10.1111\/jfpp.16306","journal-title":"J Food Process Preserv"},{"key":"4614_CR145","doi-asserted-by":"publisher","first-page":"124","DOI":"10.1016\/j.bcab.2017.06.001","volume":"11","author":"AK Meghavarnam","year":"2017","unstructured":"Meghavarnam AK, Janakiraman S (2017) Solid state fermentation: an effective fermentation strategy for the production of L-asparaginase by Fusarium culmorum (ASP-87). Biocatal Agric Biotechnol 11:124\u2013130. https:\/\/doi.org\/10.1016\/j.bcab.2017.06.001","journal-title":"Biocatal Agric Biotechnol"},{"key":"4614_CR146","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0211951","volume":"14","author":"GP Meneguetti","year":"2019","unstructured":"Meneguetti GP, Santos JHPM, Obreque KMT et al (2019) Novel site-specific PEGylated L-asparaginase. PLoS ONE 14:e0211951. https:\/\/doi.org\/10.1371\/journal.pone.0211951","journal-title":"PLoS ONE"},{"key":"4614_CR147","doi-asserted-by":"publisher","DOI":"10.1007\/s13205-020-2135-4","volume":"10","author":"KN Mihooliya","year":"2020","unstructured":"Mihooliya KN, Nandal J, Kumari A et al (2020) Studies on efficient production of a novel L-asparaginase by a newly isolated Pseudomonas resinovorans IGS-131 and its heterologous expression in Escherichia coli. 3 Biotech 10:148. https:\/\/doi.org\/10.1007\/s13205-020-2135-4","journal-title":"3 Biotech"},{"key":"4614_CR148","doi-asserted-by":"publisher","first-page":"793","DOI":"10.1007\/s40259-023-00622-5","volume":"37","author":"J Miranda","year":"2023","unstructured":"Miranda J, Lefin N, Beltran JF et al (2023) Enzyme engineering strategies for the bioenhancement of L-asparaginase used as a biopharmaceutical. BioDrugs 37:793\u2013811. https:\/\/doi.org\/10.1007\/s40259-023-00622-5","journal-title":"BioDrugs"},{"key":"4614_CR149","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1007\/s10637-021-01173-8","volume":"40","author":"T Modi","year":"2022","unstructured":"Modi T, Gervais D (2022) Improved pharmacokinetic and pharmacodynamic profile of a novel PEGylated native Erwinia chrysanthemi L-asparaginase. Invest New Drugs 40:21\u201329. https:\/\/doi.org\/10.1007\/s10637-021-01173-8","journal-title":"Invest New Drugs"},{"key":"4614_CR150","doi-asserted-by":"publisher","DOI":"10.3389\/fbioe.2020.576511","volume":"8","author":"IS Moguel","year":"2020","unstructured":"Moguel IS, Yamakawa CK, Pessoa A, Mussatto SI (2020) L-asparaginase production by Leucosporidium scottii in a bench-scale bioreactor with co-production of lipids. Front Bioeng Biotechnol 8:576511. https:\/\/doi.org\/10.3389\/fbioe.2020.576511","journal-title":"Front Bioeng Biotechnol"},{"key":"4614_CR151","doi-asserted-by":"publisher","first-page":"433","DOI":"10.1080\/10826068.2013.833110","volume":"44","author":"NS Mohan Kumar","year":"2014","unstructured":"Mohan Kumar NS, Kishore V, Manonmani HK (2014) Chemical modification of L-asparaginase from Cladosporium sp. for improved activity and thermal stability. Prep Biochem Biotechnol 44:433\u2013450. https:\/\/doi.org\/10.1080\/10826068.2013.833110","journal-title":"Prep Biochem Biotechnol"},{"key":"4614_CR152","doi-asserted-by":"publisher","first-page":"1","DOI":"10.20448\/journal.510.2018.51.1.12","volume":"5","author":"SA Moharib","year":"2018","unstructured":"Moharib SA (2018) Anticancer activity of L-asparaginase produced from Vigna unguiculata. World Scientific Research 5:1\u201312. https:\/\/doi.org\/10.20448\/journal.510.2018.51.1.12","journal-title":"World Scientific Research"},{"key":"4614_CR153","doi-asserted-by":"publisher","DOI":"10.1016\/j.colsurfb.2023.113234","volume":"225","author":"M Monajati","year":"2023","unstructured":"Monajati M, Tamaddon AM, Abolmaali SS et al (2023) L-asparaginase immobilization in supramolecular nanogels of PEG-grafted poly HPMA and bis(\u03b1-cyclodextrin) to enhance pharmacokinetics and lower enzyme antigenicity. Colloids Surf B Biointerfaces 225:113234. https:\/\/doi.org\/10.1016\/j.colsurfb.2023.113234","journal-title":"Colloids Surf B Biointerfaces"},{"key":"4614_CR154","doi-asserted-by":"publisher","DOI":"10.1016\/j.heliyon.2024.e40072","volume":"10","author":"M Monajati","year":"2024","unstructured":"Monajati M, Ariafar N, Abedi M et al (2024) Immobilization of l-asparaginase on biofunctionalized magnetic graphene oxide nanocomposite: a promising approach for enhanced stability and reusability. Heliyon 10:e40072. https:\/\/doi.org\/10.1016\/j.heliyon.2024.e40072","journal-title":"Heliyon"},{"key":"4614_CR155","doi-asserted-by":"publisher","DOI":"10.1007\/s13399-025-06779-z","author":"LBS de Moraes","year":"2025","unstructured":"de Moraes LBS, Mota GCP, Molina-Miras A et al (2025) Enhancing high-value metabolite production and asparaginase activity in Haematococcus pluvialis: impact of different organic carbon sources and feeding strategies. Biomass Convers Biorefin. https:\/\/doi.org\/10.1007\/s13399-025-06779-z","journal-title":"Biomass Convers Biorefin"},{"key":"4614_CR156","doi-asserted-by":"publisher","first-page":"292","DOI":"10.4014\/jmb.1107.07047","volume":"22","author":"A Moreno-Enriquez","year":"2012","unstructured":"Moreno-Enriquez A, Evangelista-Martinez Z, Gonzalez-Mondragon EG et al (2012) Biochemical characterization of recombinant L-asparaginase (AnsA) from Rhizobium etli, a member of an increasing rhizobial-type family of L-asparaginases. J Microbiol Biotechnol 22:292\u2013300. https:\/\/doi.org\/10.4014\/jmb.1107.07047","journal-title":"J Microbiol Biotechnol"},{"key":"4614_CR157","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1016\/j.ejbt.2019.10.001","volume":"42","author":"Y Mostafa","year":"2019","unstructured":"Mostafa Y, Alrumman S, Alamri S et al (2019) Enhanced production of glutaminase-free L-asparaginase by marine Bacillus velezensis and cytotoxic activity against breast cancer cell lines. Electron J Biotechnol 42:6\u201315. https:\/\/doi.org\/10.1016\/j.ejbt.2019.10.001","journal-title":"Electron J Biotechnol"},{"key":"4614_CR158","doi-asserted-by":"publisher","DOI":"10.3390\/ijerph19020680","volume":"19","author":"HA Moubasher","year":"2022","unstructured":"Moubasher HA, Balbool BA, Helmy YA et al (2022) Insights into asparaginase from endophytic fungus Lasiodiplodia theobromae: purification, characterization and antileukemic activity. Int J Environ Res Public Health 19:680. https:\/\/doi.org\/10.3390\/ijerph19020680","journal-title":"Int J Environ Res Public Health"},{"key":"4614_CR159","doi-asserted-by":"publisher","unstructured":"Mousa M, El-Dein MMN, Abou-Dobara MI, Metwally NE (2021) Purification and immobilization of L-asparaginase from Citrobacter freundii EGY-NE1 1\u201326. https:\/\/doi.org\/10.21203\/rs.3.rs-876391\/v1","DOI":"10.21203\/rs.3.rs-876391\/v1"},{"key":"4614_CR160","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2025.146363","volume":"321","author":"S Mousavi","year":"2025","unstructured":"Mousavi S, Tariz Y, Lagzian M, Mohammadi M (2025) Computer-aided evolution and experimental validation of a novel L-asparaginase from Bacillus sp. SD3 toward enhanced thermal stability. Int J Biol Macromol 321:146363. https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.146363","journal-title":"Int J Biol Macromol"},{"key":"4614_CR161","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1007\/s00280-001-0391-5","volume":"49","author":"H-J M\u00fcller","year":"2002","unstructured":"M\u00fcller H-J, Beier R, da Palma J (2002) PEG-asparaginase (Oncaspar) 2500 U\/m2 BSA in reinduction and relapse treatment in the ALL\/NHL-BFM protocols. Cancer Chemother Pharmacol 49:149\u2013154. https:\/\/doi.org\/10.1007\/s00280-001-0391-5","journal-title":"Cancer Chemother Pharmacol"},{"key":"4614_CR162","doi-asserted-by":"publisher","first-page":"967","DOI":"10.1007\/s00203-020-01814-1","volume":"202","author":"F Muneer","year":"2020","unstructured":"Muneer F, Siddique MH, Azeem F et al (2020) Microbial L-asparaginase: purification, characterization and applications. Arch Microbiol 202:967\u2013981. https:\/\/doi.org\/10.1007\/s00203-020-01814-1","journal-title":"Arch Microbiol"},{"key":"4614_CR163","doi-asserted-by":"publisher","DOI":"10.1590\/1519-6984.244735","volume":"82","author":"MS Nadeem","year":"2021","unstructured":"Nadeem MS, Khan JA, Al-Ghamdi MA et al (2021) Studies on the recombinant production and anticancer activity of thermostable L- asparaginase I from Pyrococcus abyssi. Braz J Biol 82:e244735. https:\/\/doi.org\/10.1590\/1519-6984.244735","journal-title":"Braz J Biol"},{"key":"4614_CR164","doi-asserted-by":"publisher","first-page":"122","DOI":"10.1016\/j.biochi.2025.03.003","volume":"233","author":"S Natanzi","year":"2025","unstructured":"Natanzi S, Sadat M, Asad S, Mahboudi H, Eslami S (2025) Cloning, Expression, Characterization and in silico studies of L-asparaginase from Vibrio sp. (GBPx3). Biochimie 233:122\u2013131. https:\/\/doi.org\/10.1016\/j.biochi.2025.03.003","journal-title":"Biochimie"},{"key":"4614_CR165","doi-asserted-by":"publisher","first-page":"1549","DOI":"10.1158\/0008-5472.CAN-17-2106","volume":"78","author":"HA Nguyen","year":"2018","unstructured":"Nguyen HA, Su Y, Zhang JY et al (2018) A novel l-asparaginase with low L-glutaminase coactivity is highly efficacious against both T- and B-cell acute lymphoblastic leukemias in vivo. Cancer Res 78:1549\u20131560. https:\/\/doi.org\/10.1158\/0008-5472.CAN-17-2106","journal-title":"Cancer Res"},{"key":"4614_CR166","doi-asserted-by":"publisher","DOI":"10.1007\/s00792-024-01360-4","volume":"28","author":"D Ni","year":"2024","unstructured":"Ni D, Xu W, Zhang W, Mu W (2024) Identification of a thermostable L-asparaginase from Pyrococcus yayanosii CH1 and its application in the reduction of acrylamide. Extremophiles 28:44. https:\/\/doi.org\/10.1007\/s00792-024-01360-4","journal-title":"Extremophiles"},{"key":"4614_CR167","doi-asserted-by":"publisher","DOI":"10.3390\/molecules25245827","volume":"25","author":"JCF Nunes","year":"2020","unstructured":"Nunes JCF, Crist\u00f3v\u00e3o RO, Freire MG et al (2020) Recent strategies and applications for L-asparaginase confinement. Molecules 25:5827. https:\/\/doi.org\/10.3390\/molecules25245827","journal-title":"Molecules"},{"key":"4614_CR168","doi-asserted-by":"publisher","DOI":"10.1016\/j.bcab.2023.102958","volume":"54","author":"Z Nur\u00e7e","year":"2023","unstructured":"Nur\u00e7e Z, Gezgin Y, Hame\u015f EE (2023) Antitumor activity of urease-free Ll-asparaginase with low glutaminase coactivity produced by marine-derived Aspergillus flavus. Biocatal Agric Biotechnol 54:102958. https:\/\/doi.org\/10.1016\/j.bcab.2023.102958","journal-title":"Biocatal Agric Biotechnol"},{"key":"4614_CR169","doi-asserted-by":"publisher","first-page":"1614","DOI":"10.1182\/blood-2010-07-298422","volume":"117","author":"MN Offman","year":"2011","unstructured":"Offman MN, Krol M, Patel N et al (2011) Rational engineering of L-asparaginase reveals importance of dual activity for cancer cell toxicity. Blood 117:1614\u20131621. https:\/\/doi.org\/10.1182\/blood-2010-07-298422","journal-title":"Blood"},{"issue":"4","key":"4614_CR170","doi-asserted-by":"publisher","first-page":"1432","DOI":"10.1007\/s12010-020-03276-z","volume":"191","author":"H Orhan","year":"2020","unstructured":"Orhan H, Akta\u015f Uygun D (2020) Immobilization of L-asparaginase on magnetic nanoparticles for cancer treatment. Appl Biochem Biotechnol 191(4):1432\u20131443. https:\/\/doi.org\/10.1007\/s12010-020-03276-z","journal-title":"Appl Biochem Biotechnol"},{"key":"4614_CR171","doi-asserted-by":"publisher","DOI":"10.1186\/s13568-023-01602-2","volume":"13","author":"S Osama","year":"2023","unstructured":"Osama S, El-Sherei MM, Al-Mahdy DA (2023) Optimization and characterization of antileukemic L-asparaginase produced by Fusarium solani endophyte. AMB Express 13:96. https:\/\/doi.org\/10.1186\/s13568-023-01602-2","journal-title":"AMB Express"},{"key":"4614_CR172","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1016\/j.procbio.2023.01.021","volume":"127","author":"F\u0130 \u00d6zdemir","year":"2023","unstructured":"\u00d6zdemir F\u0130, Karaaslan B, T\u00fclek A et al (2023) Immobilization of recombinant L-asparaginase from Geobacillus kaustophilus on magnetic MWCNT-nickel composites. Process Biochem 127:10\u201320. https:\/\/doi.org\/10.1016\/j.procbio.2023.01.021","journal-title":"Process Biochem"},{"key":"4614_CR173","doi-asserted-by":"publisher","DOI":"10.1007\/s11274-023-03684-3","volume":"39","author":"J Parashiva","year":"2023","unstructured":"Parashiva J, Nuthan BR, Bharatha M et al (2023) Response surface methodology based optimized production, purification, and characterization of L-asparaginase from Fusarium foetens. World J Microbiol Biotechnol 39:252. https:\/\/doi.org\/10.1007\/s11274-023-03684-3","journal-title":"World J Microbiol Biotechnol"},{"key":"4614_CR174","doi-asserted-by":"publisher","first-page":"757","DOI":"10.1016\/j.leukres.2015.04.008","volume":"39","author":"JH Parmentier","year":"2015","unstructured":"Parmentier JH, Maggi M, Tarasco E et al (2015) Glutaminase activity determines cytotoxicity of L-asparaginases on most leukemia cell lines. Leuk Res 39:757\u2013762. https:\/\/doi.org\/10.1016\/j.leukres.2015.04.008","journal-title":"Leuk Res"},{"key":"4614_CR175","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1016\/j.procbio.2022.07.029","volume":"121","author":"PG Patel","year":"2022","unstructured":"Patel PG, Panseriya HZ, Vala AK et al (2022) Exploring current scenario and developments in the field of microbial L-asparaginase production and applications: a review. Process Biochem 121:529\u2013541. https:\/\/doi.org\/10.1016\/j.procbio.2022.07.029","journal-title":"Process Biochem"},{"key":"4614_CR176","doi-asserted-by":"publisher","first-page":"3122","DOI":"10.1007\/s12010-022-04281-0","volume":"195","author":"P Patel","year":"2023","unstructured":"Patel P, Patel A, Agarwal-Rajput R et al (2023) Characterization, anti-proliferative activity, and bench-scale production of novel pH-stable and thermotolerant l-asparaginase from Bacillus licheniformis PPD37. Appl Biochem Biotechnol 195:3122\u20133141. https:\/\/doi.org\/10.1007\/s12010-022-04281-0","journal-title":"Appl Biochem Biotechnol"},{"key":"4614_CR177","doi-asserted-by":"publisher","DOI":"10.1016\/j.foodres.2022.111936","volume":"162","author":"V Patial","year":"2022","unstructured":"Patial V, Kumar V, Joshi R (2022) Acrylamide mitigation in foods using recombinant L-asparaginase: an extremozyme from Himalayan Pseudomonas sp. PCH182. Food Res Int 162:111936. https:\/\/doi.org\/10.1016\/j.foodres.2022.111936","journal-title":"Food Res Int"},{"key":"4614_CR178","doi-asserted-by":"publisher","DOI":"10.1016\/j.bcab.2020.101677","volume":"27","author":"V Paul","year":"2020","unstructured":"Paul V, Tiwary BN (2020) An investigation on the acrylamide mitigation potential of L-asparaginase from Aspergillus terreus BV-C strain. Biocatal Agric Biotechnol 27:101677. https:\/\/doi.org\/10.1016\/j.bcab.2020.101677","journal-title":"Biocatal Agric Biotechnol"},{"key":"4614_CR179","doi-asserted-by":"publisher","first-page":"386","DOI":"10.1016\/j.foodchem.2007.12.057","volume":"109","author":"F Pedreschi","year":"2008","unstructured":"Pedreschi F, Kaack K, Granby K (2008) The effect of asparaginase on acrylamide formation in French fries. Food Chem 109:386\u2013392. https:\/\/doi.org\/10.1016\/j.foodchem.2007.12.057","journal-title":"Food Chem"},{"key":"4614_CR180","doi-asserted-by":"publisher","first-page":"1473","DOI":"10.1016\/j.lwt.2011.02.004","volume":"44","author":"F Pedreschi","year":"2011","unstructured":"Pedreschi F, Mariotti S, Granby K, Risum J (2011) Acrylamide reduction in potato chips by using commercial asparaginase in combination with conventional blanching. LWT 44:1473\u20131476. https:\/\/doi.org\/10.1016\/j.lwt.2011.02.004","journal-title":"LWT"},{"key":"4614_CR181","doi-asserted-by":"publisher","DOI":"10.3390\/ijms24087550","volume":"24","author":"A Pedroso","year":"2023","unstructured":"Pedroso A, Herrera Bel\u00e9n L, Beltr\u00e1n JF et al (2023) In silico design of a chimeric humanized L-asparaginase. Int J Mol Sci 24:7550. https:\/\/doi.org\/10.3390\/ijms24087550","journal-title":"Int J Mol Sci"},{"key":"4614_CR182","doi-asserted-by":"publisher","first-page":"2031","DOI":"10.2174\/1389201022666210211124232","volume":"22","author":"GB Pendharkar","year":"2021","unstructured":"Pendharkar GB, Sonawane HG, Khare KA, Yadav D (2021) Production of chemotherapeutic enzyme L-asparaginase from a fungal source. Curr Pharm Biotechnol 22:2031\u20132037. https:\/\/doi.org\/10.2174\/1389201022666210211124232","journal-title":"Curr Pharm Biotechnol"},{"issue":"2","key":"4614_CR183","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1002\/cncr.25489","volume":"117","author":"R Pieters","year":"2010","unstructured":"Pieters R, Hunger SP, Boos J (2010) L-asparaginase treatment in acute lymphoblastic leukemia. Cancer 117(2):238\u2013249. https:\/\/doi.org\/10.1002\/cncr.25489","journal-title":"Cancer"},{"key":"4614_CR184","doi-asserted-by":"publisher","DOI":"10.3389\/fchem.2024.1381032","author":"K Pokrywka","year":"2024","unstructured":"Pokrywka K, Grzechowiak M, Sliwiak J et al (2024) Probing the active site of class 3 L-asparaginase by mutagenesis. I. Tinkering with the zinc coordination site of ReAV. Front Chem. https:\/\/doi.org\/10.3389\/fchem.2024.1381032","journal-title":"Front Chem"},{"key":"4614_CR185","doi-asserted-by":"publisher","first-page":"1159","DOI":"10.1111\/febs.17388","volume":"292","author":"K Pokrywka","year":"2025","unstructured":"Pokrywka K, Grzechowiak M, Sliwiak J et al (2025a) Controlling enzyme activity by mutagenesis and metal exchange to obtain crystal structures of stable substrate complexes of class 3 L-asparaginase. FEBS J 292:1159\u20131173. https:\/\/doi.org\/10.1111\/febs.17388","journal-title":"FEBS J"},{"key":"4614_CR186","doi-asserted-by":"publisher","DOI":"10.3390\/biom15070944","volume":"15","author":"K Pokrywka","year":"2025","unstructured":"Pokrywka K, Grzechowiak M, Sliwiak J et al (2025b) Probing the active site of class 3 L-Asparaginase by mutagenesis: mutations of the Ser-Lys tandems of ReAV. Biomolecules 15:944. https:\/\/doi.org\/10.3390\/biom15070944","journal-title":"Biomolecules"},{"key":"4614_CR187","doi-asserted-by":"publisher","DOI":"10.1016\/j.colsurfb.2020.111032","volume":"192","author":"LHRR Possarle","year":"2020","unstructured":"Possarle LHRR, Siqueira Junior JR, Caseli L (2020) Insertion of carbon nanotubes in Langmuir-Blodgett films of stearic acid and asparaginase enhancing the catalytic performance. Colloids Surf B Biointerfaces 192:111032. https:\/\/doi.org\/10.1016\/j.colsurfb.2020.111032","journal-title":"Colloids Surf B Biointerfaces"},{"key":"4614_CR188","doi-asserted-by":"publisher","first-page":"260","DOI":"10.1080\/10826068.2019.1692221","volume":"50","author":"P Prakash","year":"2020","unstructured":"Prakash P, Singh HR, Jha SK (2020) Production, purification and kinetic characterization of glutaminase free anti-leukemic L-asparaginase with low endotoxin level from novel soil isolate. Prep Biochem Biotechnol 50:260\u2013271. https:\/\/doi.org\/10.1080\/10826068.2019.1692221","journal-title":"Prep Biochem Biotechnol"},{"key":"4614_CR189","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1007\/s42770-023-00939-x","volume":"54","author":"A Ratuchne","year":"2023","unstructured":"Ratuchne A, Izidoro SC, Beitel SM et al (2023) A new extracellular glutaminase and urease-free l-asparaginase from Meyerozyma guilliermondii. Braz J Microbiol 54:715\u2013723. https:\/\/doi.org\/10.1007\/s42770-023-00939-x","journal-title":"Braz J Microbiol"},{"key":"4614_CR190","doi-asserted-by":"publisher","DOI":"10.1016\/j.foodcont.2020.107739","volume":"123","author":"E Rottmann","year":"2021","unstructured":"Rottmann E, Hauke KF, Krings U, Berger RG (2021) Enzymatic acrylamide mitigation in French fries \u2013 an industrial-scale case study. Food Control 123:107739. https:\/\/doi.org\/10.1016\/j.foodcont.2020.107739","journal-title":"Food Control"},{"key":"4614_CR191","doi-asserted-by":"publisher","first-page":"833","DOI":"10.1517\/14712591003769808","volume":"10","author":"M Rytting","year":"2010","unstructured":"Rytting M (2010) Peg-asparaginase for acute lymphoblastic leukemia. Expert Opin Biol Ther 10:833\u2013839. https:\/\/doi.org\/10.1517\/14712591003769808","journal-title":"Expert Opin Biol Ther"},{"key":"4614_CR192","doi-asserted-by":"publisher","first-page":"812","DOI":"10.1016\/j.ijbiomac.2020.04.080","volume":"156","author":"H Saeed","year":"2020","unstructured":"Saeed H, Hemida A, El-Nikhely N et al (2020) Highly efficient Pyrococcus furiosus recombinant L-asparaginase with no glutaminase activity: expression, purification, functional characterization, and cytotoxicity on THP-1, A549 and Caco-2 cell lines. Int J Biol Macromol 156:812\u2013828. https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.04.080","journal-title":"Int J Biol Macromol"},{"key":"4614_CR193","doi-asserted-by":"publisher","DOI":"10.1016\/j.pep.2021.105820","volume":"181","author":"H Saeed","year":"2021","unstructured":"Saeed H, Hemida A, Abdel-Fattah M et al (2021) Pseudomonas aeruginosa recombinant L-asparaginase: large scale production, purification, and cytotoxicity on THP-1, MDA-MB-231, A549, Caco2 and HCT-116 cell lines. Protein Expr Purif 181:105820. https:\/\/doi.org\/10.1016\/j.pep.2021.105820","journal-title":"Protein Expr Purif"},{"key":"4614_CR194","doi-asserted-by":"publisher","first-page":"15","DOI":"10.15171\/bi.2019.03","volume":"9","author":"A Safary","year":"2019","unstructured":"Safary A, Moniri R, Hamzeh-Mivehroud M, Dastmalchi S (2019) Highly efficient novel recombinant L-asparaginase with no glutaminase activity from a new halo-thermotolerant Bacillus strain. Bioimpacts 9:15\u201323. https:\/\/doi.org\/10.15171\/bi.2019.03","journal-title":"Bioimpacts"},{"issue":"3-4","key":"4614_CR195","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1002\/jobm.202200116","volume":"63","author":"SK Saleena","year":"2023","unstructured":"Saleena SK, Johnson JI, Joseph JK (2023) Production and optimization of L-asparaginase by Streptomyces koyangensis SK4 isolated from Arctic sediment. J Basic Microbiol 63(3\u20134):417\u2013426. https:\/\/doi.org\/10.1002\/jobm.202200116","journal-title":"J Basic Microbiol"},{"key":"4614_CR196","doi-asserted-by":"publisher","DOI":"10.1186\/s12866-025-03833-8","volume":"25","author":"AA Saleh","year":"2025","unstructured":"Saleh AA, El-Aref HM, Ezzeldin AM et al (2025) L-asparaginase from the novel Fusarium falciforme AUMC 16563: extraction, purification, characterization, and cytotoxic effects on PC-3, HePG-2, HCT-116, and MCF-7 cell lines. BMC Microbiol 25:145. https:\/\/doi.org\/10.1186\/s12866-025-03833-8","journal-title":"BMC Microbiol"},{"key":"4614_CR197","doi-asserted-by":"publisher","first-page":"2134","DOI":"10.1182\/blood.V116.21.2134.2134","volume":"116","author":"W Salzer","year":"2010","unstructured":"Salzer W, Asselin B, Supko J et al (2010) Administration of Erwinia asparaginase (Erwinase\u00ae) following allergy to PEG-asparaginase in children and young adults with acute lymphoblastic leukemia treated on AALL07P2 achieves therapeutic nadir serum asparaginase activity: a report from the Children\u2019s Oncology Group (COG). Blood 116:2134. https:\/\/doi.org\/10.1182\/blood.V116.21.2134.2134","journal-title":"Blood"},{"key":"4614_CR198","doi-asserted-by":"publisher","first-page":"1407","DOI":"10.1517\/14712598.2012.718327","volume":"12","author":"W Salzer","year":"2012","unstructured":"Salzer W, Seibel N, Smith M (2012) Erwinia asparaginase in pediatric acute lymphoblastic leukemia. Expert Opin Biol Ther 12:1407\u20131414. https:\/\/doi.org\/10.1517\/14712598.2012.718327","journal-title":"Expert Opin Biol Ther"},{"key":"4614_CR199","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1111\/nyas.12496","volume":"1329","author":"WL Salzer","year":"2014","unstructured":"Salzer WL, Asselin BL, Plourde PV et al (2014) Development of asparaginase Erwinia chrysanthemi for the treatment of acute lymphoblastic leukemia. Ann N Y Acad Sci 1329:81\u201392. https:\/\/doi.org\/10.1111\/nyas.12496","journal-title":"Ann N Y Acad Sci"},{"key":"4614_CR200","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1016\/j.procbio.2023.03.003","volume":"129","author":"I S\u00e1nchez-Moguel","year":"2023","unstructured":"S\u00e1nchez-Moguel I, Costa-Silva TA, Pillaca-Pullo OS (2023) Antarctic yeasts as a source of L-asparaginase: characterization of a glutaminase-activity free L-asparaginase from psychrotolerant yeast Leucosporidium scottii L115. Process Biochem 129:121\u2013132. https:\/\/doi.org\/10.1016\/j.procbio.2023.03.003","journal-title":"Process Biochem"},{"key":"4614_CR201","doi-asserted-by":"publisher","first-page":"776","DOI":"10.1080\/10428194.2023.2171267","volume":"64","author":"M Sandley","year":"2023","unstructured":"Sandley M, Angus J (2023) Asparaginase therapy in patients with acute lymphoblastic leukemia: expert opinion on use and toxicity management. Leuk Lymphoma 64:776\u2013787. https:\/\/doi.org\/10.1080\/10428194.2023.2171267","journal-title":"Leuk Lymphoma"},{"key":"4614_CR202","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2024.136442","volume":"281","author":"A Sania","year":"2024","unstructured":"Sania A, Muhammad MA, Sajed M et al (2024) Engineering Tk1656, a highly active l-asparaginase from Thermococcus kodakarensis, for enhanced activity and stability. Int J Biol Macromol 281:136442. https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.136442","journal-title":"Int J Biol Macromol"},{"issue":"8-9","key":"4614_CR203","doi-asserted-by":"publisher","first-page":"528","DOI":"10.1007\/s12033-016-9950-1","volume":"58","author":"EP Sannikova","year":"2016","unstructured":"Sannikova EP, Bulushova NV, Cheperegin SE et al (2016) The modified heparin-binding l-asparaginase of Wolinella succinogenes. Mol Biotechnol 58(8\u20139):528\u2013539. https:\/\/doi.org\/10.1007\/s12033-016-9950-1","journal-title":"Mol Biotechnol"},{"key":"4614_CR204","doi-asserted-by":"publisher","first-page":"241","DOI":"10.1007\/s12010-024-05002-5","volume":"197","author":"H Sapkota","year":"2025","unstructured":"Sapkota H, Singhania U, Jadhav S (2025) Isolation, identification, and characterization of L-asparaginase-producing human commensal bacterial strains: a promising next-gen probiotics. Appl Biochem Biotechnol 197:241\u2013267. https:\/\/doi.org\/10.1007\/s12010-024-05002-5","journal-title":"Appl Biochem Biotechnol"},{"key":"4614_CR205","doi-asserted-by":"publisher","first-page":"5088","DOI":"10.1074\/jbc.M115.699884","volume":"291","author":"AM Schalk","year":"2016","unstructured":"Schalk AM, Antansijevic A, Caffrey M, Lavie A (2016) Experimental data in support of a direct displacement mechanism for type I\/II L-asparaginases *. J Biol Chem 291:5088\u20135100. https:\/\/doi.org\/10.1074\/jbc.M115.699884","journal-title":"J Biol Chem"},{"key":"4614_CR206","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1080\/10826068.2021.1972426","volume":"52","author":"D Sharma","year":"2022","unstructured":"Sharma D, Mishra A (2022a) L-asparaginase production in solid-state fermentation using Aspergillus niger: process modeling by artificial neural network approach. Prep Biochem Biotechnol 52:549\u2013560. https:\/\/doi.org\/10.1080\/10826068.2021.1972426","journal-title":"Prep Biochem Biotechnol"},{"key":"4614_CR207","doi-asserted-by":"publisher","DOI":"10.1007\/s13205-022-03440-8","volume":"13","author":"D Sharma","year":"2022","unstructured":"Sharma D, Mishra A (2022b) Apoptosis induction in leukemic cells by L-asparaginase preparation from Bacillus indicus: bench-scale production, purification and therapeutic application. 3 Biotech 13:21. https:\/\/doi.org\/10.1007\/s13205-022-03440-8","journal-title":"3 Biotech"},{"key":"4614_CR208","doi-asserted-by":"publisher","first-page":"17858","DOI":"10.1007\/s11356-023-26977-4","volume":"31","author":"D Sharma","year":"2024","unstructured":"Sharma D, Mishra A (2024) Synergistic effects of ternary mixture formulation and process parameters optimization in a sequential approach for enhanced L-asparaginase production using agro-industrial wastes. Environ Sci Pollut Res 31:17858\u201317873. https:\/\/doi.org\/10.1007\/s11356-023-26977-4","journal-title":"Environ Sci Pollut Res"},{"key":"4614_CR209","doi-asserted-by":"publisher","DOI":"10.1016\/j.talo.2023.100261","volume":"8","author":"A Sharma","year":"2023","unstructured":"Sharma A, Sengupta S, Kumar L (2023) Recent advancements in photodynamic therapy and cancer biosensor using natural products. Talanta Open 8:100261. https:\/\/doi.org\/10.1016\/j.talo.2023.100261","journal-title":"Talanta Open"},{"key":"4614_CR210","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/j.ijbiomac.2016.11.115","volume":"96","author":"R Shi","year":"2017","unstructured":"Shi R, Liu Y, Mu Q et al (2017) Biochemical characterization of a novel L-asparaginase from Paenibacillus barengoltzii being suitable for acrylamide reduction in potato chips and mooncakes. Int J Biol Macromol 96:93\u201399. https:\/\/doi.org\/10.1016\/j.ijbiomac.2016.11.115","journal-title":"Int J Biol Macromol"},{"key":"4614_CR211","doi-asserted-by":"publisher","first-page":"40982","DOI":"10.1021\/acsomega.3c03491","volume":"8","author":"S Shinde","year":"2023","unstructured":"Shinde S, Balasubramaniam AK, Mulay V et al (2023) Recent advancements in extraction techniques of Ashwagandha (Withania somnifera) with insights on phytochemicals, structural significance, pharmacology, and current trends in food applications. ACS Omega 8:40982\u201341003. https:\/\/doi.org\/10.1021\/acsomega.3c03491","journal-title":"ACS Omega"},{"key":"4614_CR212","doi-asserted-by":"publisher","DOI":"10.3390\/ijms242015220","volume":"24","author":"AN Shishparenok","year":"2023","unstructured":"Shishparenok AN, Gladilina YA, Zhdanov DD (2023) Engineering and expression strategies for optimization of L-asparaginase development and production. Int J Mol Sci 24:15220. https:\/\/doi.org\/10.3390\/ijms242015220","journal-title":"Int J Mol Sci"},{"key":"4614_CR213","doi-asserted-by":"publisher","first-page":"1727","DOI":"10.1134\/S0006297924100067","volume":"89","author":"AN Shishparenok","year":"2024","unstructured":"Shishparenok AN, Petryaev ER, Koroleva SA et al (2024) Bacterial cellulose-chitosan composite for prolonged-action L-asparaginase in treatment of melanoma cells. Biochemistry (Moscow) 89:1727\u20131743. https:\/\/doi.org\/10.1134\/S0006297924100067","journal-title":"Biochemistry (Moscow)"},{"key":"4614_CR214","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.critrevonc.2015.01.002","volume":"100","author":"A Shrivastava","year":"2016","unstructured":"Shrivastava A, Khan AA, Khurshid M et al (2016) Recent developments in L-asparaginase discovery and its potential as anticancer agent. Crit Rev Oncol Hematol 100:1\u201310. https:\/\/doi.org\/10.1016\/j.critrevonc.2015.01.002","journal-title":"Crit Rev Oncol Hematol"},{"key":"4614_CR215","doi-asserted-by":"publisher","first-page":"503","DOI":"10.1002\/bab.2127","volume":"69","author":"LS da Silva","year":"2022","unstructured":"da Silva LS, Doonan LB, Pessoa. A Jr et al (2022) Structural and functional diversity of asparaginases: overview and recommendations for a revised nomenclature. Biotechnol Appl Biochem 69:503\u2013513. https:\/\/doi.org\/10.1002\/bab.2127","journal-title":"Biotechnol Appl Biochem"},{"key":"4614_CR216","doi-asserted-by":"publisher","first-page":"8409","DOI":"10.1007\/s11696-024-03681-2","volume":"78","author":"JC da Silva","year":"2024","unstructured":"da Silva JC, Bragantin B, Etchegaray A et al (2024) An electrochemical biosensor to detect anti-asparaginase antibodies using immobilized ASNase on carbon-printed electrodes. Chem Pap 78:8409\u20138416. https:\/\/doi.org\/10.1007\/s11696-024-03681-2","journal-title":"Chem Pap"},{"key":"4614_CR217","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1038\/s41586-025-09021-y","volume":"643","author":"RA Silverstein","year":"2025","unstructured":"Silverstein RA, Kim N, Kroell A-S et al (2025) Custom CRISPR\u2013Cas9 PAM variants via scalable engineering and machine learning. Nature 643:539\u2013550. https:\/\/doi.org\/10.1038\/s41586-025-09021-y","journal-title":"Nature"},{"key":"4614_CR218","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1007\/s40495-021-00271-8","volume":"8","author":"A Singh","year":"2022","unstructured":"Singh A, Verma N, Kumar K (2022) Fabrication and construction of highly sensitive polymeric nanoparticle-based electrochemical biosensor for asparagine detection. Curr Pharmacol Rep 8:62\u201371. https:\/\/doi.org\/10.1007\/s40495-021-00271-8","journal-title":"Curr Pharmacol Rep"},{"key":"4614_CR219","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1016\/j.ejbt.2024.05.002","volume":"71","author":"T Sisay","year":"2024","unstructured":"Sisay T, Mobegi VA, Wachira S, Maina N (2024) Isolation and characterization of fungi producing L-asparaginase with reduced L-glutaminase activity from soil samples. Electron J Biotechnol 71:10\u201318. https:\/\/doi.org\/10.1016\/j.ejbt.2024.05.002","journal-title":"Electron J Biotechnol"},{"key":"4614_CR220","doi-asserted-by":"publisher","DOI":"10.3389\/fchem.2024.1373312","author":"J Sliwiak","year":"2024","unstructured":"Sliwiak J, Worsztynowicz P, Pokrywka K et al (2024) Biochemical characterization of L-asparaginase isoforms from Rhizobium etli\u2014the boosting effect of zinc. Front Chem. https:\/\/doi.org\/10.3389\/fchem.2024.1373312","journal-title":"Front Chem"},{"key":"4614_CR221","doi-asserted-by":"publisher","DOI":"10.1002\/adtp.202400156","volume":"7","author":"S Sonowal","year":"2024","unstructured":"Sonowal S, Pathak K, Das D et al (2024) L-asparaginase bio-betters: insight into current formulations, optimization strategies and future bioengineering frontiers in anti-cancer drug development. Adv Ther 7:2400156. https:\/\/doi.org\/10.1002\/adtp.202400156","journal-title":"Adv Ther"},{"key":"4614_CR222","doi-asserted-by":"publisher","first-page":"1765","DOI":"10.1007\/s10123-024-00493-y","volume":"27","author":"SS Sundaram","year":"2024","unstructured":"Sundaram SS, Kannan A, Chintaluri PG et al (2024) Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis. Int Microbiol 27:1765\u20131779. https:\/\/doi.org\/10.1007\/s10123-024-00493-y","journal-title":"Int Microbiol"},{"key":"4614_CR223","doi-asserted-by":"publisher","first-page":"503","DOI":"10.1080\/10826068.2023.2249100","volume":"54","author":"K Torres-Obreque","year":"2024","unstructured":"Torres-Obreque K, Kleingesinds EK, Santos JHPM (2024) PEGylation versus glycosylation: effect on the thermodynamics and thermostability of crisantaspase. Prep Biochem Biotechnol 54:503\u2013513. https:\/\/doi.org\/10.1080\/10826068.2023.2249100","journal-title":"Prep Biochem Biotechnol"},{"key":"4614_CR224","doi-asserted-by":"publisher","DOI":"10.1007\/s12032-023-02014-9","volume":"40","author":"M Tosta P\u00e9rez","year":"2023","unstructured":"Tosta P\u00e9rez M, Herrera Bel\u00e9n L, Letelier P et al (2023) L-asparaginase as the gold standard in the treatment of acute lymphoblastic leukemia: a comprehensive review. Med Oncol 40:150. https:\/\/doi.org\/10.1007\/s12032-023-02014-9","journal-title":"Med Oncol"},{"key":"4614_CR225","doi-asserted-by":"publisher","unstructured":"Tripathy RK, Anakha J, Pande AH (2024) Towards development of biobetter: L-asparaginase a case study. Biochim Biophys Acta Gen Subj 1868:130499. https:\/\/doi.org\/10.1016\/j.bbagen.2023.130499","DOI":"10.1016\/j.bbagen.2023.130499"},{"key":"4614_CR226","doi-asserted-by":"publisher","DOI":"10.1002\/app.43421","author":"A Ulu","year":"2016","unstructured":"Ulu A, Koytepe S, Ates B (2016) Synthesis and characterization of PMMA composites activated with starch for immobilization of L-asparaginase. J Appl Polym Sci. https:\/\/doi.org\/10.1002\/app.43421","journal-title":"J Appl Polym Sci"},{"key":"4614_CR227","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1080\/10731190701460358","volume":"35","author":"N Verma","year":"2007","unstructured":"Verma N, Kumar K, Kaur G, Anand S (2007) E. coli K-12 asparaginase-based asparagine biosensor for leukemia. Artif Cells Blood Substit Biotechnol 35:449\u2013456. https:\/\/doi.org\/10.1080\/10731190701460358","journal-title":"Artif Cells Blood Substit Biotechnol"},{"key":"4614_CR228","first-page":"809","volume":"3","author":"N Verma","year":"2012","unstructured":"Verma N, Bansal M, Kumar S (2012) Whole cell based miniaturized fiber optic biosensor to monitor L-asparagine. Adv Appl Sci Res 3:809\u2013814","journal-title":"Adv Appl Sci Res"},{"key":"4614_CR229","doi-asserted-by":"publisher","first-page":"1219","DOI":"10.1016\/j.bbapap.2014.03.013","volume":"1844","author":"S Verma","year":"2014","unstructured":"Verma S, Mehta RK, Maiti P et al (2014) Improvement of stability and enzymatic activity by site-directed mutagenesis of E. coli asparaginase II. Biochimica et Biophysica Acta (BBA) 1844:1219\u20131230. https:\/\/doi.org\/10.1016\/j.bbapap.2014.03.013","journal-title":"Biochimica et Biophysica Acta (BBA)"},{"key":"4614_CR230","doi-asserted-by":"publisher","DOI":"10.3390\/pharmaceutics13111965","volume":"13","author":"F Villanueva-Flores","year":"2021","unstructured":"Villanueva-Flores F, Z\u00e1rate-Romero A, Torres AG, Huerta-Saquero A (2021) Encapsulation of asparaginase as a promising strategy to improve in vivo drug performance. Pharmaceutics 13:1965. https:\/\/doi.org\/10.3390\/pharmaceutics13111965","journal-title":"Pharmaceutics"},{"key":"4614_CR231","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1080\/02648725.2017.1357294","volume":"33","author":"A Vimal","year":"2017","unstructured":"Vimal A, Kumar A (2017) Biotechnological production and practical application of L-asparaginase enzyme. Biotechnol Genet Eng Rev 33:40\u201361. https:\/\/doi.org\/10.1080\/02648725.2017.1357294","journal-title":"Biotechnol Genet Eng Rev"},{"key":"4614_CR232","doi-asserted-by":"publisher","DOI":"10.1007\/s10989-021-10312-x","volume":"28","author":"A Vimal","year":"2021","unstructured":"Vimal A, Kumar A (2021) L-asparaginase: need for an expedition from an enzymatic molecule to antimicrobial drug. Int J Pept Res Ther 28:9. https:\/\/doi.org\/10.1007\/s10989-021-10312-x","journal-title":"Int J Pept Res Ther"},{"key":"4614_CR233","doi-asserted-by":"publisher","DOI":"10.1007\/s00284-022-03095-x","volume":"79","author":"A Vimal","year":"2022","unstructured":"Vimal A, Kumar A (2022) Optimized production of medically significant enzyme L-asparaginase under submerged and solid-state fermentation from agricultural wastes. Curr Microbiol 79:394. https:\/\/doi.org\/10.1007\/s00284-022-03095-x","journal-title":"Curr Microbiol"},{"key":"4614_CR234","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1007\/s00280-017-3492-5","volume":"81","author":"S V\u00f6ller","year":"2018","unstructured":"V\u00f6ller S, Pichlmeier U, Zens A, Hempel G (2018) Pharmacokinetics of recombinant asparaginase in children with acute lymphoblastic leukemia. Cancer Chemother Pharmacol 81:305\u2013314. https:\/\/doi.org\/10.1007\/s00280-017-3492-5","journal-title":"Cancer Chemother Pharmacol"},{"key":"4614_CR235","doi-asserted-by":"publisher","first-page":"975","DOI":"10.1016\/j.ijbiomac.2021.07.107","volume":"186","author":"Y Wang","year":"2021","unstructured":"Wang Y, Xu W, Wu H et al (2021) Microbial production, molecular modification, and practical application of L-asparaginase: a review. Int J Biol Macromol 186:975\u2013983. https:\/\/doi.org\/10.1016\/j.ijbiomac.2021.07.107","journal-title":"Int J Biol Macromol"},{"key":"4614_CR236","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1016\/j.procbio.2019.03.009","volume":"81","author":"SR Wlodarczyk","year":"2019","unstructured":"Wlodarczyk SR, Costa-Silva TA, Pessoa-Jr A et al (2019) Effect of osmolytes on the activity of anti-cancer enzyme L-asparaginase II from Erwinia chrysanthemi. Process Biochem 81:123\u2013131. https:\/\/doi.org\/10.1016\/j.procbio.2019.03.009","journal-title":"Process Biochem"},{"key":"4614_CR237","doi-asserted-by":"publisher","DOI":"10.1016\/j.mimet.2021.106358","volume":"191","author":"LS Yap","year":"2021","unstructured":"Yap LS, Lee WL, Ting ASY (2021) Optimization of L-asparaginase production from endophytic Fusarium proliferatum using OFAT and RSM and its cytotoxic evaluation. J Microbiol Methods 191:106358. https:\/\/doi.org\/10.1016\/j.mimet.2021.106358","journal-title":"J Microbiol Methods"},{"key":"4614_CR238","doi-asserted-by":"publisher","first-page":"4751","DOI":"10.1007\/s11033-019-04921-5","volume":"46","author":"M Yari","year":"2019","unstructured":"Yari M, Eslami M, Ghoshoon MB et al (2019) Decreasing the immunogenicity of Erwinia chrysanthemi asparaginase via protein engineering: computational approach. Mol Biol Rep 46:4751\u20134761. https:\/\/doi.org\/10.1007\/s11033-019-04921-5","journal-title":"Mol Biol Rep"},{"key":"4614_CR239","doi-asserted-by":"publisher","DOI":"10.1016\/j.bej.2023.108806","volume":"191","author":"B Yilmazer Aktar","year":"2023","unstructured":"Yilmazer Aktar B, Georgakis N, Labrou N (2023) Comparative structural and kinetic study for development of a novel candidate L-asparaginase based pharmaceutical. Biochem Eng J 191:108806. https:\/\/doi.org\/10.1016\/j.bej.2023.108806","journal-title":"Biochem Eng J"},{"key":"4614_CR240","doi-asserted-by":"publisher","first-page":"415","DOI":"10.1016\/j.lwt.2019.04.050","volume":"109","author":"S Yim","year":"2019","unstructured":"Yim S, Kim M (2019) Purification and characterization of thermostable L-asparaginase from Bacillus amyloliquefaciens MKSE in Korean soybean paste. LWT 109:415\u2013421. https:\/\/doi.org\/10.1016\/j.lwt.2019.04.050","journal-title":"LWT"},{"key":"4614_CR241","doi-asserted-by":"publisher","DOI":"10.3390\/fermentation8050218","volume":"8","author":"B Yuan","year":"2022","unstructured":"Yuan B, Ma P, Fan Y et al (2022) Construction of L-asparaginase stable mutation for the application in food acrylamide mitigation. Fermentation 8:218. https:\/\/doi.org\/10.3390\/fermentation8050218","journal-title":"Fermentation"},{"key":"4614_CR242","doi-asserted-by":"publisher","DOI":"10.3390\/biology10121346","volume":"10","author":"X Zhang","year":"2021","unstructured":"Zhang X, Wang Z, Wang Y et al (2021) Heterologous expression and rational design of L-asparaginase from Rhizomucor miehei to improve thermostability. Biology 10:1346. https:\/\/doi.org\/10.3390\/biology10121346","journal-title":"Biology"},{"key":"4614_CR243","doi-asserted-by":"publisher","DOI":"10.1016\/j.bcp.2023.115473","volume":"210","author":"Y Zhang","year":"2023","unstructured":"Zhang Y, Sultonova RD, You S-H (2023) The anticancer effect of PASylated calreticulin-targeting L-ASNase in solid tumor bearing mice with immunogenic cell death-inducing chemotherapy. Biochem Pharmacol 210:115473. https:\/\/doi.org\/10.1016\/j.bcp.2023.115473","journal-title":"Biochem Pharmacol"},{"key":"4614_CR244","doi-asserted-by":"publisher","DOI":"10.3390\/biom14060686","volume":"14","author":"L Zhang","year":"2024","unstructured":"Zhang L, Ding S, Tang X et al (2024a) The improved antineoplastic activity of thermophilic L-asparaginase Tli10209 via site-directed mutagenesis. Biomolecules 14:686. https:\/\/doi.org\/10.3390\/biom14060686","journal-title":"Biomolecules"},{"key":"4614_CR245","doi-asserted-by":"publisher","first-page":"3387","DOI":"10.1007\/s12010-023-04715-3","volume":"196","author":"W Zhang","year":"2024","unstructured":"Zhang W, Dai Q, Huang Z, Xu W (2024b) Identification and thermostability modification of the mesophilic L-asparaginase from Limosilactobacillus secaliphilus. Appl Biochem Biotechnol 196:3387\u20133401. https:\/\/doi.org\/10.1007\/s12010-023-04715-3","journal-title":"Appl Biochem Biotechnol"},{"key":"4614_CR246","doi-asserted-by":"publisher","DOI":"10.1016\/j.biomaterials.2024.122740","volume":"312","author":"S Zhang","year":"2025","unstructured":"Zhang S, Gong L, Sun Y et al (2025) An ultra-long-acting L-asparaginase synergizes with an immune checkpoint inhibitor in starvation-immunotherapy of metastatic solid tumors. Biomaterials 312:122740. https:\/\/doi.org\/10.1016\/j.biomaterials.2024.122740","journal-title":"Biomaterials"},{"key":"4614_CR247","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2023.128690","volume":"257","author":"Y Zhou","year":"2024","unstructured":"Zhou Y, Shen J, Chi H (2024) Rational engineering and insight for a L-glutaminase activity reduced type II L-asparaginase from Bacillus licheniformis and its antileukemic activity in vitro. Int J Biol Macromol 257:128690. https:\/\/doi.org\/10.1016\/j.ijbiomac.2023.128690","journal-title":"Int J Biol Macromol"},{"key":"4614_CR248","doi-asserted-by":"publisher","first-page":"841","DOI":"10.1007\/s00792-015-0763-0","volume":"19","author":"S Zuo","year":"2015","unstructured":"Zuo S, Zhang T, Jiang B, Mu W (2015a) Reduction of acrylamide level through blanching with treatment by an extremely thermostable L-asparaginase during French fries processing. Extremophiles 19:841\u2013851. https:\/\/doi.org\/10.1007\/s00792-015-0763-0","journal-title":"Extremophiles"},{"key":"4614_CR249","doi-asserted-by":"publisher","first-page":"1069","DOI":"10.1007\/s00253-014-6271-9","volume":"99","author":"S Zuo","year":"2015","unstructured":"Zuo S, Zhang T, Jiang B, Mu W (2015b) Recent research progress on microbial L-asparaginases. Appl Microbiol Biotechnol 99:1069\u20131079. https:\/\/doi.org\/10.1007\/s00253-014-6271-9","journal-title":"Appl Microbiol Biotechnol"}],"container-title":["World Journal of Microbiology and Biotechnology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11274-025-04614-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11274-025-04614-1\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11274-025-04614-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,11,26]],"date-time":"2025-11-26T18:07:23Z","timestamp":1764180443000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11274-025-04614-1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,10]]},"references-count":249,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2025,10]]}},"alternative-id":["4614"],"URL":"https:\/\/doi.org\/10.1007\/s11274-025-04614-1","relation":{},"ISSN":["0959-3993","1573-0972"],"issn-type":[{"value":"0959-3993","type":"print"},{"value":"1573-0972","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,10]]},"assertion":[{"value":"19 August 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"24 September 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"16 October 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}},{"value":"During the preparation of this work, the authors used Co-pilot, developed by Microsoft and Grammarly, in order to improve the readability and language of the manuscript. After using this tool\/service, the authors reviewed and edited the content as needed and take full responsibility for the content of the published article.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declaration of generative AI and AI-assisted technologies in the writing process"}}],"article-number":"389"}}