{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T18:22:02Z","timestamp":1793298122616,"version":"4.5.0"},"reference-count":37,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,1,13]],"date-time":"2024-01-13T00:00:00Z","timestamp":1705104000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2024,1,13]],"date-time":"2024-01-13T00:00:00Z","timestamp":1705104000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"name":"Hochschule Offenburg"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Appl Microbiol Biotechnol"],"published-print":{"date-parts":[[2024,12]]},"abstract":"<jats:sec>\n            <jats:title>Abstract<\/jats:title>\n            <jats:p>A novel peptidyl-lys metalloendopeptidase (<jats:italic>Tc<\/jats:italic>-LysN) from <jats:italic>Tramates coccinea<\/jats:italic> was recombinantly expressed in <jats:italic>Komagataella phaffii<\/jats:italic> using the native pro-protein sequence. The peptidase was secreted into the culture broth as zymogen (~38 kDa) and mature enzyme (~19.8 kDa) simultaneously. The mature <jats:italic>Tc<\/jats:italic>-LysN was purified to homogeneity with a single step anion-exchange chromatography at pH 7.2. N-terminal sequencing using TMTpro Zero and mass spectrometry of the mature <jats:italic>Tc-<\/jats:italic>LysN indicated that the pro-peptide was cleaved between the amino acid positions 184 and 185 at the Kex2 cleavage site present in the native pro-protein sequence. The pH optimum of <jats:italic>Tc<\/jats:italic>-LysN was determined to be 5.0 while it maintained \u226560% activity between pH values 4.5\u20147.5 and \u226530% activity between pH values 8.5\u201410.0, indicating its broad applicability. The temperature maximum of <jats:italic>Tc<\/jats:italic>-LysN was determined to be 60 \u00b0C. After 18 h of incubation at 80 \u00b0C, <jats:italic>Tc<\/jats:italic>-LysN still retained ~20% activity. Organic solvents such as methanol and acetonitrile, at concentrations as high as 40% (v\/v), were found to enhance <jats:italic>Tc<\/jats:italic>-LysN\u2019s activity up to ~100% and ~50%, respectively. <jats:italic>Tc<\/jats:italic>-LysN\u2019s thermostability, ability to withstand up to 8 M urea, tolerance to high concentrations of organic solvents, and an acidic pH optimum make it a viable candidate to be employed in proteomics workflows in which alkaline conditions might pose a challenge. The nano-LC-MS\/MS analysis revealed bovine serum albumin (BSA)\u2019s sequence coverage of 84% using <jats:italic>Tc<\/jats:italic>-LysN which was comparable to the sequence coverage of 90% by trypsin peptides.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Key points<\/jats:title>\n            <jats:p>\u2022<jats:italic>A novel LysN from Trametes coccinea (Tc-LysN) was expressed in Komagataella phaffii and purified to homogeneity<\/jats:italic>\n            <\/jats:p>\n            <jats:p>\u2022<jats:italic>Tc-LysN is thermostable, applicable over a broad pH range, and tolerates high concentrations of denaturants<\/jats:italic>\n            <\/jats:p>\n            <jats:p>\u2022<jats:italic>Tc-LysN was successfully applied for protein digestion and mass spectrometry fingerprinting<\/jats:italic>\n            <\/jats:p>\n          <\/jats:sec>","DOI":"10.1007\/s00253-023-12986-3","type":"journal-article","created":{"date-parts":[[2024,1,13]],"date-time":"2024-01-13T09:02:51Z","timestamp":1705136571000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["A novel, robust peptidyl-lys metalloendopeptidase from Trametes coccinea recombinantly expressed in Komagataella phaffii"],"prefix":"10.1007","volume":"108","author":[{"given":"Uzair","family":"Ahmed","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tobias","family":"Stadelmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Heid","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Berit","family":"W\u00fcrtz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jens","family":"Pfannstiel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katrin","family":"Ochsenreither","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5190-8233","authenticated-orcid":false,"given":"Thomas","family":"Eisele","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,1,13]]},"reference":[{"issue":"12","key":"12986_CR1","doi-asserted-by":"publisher","first-page":"5190","DOI":"10.1002\/JSFA.11871","volume":"102","author":"U Ahmed","year":"2022","unstructured":"Ahmed U, Pfannstiel J, Stressler T, Eisele T (2022) Purification and characterization of a fungal aspartic peptidase from Trichoderma reesei and its application for food and animal feed protein hydrolyses. J Sci Food Agric 102(12):5190\u20135199. https:\/\/doi.org\/10.1002\/JSFA.11871","journal-title":"J Sci Food Agric"},{"key":"12986_CR2","unstructured":"Barrett AJ, Rawlings ND, Woessner JF (2004) Handbook of proteolytic enzymes 2nd edition"},{"issue":"2","key":"12986_CR3","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1080\/10409238.2020.1742090","volume":"55","author":"L Boon","year":"2020","unstructured":"Boon L, Ugarte-Berzal E, Vandooren J, Opdenakker G (2020) Protease propeptide structures, mechanisms of activation, and functions. Crit Rev Biochem Mol Biol 55(2):111\u2013165. https:\/\/doi.org\/10.1080\/10409238.2020.1742090","journal-title":"Crit Rev Biochem Mol Biol"},{"issue":"1-2","key":"12986_CR4","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","volume":"72","author":"MM Bradford","year":"1976","unstructured":"Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72(1-2):248\u2013254. https:\/\/doi.org\/10.1016\/0003-2697(76)90527-3","journal-title":"Anal Biochem"},{"issue":"7","key":"12986_CR5","doi-asserted-by":"publisher","first-page":"497","DOI":"10.1016\/S0958-6946(03)00057-8","volume":"13","author":"P Degraeve","year":"2003","unstructured":"Degraeve P, Martial-Gros A (2003) Purification and partial characterisation of X-prolyl dipeptidyl aminopeptidase of Lactobacillus helveticus ITG LH1. Int Dairy J 13(7):497\u2013507. https:\/\/doi.org\/10.1016\/S0958-6946(03)00057-8","journal-title":"Int Dairy J"},{"issue":"3-4","key":"12986_CR6","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1515\/bmc.2010.025","volume":"1","author":"IV Demidyuk","year":"2010","unstructured":"Demidyuk IV, Shubin AV, Gasanov EV, Kostrov SV (2010) Propeptides as modulators of functional activity of proteases. Biomol Concepts 1(3-4):305\u2013322. https:\/\/doi.org\/10.1515\/bmc.2010.025","journal-title":"Biomol Concepts"},{"issue":"8","key":"12986_CR7","doi-asserted-by":"publisher","first-page":"1063","DOI":"10.1016\/S0969-2126(02)00810-9","volume":"10","author":"WT Desmarais","year":"2002","unstructured":"Desmarais WT, Bienvenue DL, Bzymek KP, Holz RC, Petsko GA, Ringe D (2002) The 1.20 \u00c5 resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with Tris: a tale of buffer inhibition. Structure 10(8):1063\u20131072. https:\/\/doi.org\/10.1016\/S0969-2126(02)00810-9","journal-title":"Structure"},{"issue":"11","key":"12986_CR8","doi-asserted-by":"publisher","first-page":"2074","DOI":"10.1271\/bbb.59.2074","volume":"59","author":"N Dohmae","year":"1995","unstructured":"Dohmae N, Hayashi K, Miki K, Tsumuraya Y, Hashimoto Y (1995) Purification and characterization of intracellular proteinases in Pleurotus ostreatus fruiting bodies. Biotechnol Biochem 59(11):2074\u20132080. https:\/\/doi.org\/10.1271\/bbb.59.2074","journal-title":"Biotechnol Biochem"},{"key":"12986_CR9","doi-asserted-by":"publisher","unstructured":"Engler C, Kandzia R, Marillonnet S (2008) A one pot, one step, precision cloning method with high throughput capability. PLoS One 3(11). https:\/\/doi.org\/10.1371\/JOURNAL.PONE.0003647","DOI":"10.1371\/JOURNAL.PONE.0003647"},{"issue":"2","key":"12986_CR10","doi-asserted-by":"publisher","first-page":"523","DOI":"10.1111\/j.1432-1033.1979.tb12921.x","volume":"94","author":"BE Fischer","year":"1979","unstructured":"Fischer BE, Haring UK, Tribolet R, Sigel H (1979) Metal ion\/buffer interactions: Stability of binary and ternary complexes containing 2-amino-2(Hydroxymethyl)-~l, 3-propanediol (Tris) and adenosine 5\u2019-triphosphate (ATP). Eur J Biochem 94(2):523\u2013530. https:\/\/doi.org\/10.1111\/j.1432-1033.1979.tb12921.x","journal-title":"Eur J Biochem"},{"key":"12986_CR11","doi-asserted-by":"publisher","unstructured":"Fuller RS, Sterne RE, Thorner J. Enzymes required for yeast prohormone processing Vol 50.; 1988. https:\/\/doi.org\/10.1146\/annurev.ph.50.030188.002021","DOI":"10.1146\/annurev.ph.50.030188.002021"},{"issue":"1","key":"12986_CR12","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1038\/nmeth.3177","volume":"12","author":"PF Huesgen","year":"2014","unstructured":"Huesgen PF, Lange PF, Rogers LD, Solis N, Eckhard U, Kleifeld O, Goulas T, Gomis-R\u00fcth FX, Overall CM (2014) LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification. Nat Methods 12(1):55\u201358. https:\/\/doi.org\/10.1038\/nmeth.3177","journal-title":"Nat Methods"},{"key":"12986_CR13","doi-asserted-by":"publisher","first-page":"573","DOI":"10.1007\/BF00152446","volume":"9","author":"SL Iversen","year":"1995","unstructured":"Iversen SL, J\u00f8rgensen MH (1995) Azocasein assay for alkaline protease in complex fermentation broth. Biotechnol Tech 9:573\u2013576. https:\/\/doi.org\/10.1007\/BF00152446","journal-title":"Biotechnol Tech"},{"key":"12986_CR14","doi-asserted-by":"publisher","unstructured":"Kaushik N, Rohila D, Arora U, Raut R, Lamminm\u00e4ki U, Khanna N, Batra G (2016) Casamino acids facilitate the secretion of recombinant dengue virus serotype-3 envelope domain III in Pichia pastoris. BMC Biotechnol Published online. https:\/\/doi.org\/10.1186\/s12896-016-0243-3","DOI":"10.1186\/s12896-016-0243-3"},{"issue":"20","key":"12986_CR15","doi-asserted-by":"publisher","first-page":"5383","DOI":"10.1021\/ac025747h","volume":"74","author":"A Keller","year":"2002","unstructured":"Keller A, Nesvizhskii AI, Kolker E, Aebersold R (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS\/MS and database search. Anal Chem 74(20):5383\u20135392. https:\/\/doi.org\/10.1021\/ac025747h","journal-title":"Anal Chem"},{"issue":"3","key":"12986_CR16","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1038\/nbt.1611","volume":"28","author":"O Kleifeld","year":"2010","unstructured":"Kleifeld O, Doucet A, Auf Dem Keller U, Prudova A, Schilling O, Kainthan RK, Starr AE, Foster LJ, Kizhakkedathu JN, Overall CM (2010) Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products. Nat Biotechnol 28(3):281\u2013288. https:\/\/doi.org\/10.1038\/nbt.1611","journal-title":"Nat Biotechnol"},{"issue":"5259","key":"12986_CR17","doi-asserted-by":"publisher","first-page":"680","DOI":"10.1038\/227680a0","volume":"227","author":"UK Laemmli","year":"1970","unstructured":"Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227(5259):680\u2013685. https:\/\/doi.org\/10.1038\/227680a0","journal-title":"Nature"},{"issue":"2","key":"12986_CR18","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1016\/0005-2744(78)90087-6","volume":"522","author":"WG Lewis","year":"1978","unstructured":"Lewis WG, Basford JM, Walton PL (1978) Specificity and inhibition studies of Armillaria mellea protease. BBA - Enzymol 522(2):551\u2013560. https:\/\/doi.org\/10.1016\/0005-2744(78)90087-6","journal-title":"BBA - Enzymol"},{"issue":"17","key":"12986_CR19","doi-asserted-by":"publisher","first-page":"4646","DOI":"10.1021\/ac0341261","volume":"75","author":"AI Nesvizhskii","year":"2003","unstructured":"Nesvizhskii AI, Keller A, Kolker E, Aebersold R (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 75(17):4646\u20134658. https:\/\/doi.org\/10.1021\/ac0341261","journal-title":"Anal Chem"},{"issue":"1","key":"12986_CR20","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1093\/oxfordjournals.jbchem.a022074","volume":"124","author":"T Nonaka","year":"1998","unstructured":"Nonaka T, Hashimoto Y, Takio K (1998) Kinetic characterization of lysine-specific metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus fruiting bodies 1. J Biochem 124(1):157\u2013162 Accessed July 3, 2022. https:\/\/academic.oup.com\/jb\/article\/124\/1\/157\/823188","journal-title":"J Biochem"},{"key":"12986_CR21","doi-asserted-by":"publisher","first-page":"1014","DOI":"10.1093\/jb\/118.5.1014","volume":"118","author":"T Nonaka","year":"1995","unstructured":"Nonaka T, Ishikawa H, Tsumuraya Y, Hashimoto Y, Dohmae N, Takio K (1995) Characterization of a thermostable lysine-specific metalloendopeptidase from the fruiting bodies of a Basidiomycete, Grifola frondosa. J Biochem 118:1014\u20131020 Accessed July 3, 2022. https:\/\/academic.oup.com\/jb\/article\/118\/5\/1014\/790066","journal-title":"J Biochem"},{"issue":"4","key":"12986_CR22","doi-asserted-by":"publisher","first-page":"461","DOI":"10.1093\/jb\/mvv115","volume":"159","author":"ASR \u00d8dum","year":"2016","unstructured":"\u00d8dum ASR, \u00d8stergaard S, N\u00f8rby I, Meldal M, Olesen K (2016) Heterologous expression of peptidyl-Lys metallopeptidase of Armillaria mellea and mutagenic analysis of the recombinant peptidase. J Biochem 159(4):461\u2013470. https:\/\/doi.org\/10.1093\/jb\/mvv115","journal-title":"J Biochem"},{"issue":"3","key":"12986_CR23","doi-asserted-by":"publisher","first-page":"452","DOI":"10.1002\/BIT.21919","volume":"101","author":"VT Pham","year":"2008","unstructured":"Pham VT, Ewing E, Kaplan H, Choma C, Hefford MA (2008) Glycation improves the thermostability of trypsin and chymotrypsin. Biotechnol Bioeng 101(3):452\u2013459. https:\/\/doi.org\/10.1002\/BIT.21919","journal-title":"Biotechnol Bioeng"},{"key":"12986_CR24","doi-asserted-by":"publisher","first-page":"8827","DOI":"10.1039\/c0cc02523b","volume":"46","author":"R Raijmakers","year":"2010","unstructured":"Raijmakers R, Neerincx P, Mohammed S, Heck AJR (2010) Cleavage specificities of the brother and sister proteases Lys-C and Lys-Nw. Chem Commun 46:8827. https:\/\/doi.org\/10.1039\/c0cc02523b","journal-title":"Chem Commun"},{"issue":"3","key":"12986_CR25","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1021\/ac026117i","volume":"75","author":"J Rappsilber","year":"2003","unstructured":"Rappsilber J, Ishihama Y, Mann M (2003) Stop and Go Extraction tips for matrix-assisted laser desorption\/ionization, nanoelectrospray, and LC\/MS sample pretreatment in proteomics. Anal Chem 75(3):663\u2013670. https:\/\/doi.org\/10.1021\/ac026117i","journal-title":"Anal Chem"},{"issue":"5","key":"12986_CR26","doi-asserted-by":"publisher","first-page":"287","DOI":"10.2323\/jgam.48.287","volume":"48","author":"T Saito","year":"2002","unstructured":"Saito T, Dohmae N, Tsujimoto M, Takio K (2002) PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys metalloendopeptidase precursor of Grifola frondosa. J Gen Appl Microbiol 48(5):287\u2013292. https:\/\/doi.org\/10.2323\/jgam.48.287","journal-title":"J Gen Appl Microbiol"},{"issue":"4362","key":"12986_CR27","doi-asserted-by":"publisher","first-page":"1025","DOI":"10.1038\/1711025a0","volume":"171","author":"F Sanger","year":"1953","unstructured":"Sanger F (1953) A Disulphide Interchange Reaction. Nature 171(4362):1025\u20131026. https:\/\/doi.org\/10.1038\/1711025a0","journal-title":"Nature"},{"issue":"5","key":"12986_CR28","doi-asserted-by":"publisher","first-page":"850","DOI":"10.1021\/ac950914h","volume":"68","author":"A Shevchenko","year":"1996","unstructured":"Shevchenko A, Wilm M, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68(5):850\u2013858. https:\/\/doi.org\/10.1021\/ac950914h","journal-title":"Anal Chem"},{"issue":"4","key":"12986_CR29","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1016\/J.BCAB.2014.08.002","volume":"3","author":"T Stressler","year":"2014","unstructured":"Stressler T, Eisele T, Kleinthom\u00e4 AK, Meyer S, Fischer L (2014) Partial purification and characterization of Lys-N from Grifola frondosa using a novel, specific assay. Biocatal Agric Biotechnol 3(4):275\u2013281. https:\/\/doi.org\/10.1016\/J.BCAB.2014.08.002","journal-title":"Biocatal Agric Biotechnol"},{"issue":"26","key":"12986_CR30","doi-asserted-by":"publisher","first-page":"17920","DOI":"10.1074\/jbc.M600907200","volume":"281","author":"C Tallant","year":"2006","unstructured":"Tallant C, Garc\u00eda-Castellanos R, Seco J, Baumann U, Gomis-R\u00fcth FX (2006) Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases*. J Biol Chem 281(26):17920\u201317928. https:\/\/doi.org\/10.1074\/jbc.M600907200","journal-title":"J Biol Chem"},{"key":"12986_CR31","doi-asserted-by":"publisher","unstructured":"Taouatas N, Drugan MM, Heck AJR, Mohammed S. Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase. Published online 2008. https:\/\/doi.org\/10.1038\/NMETH.1204","DOI":"10.1038\/NMETH.1204"},{"issue":"8","key":"12986_CR32","doi-asserted-by":"publisher","first-page":"4282","DOI":"10.1021\/pr100341e","volume":"9","author":"N Taouatas","year":"2010","unstructured":"Taouatas N, Heck AJR, Mohammed S (2010) Evaluation of metalloendopeptidase Lys-N protease performance under different sample handling conditions. J Proteome Res 9(8):4282\u20134288. https:\/\/doi.org\/10.1021\/pr100341e","journal-title":"J Proteome Res"},{"key":"12986_CR33","doi-asserted-by":"publisher","unstructured":"Tsai PL, Chen S-F, Huang SY (2013) Mass spectrometry-based strategies for protein disulfide bond identification. Rev Anal Chem 32(4). https:\/\/doi.org\/10.1515\/revac-2013-0011","DOI":"10.1515\/revac-2013-0011"},{"issue":"14","key":"12986_CR34","doi-asserted-by":"publisher","first-page":"2612","DOI":"10.1111\/febs.13287","volume":"282","author":"L Tsiatsiani","year":"2015","unstructured":"Tsiatsiani L, Heck AJR (2015) Proteomics beyond trypsin. FEBS J 282(14):2612\u20132626. https:\/\/doi.org\/10.1111\/febs.13287","journal-title":"FEBS J"},{"issue":"2","key":"12986_CR35","doi-asserted-by":"publisher","first-page":"940","DOI":"10.1128\/JB.112.2.940-949.1972","volume":"112","author":"M Wingard","year":"1972","unstructured":"Wingard M, Matsueda G, Wolfe RS (1972) Myxobacter AL-1 protease II: specific peptide bond cleavage on the amino side of lysine. J Bacteriol 112(2):940\u2013949. https:\/\/doi.org\/10.1128\/JB.112.2.940-949.1972","journal-title":"J Bacteriol"},{"key":"12986_CR36","doi-asserted-by":"publisher","unstructured":"Wis JR, Zougman A, Nagaraj N, Mann M. Universal sample preparation method for proteome analysis. Published online 2009. https:\/\/doi.org\/10.1038\/NMETH.1322","DOI":"10.1038\/NMETH.1322"},{"key":"12986_CR37","doi-asserted-by":"publisher","unstructured":"Zhao M, Hao B, Li H, Cai M, Xie J, Liu H, Tan M, Zhai L, Yu Q (2020) Peptidyl-Lys metalloendopeptidase (Lys-N) purified from dry fruit of Grifola frondosa demonstrates \u201cmirror\u201d digestion property with lysyl endopeptidase (Lys-C). Rapid Commun Mass Spectrom 34(2). https:\/\/doi.org\/10.1002\/RCM.8573","DOI":"10.1002\/RCM.8573"}],"container-title":["Applied Microbiology and Biotechnology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00253-023-12986-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00253-023-12986-3\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00253-023-12986-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,5,27]],"date-time":"2025-05-27T20:41:30Z","timestamp":1748378490000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00253-023-12986-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,1,13]]},"references-count":37,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2024,12]]}},"alternative-id":["12986"],"URL":"https:\/\/doi.org\/10.1007\/s00253-023-12986-3","relation":{},"ISSN":["0175-7598","1432-0614"],"issn-type":[{"value":"0175-7598","type":"print"},{"value":"1432-0614","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,1,13]]},"assertion":[{"value":"23 August 2023","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 December 2023","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"24 December 2023","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"13 January 2024","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"This article does not contain any studies with human participants or animals performed by any of the authors.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical approval"}},{"value":"The authors declare no competing interests.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}],"article-number":"103"}}