{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,17]],"date-time":"2026-07-17T04:17:59Z","timestamp":1784261879555,"version":"3.55.0"},"reference-count":51,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,10,1]],"date-time":"2024-10-01T00:00:00Z","timestamp":1727740800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,10,1]],"date-time":"2024-10-01T00:00:00Z","timestamp":1727740800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,10,1]],"date-time":"2024-10-01T00:00:00Z","timestamp":1727740800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,10,1]],"date-time":"2024-10-01T00:00:00Z","timestamp":1727740800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,10,1]],"date-time":"2024-10-01T00:00:00Z","timestamp":1727740800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,10,1]],"date-time":"2024-10-01T00:00:00Z","timestamp":1727740800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,10,1]],"date-time":"2024-10-01T00:00:00Z","timestamp":1727740800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100022241","name":"Office of Research, Innovation and Commercialization, University of Agriculture Faisalabad","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100022241","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2024,10]]},"DOI":"10.1016\/j.bioorg.2024.107658","type":"journal-article","created":{"date-parts":[[2024,7,20]],"date-time":"2024-07-20T14:58:50Z","timestamp":1721487530000},"page":"107658","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"special_numbering":"C","title":["Auto-induction, biochemical characterization and application of a novel thermo-alkaline and detergent-stable lipase (S9 peptidase domain) from Thermotoga petrophila as cleaning additive and degrading oil\/fat wastes"],"prefix":"10.1016","volume":"151","author":[{"given":"Fatima","family":"Akram","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taseer","family":"Fatima","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ikram","family":"ul Haq","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"11","key":"10.1016\/j.bioorg.2024.107658_b0005","doi-asserted-by":"crossref","first-page":"597","DOI":"10.3390\/cryst9110597","article-title":"Carboxylic ester hydrolases in bacteria: active site, structure, function and application","volume":"9","author":"Oh","year":"2019","journal-title":"Cryst."},{"issue":"11","key":"10.1016\/j.bioorg.2024.107658_b0010","doi-asserted-by":"crossref","first-page":"1942","DOI":"10.1002\/pro.3016","article-title":"Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures","volume":"25","author":"Chen","year":"2016","journal-title":"Prot. Sci."},{"issue":"2","key":"10.1016\/j.bioorg.2024.107658_b0015","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1002\/jctb.6745","article-title":"Insights into polyester plastic biodegradation by carboxyl ester hydrolases","volume":"97","author":"Gricajeva","year":"2021","journal-title":"J. Chem. Technol. Biotechnol."},{"key":"10.1016\/j.bioorg.2024.107658_b0020","series-title":"Assessing and utilizing esterase specificity in antimicrobial prodrug development","first-page":"199","author":"Hetrick","year":"2022"},{"issue":"23","key":"10.1016\/j.bioorg.2024.107658_b0025","doi-asserted-by":"crossref","first-page":"15394","DOI":"10.3390\/ijms232315394","article-title":"Cold-Active Lipases and Esterases: A review on recombinant overexpression and other essential issues","volume":"23","author":"Matinja","year":"2022","journal-title":"Int. J. Mol. Sci."},{"issue":"12","key":"10.1016\/j.bioorg.2024.107658_b0030","doi-asserted-by":"crossref","first-page":"13579","DOI":"10.3390\/ijms160613579","article-title":"Cloning, expression and characterization of a thermostable esterase HydS14 from Actinomadura sp. Strain S14 in Pichia pastoris","volume":"16","author":"Sriyapai","year":"2015","journal-title":"Int. J. Mol. Sci."},{"issue":"2","key":"10.1016\/j.bioorg.2024.107658_b0035","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1128\/AEM.03640-13","article-title":"The secreted esterase of Propionibacterium freudenreichii has a major role in cheese lipolysis","volume":"80","author":"Mukdsi","year":"2014","journal-title":"Appl. Environ. Microbiol."},{"issue":"4","key":"10.1016\/j.bioorg.2024.107658_b0040","first-page":"521","article-title":"An appraisal on prominent industrial and biotechnological applications of bacterial lipases","volume":"65","author":"Akram","year":"2023","journal-title":"Mol. Biotechnol."},{"issue":"3","key":"10.1016\/j.bioorg.2024.107658_b0045","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.3390\/ijms23031262","article-title":"Evaluation of the impact of esterases and lipases from the circulatory system against substrates of different lipophilicity","volume":"23","author":"Lam","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bioorg.2024.107658_b0050","doi-asserted-by":"crossref","DOI":"10.1016\/j.jclepro.2019.117925","article-title":"Recent trends in hyperthermophilic enzymes production and future perspectives for biofuel industry: A critical review","volume":"238","author":"Ebaid","year":"2019","journal-title":"J. Clean. Prod."},{"issue":"9","key":"10.1016\/j.bioorg.2024.107658_b0055","first-page":"034","article-title":"Lipolytic activity of Itb1. 1 and Lk3 thermostable lipases expressed in Escherichia coli and Pichia pastoris","volume":"12","author":"Simatupang","year":"2022","journal-title":"J. Appl Pharm. Sci."},{"key":"10.1016\/j.bioorg.2024.107658_b0060","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.pep.2018.05.008","article-title":"Auto-induction for high level production of biologically active reteplase in Escherichia coli","volume":"151","author":"Fathi-Roudsari","year":"2018","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.bioorg.2024.107658_b0065","doi-asserted-by":"crossref","first-page":"7251","DOI":"10.1007\/s11033-012-1555-6","article-title":"Kinetic and thermodynamic study of cloned thermostable endo-1,4-\u03b2-xylanase from Thermotoga petrophila in mesophilic host","volume":"39","author":"Haq","year":"2012","journal-title":"Mol. Biol. Rep."},{"key":"10.1016\/j.bioorg.2024.107658_b0070","doi-asserted-by":"crossref","first-page":"1132","DOI":"10.1016\/j.ijbiomac.2018.11.189","article-title":"Enhanced production, overexpression and characterization of a hyperthermophilic multimodular GH family 2 \u03b2-glucuronidase (TpGUS) cloned from Thermotoga petrophila RKU-1T in a mesophilic host","volume":"123","author":"Haq","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"issue":"1\u20132","key":"10.1016\/j.bioorg.2024.107658_b0075","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of Protein-Dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bioorg.2024.107658_b0080","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.pep.2005.01.016","article-title":"Protein production by auto-induction in high-density shaking cultures","volume":"41","author":"Studier","year":"2005","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.bioorg.2024.107658_b0085","doi-asserted-by":"crossref","first-page":"1482","DOI":"10.1007\/s12010-015-1659-2","article-title":"Expression and Characterization of a Novel Thermo-Alkalistable Lipase from Hyperthermophilic Bacterium Thermotoga maritima","volume":"176","author":"Tian","year":"2015","journal-title":"Appl. Biochem. Biotechnol."},{"key":"10.1016\/j.bioorg.2024.107658_b0090","doi-asserted-by":"crossref","first-page":"400","DOI":"10.2174\/157341112801264879","article-title":"Analytical methods for lipases activity determination: A review","volume":"8","author":"Stoytcheva","year":"2012","journal-title":"Curr. Anal. Chem."},{"issue":"8","key":"10.1016\/j.bioorg.2024.107658_b0095","doi-asserted-by":"crossref","first-page":"e0273368","DOI":"10.1371\/journal.pone.0273368","article-title":"Optimization and characterization of alkaliphilic lipase from a novel Bacillus cereus NC7401 strain isolated from diesel fuel polluted soil","volume":"17","author":"Akhter","year":"2022","journal-title":"PLoS One"},{"issue":"1","key":"10.1016\/j.bioorg.2024.107658_b0100","doi-asserted-by":"crossref","first-page":"19670","DOI":"10.1038\/s41598-021-98927-4","article-title":"Application and characterization of crude fungal lipases used to degrade fat and oil wastes","volume":"11","author":"Alabdalall","year":"2021","journal-title":"Sci. Rep."},{"issue":"16","key":"10.1016\/j.bioorg.2024.107658_b0105","doi-asserted-by":"crossref","first-page":"9367","DOI":"10.3390\/ijms23169367","article-title":"Identification of a novel lipase with AHSMG pentapeptide in hypocreales and glomerellales filamentous fungi","volume":"23","author":"Guti\u00e9rrez-Dom\u00ednguez","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bioorg.2024.107658_b0110","article-title":"Characterization of a novel esterase EST33 from an Antarctic bacterium: a representative of a new esterase family","volume":"13","author":"Liu","year":"2022","journal-title":"Front. Microbial."},{"key":"10.1016\/j.bioorg.2024.107658_b0115","doi-asserted-by":"crossref","DOI":"10.1016\/j.ab.2020.113741","article-title":"Overexpression and characterization of TnCel12B, a hyperthermophilic GH12 endo-1,4-\u03b2-glucanase cloned from Thermotoga naphthophila RKU-10T","volume":"599","author":"Akram","year":"2020","journal-title":"Anal. Biochem."},{"issue":"2","key":"10.1016\/j.bioorg.2024.107658_b0120","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.bbrc.2016.05.061","article-title":"Crystal structure of Thermotoga maritima acetyl esterase complex with a substrate analog: Insights into the distinctive substrate specificity in the CE7 carbohydrate esterase family","volume":"476","author":"Singh","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"1","key":"10.1016\/j.bioorg.2024.107658_b0125","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.bbrc.2018.11.105","article-title":"X-ray structure and characterization of a thermostable lipase from Geobacillus thermoleovorans","volume":"508","author":"Moharana","year":"2019","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"2","key":"10.1016\/j.bioorg.2024.107658_b0130","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1007\/s12010-020-03329-3","article-title":"Cloning, characterization, and structural modeling of an extremophilic bacterial lipase isolated from saline habitats of the thar desert","volume":"192","author":"Verma","year":"2020","journal-title":"Appl. Biochem. Biotechnol."},{"key":"10.1016\/j.bioorg.2024.107658_b0135","doi-asserted-by":"crossref","first-page":"483","DOI":"10.4014\/jmb.2012.12036","article-title":"Identification and characterization of a novel thermostable GDSL-type lipase from Geobacillus thermocatenulatus","volume":"31","author":"Jo","year":"2021","journal-title":"J. Microbiol. Biotechnol."},{"issue":"4","key":"10.1016\/j.bioorg.2024.107658_b0140","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1016\/j.jksus.2017.12.018","article-title":"Optimization and production of lipase enzyme from bacterial strains isolated from petrol spilled soil","volume":"31","author":"Bharathi","year":"2019","journal-title":"J. King. Saud. Univ. Sci."},{"key":"10.1016\/j.bioorg.2024.107658_b0145","doi-asserted-by":"crossref","first-page":"2590","DOI":"10.3390\/microorganisms9122590","article-title":"Investigation of lipolytic-secreting bacteria from an artificially polluted soil using a modified culture method and optimization of their lipase production","volume":"9","author":"Pham","year":"2021","journal-title":"Microorganisms"},{"issue":"10","key":"10.1016\/j.bioorg.2024.107658_b0150","doi-asserted-by":"crossref","first-page":"1180","DOI":"10.2174\/0929866528666210805120715","article-title":"Boosting auto-induction of recombinant proteins in Escherichia coli with glucose and lactose additives","volume":"28","author":"Tahara","year":"2021","journal-title":"Protein Pept. Lett."},{"issue":"11","key":"10.1016\/j.bioorg.2024.107658_b0155","doi-asserted-by":"crossref","first-page":"3925","DOI":"10.3390\/ijms21113925","article-title":"Functional heterologous expression of mature lipase LipA from Pseudomonas aeruginosa PSA01 in Escherichia coli SHuffle and BL21 (DE3): effect of the expression host on thermal stability and solvent tolerance of the enzyme produced","volume":"21","author":"Pulido","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bioorg.2024.107658_b0160","doi-asserted-by":"crossref","DOI":"10.1002\/jsde.12731","article-title":"Heterologous expression and characterization of a novel thermostable and alkali stable recombinant lipase enzyme from Bacillus thuringensis into E. coli BL21(DE3) for detergent formulation","author":"Zafar","year":"2024","journal-title":"J. Surfactant Deterg."},{"key":"10.1016\/j.bioorg.2024.107658_b0165","doi-asserted-by":"crossref","DOI":"10.3389\/fbioe.2021.630551","article-title":"Challenges associated with the formation of recombinant protein inclusion bodies in Escherichia coli and Strategies to address them for industrial applications","volume":"9","author":"Bhatwa","year":"2021","journal-title":"Front. Bioeng. Biotechnol."},{"issue":"2","key":"10.1016\/j.bioorg.2024.107658_b0170","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1038\/s41428-020-00411-9","article-title":"IPTG-independent auto-induction of extracellular matrix proteins using recombinant E. coli as the expression host","volume":"53","author":"Kataoka","year":"2020","journal-title":"Polym. J."},{"issue":"1","key":"10.1016\/j.bioorg.2024.107658_b0175","doi-asserted-by":"crossref","DOI":"10.1093\/jimb\/kuad034","article-title":"Mechanistic aspects of IPTG (isopropylthio-\u03b2-galactoside) transport across the cytoplasmic membrane of Escherichia coli \u2013 a rate limiting step in the induction of recombinant protein expression","volume":"50","author":"Simas","year":"2023","journal-title":"J. Ind. Microbiol. Biotechnol."},{"issue":"8","key":"10.1016\/j.bioorg.2024.107658_b0180","doi-asserted-by":"crossref","DOI":"10.1002\/biot.202100143","article-title":"Supplementation of critical amino acids improves glycerol and lactose uptake and enhances recombinant protein production in Escherichia coli","volume":"16","author":"Kumar","year":"2021","journal-title":"Biotechnol. J."},{"issue":"1","key":"10.1016\/j.bioorg.2024.107658_b0185","doi-asserted-by":"crossref","DOI":"10.1186\/s13568-018-0711-3","article-title":"Expression optimization of recombinant cholesterol oxidase in Escherichia coli and its purification and characterization","volume":"8","author":"Fazaeli","year":"2018","journal-title":"AMB Express"},{"issue":"1","key":"10.1016\/j.bioorg.2024.107658_b0190","doi-asserted-by":"crossref","DOI":"10.1088\/1755-1315\/1255\/1\/012050","article-title":"Autoinduction expression of Bst DNA polymerase using lac operon-controlled expression systems in Escherichia coli","volume":"1255","author":"Laksmi","year":"2023","journal-title":"IOP. Conf. Ser. Earth. Environ. Sci."},{"issue":"1","key":"10.1016\/j.bioorg.2024.107658_b0195","first-page":"1","article-title":"Impact of glycerol as carbon source onto specific sugar and inducer uptake rates and inclusion body productivity in E. coli BL21 (DE3)","volume":"5","author":"Kopp","year":"2017","journal-title":"Bioeng."},{"key":"10.1016\/j.bioorg.2024.107658_b0200","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.ijbiomac.2021.01.214","article-title":"Characterization of a novel lipase from Bacillus licheniformis NCU CS-5 for applications in detergent industry and biodegradation of 2,4-D butyl ester","volume":"176","author":"Zhao","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"issue":"1","key":"10.1016\/j.bioorg.2024.107658_b0205","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1007\/s11802-021-4506-9","article-title":"Identification and characterization of a novel alkali- and high temperature-tolerant lipase (Lip4346) from a macroalgae-associated bacterial strain","volume":"20","author":"Gu","year":"2021","journal-title":"J. Ocean Univ. China"},{"key":"10.1016\/j.bioorg.2024.107658_b0210","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.cocis.2016.04.004","article-title":"Not only pH. Specific buffer effects in biological systems","volume":"23","author":"Salis","year":"2016","journal-title":"Curr. Opin. Colloid Interface Sci."},{"issue":"22","key":"10.1016\/j.bioorg.2024.107658_b0215","doi-asserted-by":"crossref","first-page":"7386","DOI":"10.1039\/D1CY01486B","article-title":"Preparation and characterization of a novel thermostable lipase from Thermomicrobiumroseum","volume":"11","author":"Fang","year":"2021","journal-title":"Cat. Sci. Technol."},{"key":"10.1016\/j.bioorg.2024.107658_b0220","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1080\/14756366.2020.1861607","article-title":"Production, purification and biochemical characterisation of a novel lipase from a newly identified lipolytic bacterium Staphylococcus caprae NCU S6","volume":"36","author":"Zhao","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"3","key":"10.1016\/j.bioorg.2024.107658_b0225","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.bcab.2013.03.009","article-title":"Production, characterization and applications of organic solvent tolerant lipase by Pseudomonas aeruginosa AAU2","volume":"2","author":"Bose","year":"2013","journal-title":"Biocatal. Agric. Biotechnol."},{"issue":"2","key":"10.1016\/j.bioorg.2024.107658_b0230","first-page":"119","article-title":"The role of metals in enzyme activity","volume":"7","author":"Riordan","year":"1977","journal-title":"Ann. Clin. Lab. Sci."},{"issue":"3","key":"10.1016\/j.bioorg.2024.107658_b0235","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1080\/13102818.2018.1446764","article-title":"Purification and characterization of alkaline lipase production by Pseudomonas aeruginosa HFE733 and application for biodegradation in food wastewater treatment","volume":"32","author":"Hu","year":"2018","journal-title":"Biotechnol. Biotechnol. Equip."},{"key":"10.1016\/j.bioorg.2024.107658_b0240","doi-asserted-by":"crossref","DOI":"10.1016\/j.ab.2019.113554","article-title":"Recombinant cold-adapted halotolerant, organic solvent-stable esterase (estHIJ) from Bacillus halodurans","volume":"591","author":"Noby","year":"2020","journal-title":"Anal. Biochem."},{"issue":"5","key":"10.1016\/j.bioorg.2024.107658_b0245","doi-asserted-by":"crossref","first-page":"e0286091","DOI":"10.1371\/journal.pone.0286091","article-title":"Biochemical characterization of an alkaline and detergent-stable Lipase from Fusarium annulatum Bugnicourt strain CBS associated with olive tree dieback","volume":"18","author":"Dab","year":"2023","journal-title":"PLoS One"},{"issue":"18","key":"10.1016\/j.bioorg.2024.107658_b0250","doi-asserted-by":"crossref","first-page":"13768","DOI":"10.3390\/ijms241813768","article-title":"Enhancing the hydrolytic activity of a lipase towards larger triglycerides through lid domain engineering","volume":"24","author":"Fern\u00e1ndez-L\u00f3pez","year":"2023","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/j.bioorg.2024.107658_b0255","doi-asserted-by":"crossref","DOI":"10.1186\/s12896-023-00818-1","article-title":"Preparation, purification, and biochemical of fat-degrading bacterial enzymes from pig carcass compost and its application","volume":"23","author":"Duan","year":"2023","journal-title":"BMC Biotechnol."}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206824005637?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206824005637?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,18]],"date-time":"2026-06-18T00:38:41Z","timestamp":1781743121000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0045206824005637"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,10]]},"references-count":51,"alternative-id":["S0045206824005637"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2024.107658","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2024,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Auto-induction, biochemical characterization and application of a novel thermo-alkaline and detergent-stable lipase (S9 peptidase domain) from Thermotoga petrophila as cleaning additive and degrading oil\/fat wastes","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2024.107658","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"107658"}}