{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T11:49:56Z","timestamp":1791892196624,"version":"4.3.4"},"reference-count":124,"publisher":"Public Library of Science (PLoS)","issue":"12","license":[{"start":{"date-parts":[[2024,12,17]],"date-time":"2024-12-17T00:00:00Z","timestamp":1734393600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002385","name":"Ministry of Higher Education","doi-asserted-by":"publisher","award":["FRGS\/1\/2023\/STG02\/USM\/02\/7"],"award-info":[{"award-number":["FRGS\/1\/2023\/STG02\/USM\/02\/7"]}],"id":[{"id":"10.13039\/501100002385","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"abstract":"<jats:p>This study focuses on a novel lipase from <jats:italic>Bacillus licheniformis<\/jats:italic> IBRL-CHS2. The lipase gene was cloned into the pGEM-T Easy vector, and its sequences were registered in GenBank (KU984433 and AOT80658). It was identified as a member of the bacterial lipase subfamily 1.4. The pCold I vector and <jats:italic>E<\/jats:italic>. <jats:italic>coli<\/jats:italic> BL21 (DE3) host were utilized for expression, with the best results obtained by removing the enzyme\u2019s signal peptide. Optimal conditions were found to be 15\u00b0C for 24 h, using 0.2 mM Isopropyl \u03b2-D-1-thiogalactopyranoside (IPTG). The His-tagged lipase was purified 13-fold with a 68% recovery and a specific activity of 331.3 U\/mg using affinity purification. The lipase demonstrated optimal activity at 35\u00b0C and pH 7. It remained stable after 24 h in 25% (v\/v) organic solvents such as isooctane, n-hexane, dimethyl sulfoxide (DMSO), and methanol, which enhanced its activity. Chloroform and diethyl ether inhibited the lipase. The enzyme exhibited the highest affinity for <jats:italic>p<\/jats:italic>-nitrophenol laurate (C12:0) with a K<jats:sub>m<\/jats:sub> of 0.36 mM and a V<jats:sub>max<\/jats:sub> of 357 \u03bcmol min<jats:sup>-1<\/jats:sup> mg<jats:sup>-1<\/jats:sup>. Among natural oils, it performed best with coconut oil and worst with olive oil. The lipase was stable in the presence of 1 mM and 5 mM Ca<jats:sup>2<\/jats:sup>\u207a, K\u207a, Na\u207a, Mg<jats:sup>2<\/jats:sup>\u207a, and Ba<jats:sup>2<\/jats:sup>\u207a, but its activity decreased with Zn<jats:sup>2<\/jats:sup>\u207a and Al<jats:sup>3<\/jats:sup>\u207a. Non-ionic surfactants like Triton X-100, Nonidet P40, Tween 20, and Tween 40 boosted activity, while Sodium Dodecyl Sulfate (SDS) inhibited it. This lipase\u2019s unique properties, particularly its stability in organic solvents, make it suitable for applications in organic synthesis and various industries.<\/jats:p>","DOI":"10.1371\/journal.pone.0314556","type":"journal-article","created":{"date-parts":[[2024,12,17]],"date-time":"2024-12-17T18:34:01Z","timestamp":1734460441000},"page":"e0314556","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":4,"title":["Characterization of a novel subfamily 1.4 lipase from Bacillus licheniformis IBRL-CHS2: Cloning and expression optimization"],"prefix":"10.1371","volume":"19","author":[{"ORCID":"https:\/\/orcid.org\/0009-0003-1854-4575","authenticated-orcid":true,"given":"Ammar","family":"Khazaal Kadhim Almansoori","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nidyaletchmy Subba","family":"Reddy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mustafa","family":"Abdulfattah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah Solehah","family":"Ismail","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8945-4428","authenticated-orcid":true,"given":"Rashidah","family":"Abdul Rahim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2024,12,17]]},"reference":[{"issue":"2","key":"pone.0314556.ref001","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1007\/s12155-021-10333-w","article-title":"Biodiesel Production Using Homogeneous, Heterogeneous, and Enzyme Catalysts via Transesterification and Esterification Reactions: a Critical Review","volume":"15","author":"V. Mandari","year":"2021","journal-title":"BioEnergy Res."},{"key":"pone.0314556.ref002","doi-asserted-by":"crossref","first-page":"110502","DOI":"10.1016\/j.msec.2019.110502","article-title":"Magnetic dextrin nanobiomaterial: An organic-inorganic hybrid catalyst for the synthesis of biologically active polyhydroquinoline derivatives by asymmetric Hantzsch reaction","volume":"109","author":"A. Maleki","year":"2020","journal-title":"Mater. Sci. Eng. C"},{"issue":"1","key":"pone.0314556.ref003","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1186\/s12870-020-02823-4","article-title":"Lipases of germinating jojoba seeds efficiently hydrolyze triacylglycerols and wax esters and display wax ester-synthesizing activity","volume":"21","author":"A. Kawi\u0144ski","year":"2021","journal-title":"BMC Plant Biol."},{"issue":"1","key":"pone.0314556.ref004","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1021\/acs.jafc.0c07430","article-title":"Integral Stereoselectivity of Lipase Based on the Chromatographic Resolution of Enantiomeric\/Regioisomeric Diacylglycerols","volume":"69","author":"Y. Choi","year":"2021","journal-title":"J. Agric. Food Chem."},{"key":"pone.0314556.ref005","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/B978-0-12-819813-1.00006-2","article-title":"The lipases and their applications with emphasis on food industry","author":"A. Mehta","year":"2021","journal-title":"In Microbial Biotechnology in Food and Health"},{"issue":"9","key":"pone.0314556.ref006","first-page":"1032","article-title":"Advances in Recombinant Lipases: Production, Engineering, Immobilization and Application in the Pharmaceutical Industry.","volume":"10","author":"F. J. Contesini","year":"2020","journal-title":"Catal"},{"issue":"4","key":"pone.0314556.ref007","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1504\/IJBRA.2011.043770","article-title":"LIPABASE: A database for \u2018true\u2019 lipase family enzymes.","volume":"7","author":"A. Messaoudi","year":"2011","journal-title":"Int J Bioinform Res Appl"},{"issue":"1","key":"pone.0314556.ref008","first-page":"8","article-title":"Bacillus pumilus su\u015fundan elde edilen yeni termostabil lipaz\u0131n biyokimyasal karakterizasyonu","volume":"40","author":"F. Laachari","year":"2015","journal-title":"Turk. J. Biochem."},{"key":"pone.0314556.ref009","article-title":"Sequence identification and in silico characterization of novel thermophilic lipases from Geobacillus species","author":"Y. S\u00fcrmeli","year":"2023","journal-title":"Biotechnol. Appl. Biochem."},{"issue":"15","key":"pone.0314556.ref010","doi-asserted-by":"crossref","first-page":"3430","DOI":"10.3390\/molecules25153430","article-title":"Ion-Pair Interaction and Hydrogen Bonds as Main Features of Protein Thermostability in Mutated T1 Recombinant Lipase Originating from Geobacillus zalihae","volume":"25","author":"S. N. H. Ishak","year":"2020","journal-title":"Molecules"},{"issue":"3","key":"pone.0314556.ref011","doi-asserted-by":"crossref","first-page":"e0149851","DOI":"10.1371\/journal.pone.0149851","article-title":"Analysis of comparative sequence and genomic data to verify phylogenetic relationship and explore a new subfamily of bacterial lipases","volume":"11","author":"M. Masomian","year":"2016","journal-title":"PLoS ONE"},{"key":"pone.0314556.ref012","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1007\/s11274-009-0213-1","article-title":"Cloning, expression and biochemical characterization of a thermostable lipase from G. stearothermophilus JC","volume":"26","author":"Y. Jiang","year":"2010","journal-title":"World J. Microbiol. Biotechnol."},{"issue":"7","key":"pone.0314556.ref013","doi-asserted-by":"crossref","first-page":"e0130289","DOI":"10.1371\/journal.pone.0130289","article-title":"Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilis","volume":"10","author":"P. C. Rathi","year":"2015","journal-title":"PLOS ONE"},{"issue":"16","key":"pone.0314556.ref014","doi-asserted-by":"crossref","first-page":"3919","DOI":"10.1021\/acs.jpcb.4c00405","article-title":"Hydrophobic Clusters Regulate Surface Hydration Dynamics of Bacillus subtilis Lipase A","volume":"128","author":"A. M. Jaufer","year":"2024","journal-title":"J. Phys. Chem. B"},{"issue":"23","key":"pone.0314556.ref015","first-page":"7545","article-title":"Lipase A from Bacillus subtilis: Substrate Binding, Conformational Dynamics, and Signatures of a Lid. J. Chem. Inf. Model.","volume":"63","author":"S. Behera","year":"2023","journal-title":"JCIM"},{"issue":"11","key":"pone.0314556.ref016","doi-asserted-by":"crossref","first-page":"4253","DOI":"10.1007\/s00253-019-09717-y","article-title":"Current knowledge on enzymatic PET degradation and its possible application to waste stream management and other fields","volume":"103","author":"F. Kawai","year":"2019","journal-title":"Appl. Microbiol. Biotechnol."},{"issue":"1","key":"pone.0314556.ref017","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1186\/s13068-020-01696-x","article-title":"Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus.","volume":"13","author":"L. T. H. L. Le","year":"2020","journal-title":"Biotechnol. Biofuels"},{"key":"pone.0314556.ref018","first-page":"118","article-title":"Overexpression, Purification and Characterization of Organic Solvent Stable Lipase from Bacillus licheniformis RSP-09","volume":"17","author":"B. Madan","year":"2009","journal-title":"J. Mol. Microbiol. Biotechnol."},{"key":"pone.0314556.ref019","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1016\/S0141-0229(01)00316-7","article-title":"Over-expression and properties of a purified recombinant Bacillus licheniformis lipase: a comparative report on Bacillus lipases","volume":"28","author":"M. B. Nthangeni","year":"2001","journal-title":"Enzyme Microb. Technol."},{"issue":"10","key":"pone.0314556.ref020","doi-asserted-by":"crossref","first-page":"R77","DOI":"10.1186\/gb-2004-5-10-r77","article-title":"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species","volume":"5","author":"M. Rey","year":"2004","journal-title":"Genome Biol."},{"issue":"10","key":"pone.0314556.ref021","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1007\/s12275-014-4217-7","article-title":"Surface display expression of Bacillus licheniformis lipase in Escherichia coli using Lpp\u2019OmpA chimera","volume":"52","author":"J. Jo","year":"2014","journal-title":"J. Microbiol."},{"issue":"Supp. 1","key":"pone.0314556.ref022","doi-asserted-by":"crossref","first-page":"145","DOI":"10.21315\/tlsr2016.27.3.20","article-title":"Cloning and Expression of a Subfamily 1.4 Lipase from Bacillus licheniformis IBRL-CHS2","volume":"27","author":"N. N. S. Reddy","year":"2016","journal-title":"Trop Life Sci Res"},{"key":"pone.0314556.ref023","unstructured":"Noor Mazuin, A. B., Darah, I., & Rashidah, A. R. (2009). Identification of lipase producing Bacillus licheniformis isolated from volcanic area of Cangar, Surabaya, Indonesia. Proc. 2nd Universiti Sains Malaysia-Universitas Airlangga Collaborative Conference, Surabaya, Indonesia, Pp: 111."},{"key":"pone.0314556.ref024","first-page":"283","author":"J. Doyle","year":"1991"},{"issue":"1\u20132","key":"pone.0314556.ref025","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":"M. M. Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"pone.0314556.ref026","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/2191-0855-3-22","article-title":"Densitometry based microassay for the determination of lipase depolymerizing activity on polyhydroxyalkanoate","volume":"3","author":"D. H. Ch\u2019ng","year":"2013","journal-title":"AMB Express"},{"key":"pone.0314556.ref027","doi-asserted-by":"crossref","first-page":"1693","DOI":"10.1007\/s11274-010-0347-1","article-title":"A unique thermostable and organic solvent tolerant lipase from newly isolated Aneurinibacillus thermoaerophilus strain HZ: Physical factor studies","volume":"26","author":"M. Masomian","year":"2010","journal-title":"World J. Microbiol. Biotechnol."},{"key":"pone.0314556.ref028","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1007\/BF02676129","article-title":"A simple and rapid colorimetric method for determination of free fatty acids for lipase assay","volume":"63","author":"D. Y. Kwon","year":"1986","journal-title":"J. Am. Oil Chem. Soc."},{"key":"pone.0314556.ref029","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.ab.2005.03.006","article-title":"High yield purification of an organic solvent-tolerant lipase from Pseudomonas sp. strain S5","volume":"341","author":"R. N. Z. R. A. Rahman","year":"2005","journal-title":"Anal. Biochem."},{"issue":"4","key":"pone.0314556.ref030","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1590\/S1517-83822006000400019","article-title":"Characterization of alkaline lipase from Fusarium oxysporum and the effect of different surfactants and detergents on the enzyme activity","volume":"37","author":"J. N. Prazeres","year":"2006","journal-title":"Braz. J. Microbiol."},{"key":"pone.0314556.ref031","doi-asserted-by":"crossref","first-page":"6459","DOI":"10.1046\/j.1432-1327.2000.01736.x","article-title":"A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase","volume":"267","author":"T. Eggert","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"pone.0314556.ref032","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molcatb.2010.09.002","article-title":"Catalytic properties and potential applications of Bacillus lipases","volume":"68","author":"M. Guncheva","year":"2011","journal-title":"J. Mol. Catal. B Enzym."},{"key":"pone.0314556.ref033","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1007\/s10482-014-0274-5","article-title":"Functional expression of a novel alkaline-adapted lipase of Bacillus amyloliquefaciens from stinky tofu brine and development of immobilized enzyme for biodiesel production","volume":"106","author":"X. Cai","year":"2014","journal-title":"Antonie van Leeuwenhoek"},{"key":"pone.0314556.ref034","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1016\/S0958-1669(02)00341-5","article-title":"Lipases for biotechnology","volume":"13","author":"K. E. Jaeger","year":"2002","journal-title":"Curr. Opin. Biotechnol."},{"key":"pone.0314556.ref035","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.ijbiomac.2016.07.015","article-title":"Lipase of Bacillus stratosphericus L1: Cloning, expression and characterization","volume":"92","author":"A. Gricajeva","year":"2016","journal-title":"Int. J. Biol. Macromol."},{"key":"pone.0314556.ref036","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1007\/s10930-013-9502-5","article-title":"Strategies for the production of recombinant protein in Escherichia coli","volume":"32","author":"G. J. Gopal","year":"2013","journal-title":"Protein J."},{"issue":"2","key":"pone.0314556.ref037","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.pep.2005.01.006","article-title":"Secretory expression of thermostable T1 lipase through bacteriocin release protein","volume":"40","author":"R. N. Z. R. A. Rahman","year":"2005","journal-title":"Protein Expr. Purif"},{"key":"pone.0314556.ref038","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1007\/s00792-007-0069-y","article-title":"A thermoalkaliphilic lipase of Geobacillus sp. T1","volume":"11","author":"T. C. Leow","year":"2007","journal-title":"Extremophiles"},{"key":"pone.0314556.ref039","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1271\/bbb.64.280","article-title":"Thermostable lipase of Bacillus stearothermophilus: High level production, purification and calcium-dependent thermostability","volume":"64","author":"M. H. Kim","year":"2000","journal-title":"Biosci. Biotechnol. Biochem."},{"issue":"13","key":"pone.0314556.ref040","doi-asserted-by":"crossref","first-page":"6972","DOI":"10.1016\/j.biortech.2011.03.083","article-title":"High level expression and characterization of a novel thermostable, organic solvent tolerant, 1,3-regioselective lipase from Geobacillus sp. strain ARM","volume":"102","author":"A. Ebrahimpour","year":"2011","journal-title":"Bioresour. Technol."},{"key":"pone.0314556.ref041","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1007\/s12010-011-9309-9","article-title":"Co-expression of an organic solvent-tolerant lipase and its cognate foldase of Pseudomonas aeruginosa cs-2 and the application of the immobilized recombinant lipase","volume":"165","author":"R. Peng","year":"2011","journal-title":"Appl. Biochem. Biotechnol."},{"key":"pone.0314556.ref042","doi-asserted-by":"crossref","first-page":"2387","DOI":"10.1007\/s12010-010-9011-3","article-title":"Significantly improved expression and biochemical properties of recombinant Serratia marcescens lipase as robust biocatalyst for kinetic resolution of chiral ester","volume":"162","author":"Y. Wang","year":"2010","journal-title":"Appl. Biochem. Biotechnol."},{"issue":"11","key":"pone.0314556.ref043","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1016\/j.procbio.2013.08.016","article-title":"Molecular cloning of a thermo-alkaliphilic lipase from Bacillus subtilis DR8806: Expression and biochemical characterization","volume":"48","author":"S. Emtenani","year":"2013","journal-title":"Process Biochem."},{"issue":"4","key":"pone.0314556.ref044","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.1590\/S1517-838246420141068","article-title":"Gene cloning, expression and characterization of the Bacillus amyloliquefaciens PS35 lipase","volume":"46","author":"P. Kanmani","year":"2015","journal-title":"Braz. J. Microbiol."},{"key":"pone.0314556.ref045","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.pep.2005.06.004","article-title":"Overexpression and characterization of a lipase from Bacillus subtilis","volume":"45","author":"J. Ma","year":"2006","journal-title":"Protein Expr. Purif."},{"key":"pone.0314556.ref046","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/S0014-5793(01)02665-5","article-title":"Lipolytic enzymes LipA and LipB from Bacillus subtilis in regulation of gene expression, biochemical properties, and three-dimensional structure","volume":"502","author":"T. Eggert","year":"2001","journal-title":"FEBS Lett."},{"key":"pone.0314556.ref047","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S1388-1981(02)00214-7","article-title":"Expression and characterization of Ca2+ -independent lipase from Bacillus pumilus B26","volume":"1583","author":"H. K. Kim","year":"2002","journal-title":"Biochim. Biophys. Acta"},{"issue":"21","key":"pone.0314556.ref048","doi-asserted-by":"crossref","first-page":"5245","DOI":"10.3390\/ijms20215245","article-title":"Disulfide Engineered Lipase to Enhance the Catalytic Activity: A Structure-Based Approach on BTL2.","volume":"20","author":"C. A. Godoy","year":"2019","journal-title":"Int. J. Mol. Sci."},{"issue":"5","key":"pone.0314556.ref049","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.biotechadv.2008.05.003","article-title":"Cold active microbial lipases: Some hot issues and recent developments","volume":"26","author":"B. Joseph","year":"2008","journal-title":"Biotechnol. Adv."},{"issue":"8","key":"pone.0314556.ref050","doi-asserted-by":"crossref","first-page":"1912","DOI":"10.1016\/j.biotechadv.2015.11.001","article-title":"Some like it hot, some like it cold: Temperature dependent biotechnological applications and improvements in extremophilic enzymes","volume":"33","author":"K. S. Siddiqui","year":"2015","journal-title":"Biotechnol. Adv."},{"issue":"2","key":"pone.0314556.ref051","doi-asserted-by":"crossref","first-page":"259","DOI":"10.3390\/molecules25020259","article-title":"\u0394-FeOOH as Support for Immobilization Peroxidase: Optimization via a Chemometric Approach.","volume":"25","author":"T. S. Tavares","year":"2020","journal-title":"Mol.,"},{"issue":"1","key":"pone.0314556.ref052","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1186\/s12896-021-00686-7","article-title":"Optimization and scale-up of \u03b1-amylase production by Aspergillus oryzae using solid-state fermentation of edible oil cakes","volume":"21","author":"M. Balakrishnan","year":"2021","journal-title":"BMC Biotechnol."},{"issue":"1","key":"pone.0314556.ref053","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1186\/s43141-021-00144-z","article-title":"Optimization of extracellular ethanol-tolerant \u03b2-glucosidase production from a newly isolated Aspergillus sp. DHE7 via solid state fermentation using jojoba meal as substrate: purification and biochemical characterization for biofuel preparation","volume":"19","author":"D. H. El-Ghonemy","year":"2021","journal-title":"J. Genet. Eng. Biotechnol."},{"key":"pone.0314556.ref054","doi-asserted-by":"crossref","first-page":"27","DOI":"10.9734\/mrji\/2021\/v31i530318","article-title":"Lipolytic Activities of Bacteria and Fungi Isolated from Soil Samples","author":"R. O. Fashogbon","year":"2021","journal-title":"Microbiol. Res. J. Int."},{"issue":"2","key":"pone.0314556.ref055","doi-asserted-by":"crossref","first-page":"1","DOI":"10.54536\/ajlsi.v1i2.303","article-title":"Characterisation Studies on Lipases of Brevibacterium, Bacillus and Pseudomonas Spp Produced Under Sub-Merged Fermentation of Different Carbon Sources.","volume":"1","year":"2022","journal-title":"Am. J. Life Sci. Innov."},{"issue":"15","key":"pone.0314556.ref056","doi-asserted-by":"crossref","first-page":"9171","DOI":"10.1021\/acscatal.2c02881","article-title":"Unraveling Alcohol Dehydrogenase Catalysis in Organic\u2013Aqueous Biphasic Systems Combining Experiments and Molecular Dynamics Simulations.","volume":"12","author":"N. Zhang","year":"2022","journal-title":"ACS Catalysis"},{"issue":"8","key":"pone.0314556.ref057","doi-asserted-by":"crossref","first-page":"1756","DOI":"10.1002\/pro.5560060816","article-title":"Dimethyl sulfoxide binding to globular proteins: A nuclear magnetic relaxation dispersion study","volume":"6","author":"H. J\u00f3hannesson","year":"1997","journal-title":"Protein Sci."},{"key":"pone.0314556.ref058","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1111\/j.1432-1033.1993.tb18127.x","article-title":"Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme","volume":"216","author":"E. Lesuisse","year":"1993","journal-title":"Eur. J. Biochem."},{"key":"pone.0314556.ref059","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.molcatb.2016.06.003","article-title":"Organic solvent-tolerant, cold-adapted lipases PML and LipS exhibit increased conformational flexibility in polar organic solvents","volume":"131","author":"V. Dachuri","year":"2016","journal-title":"J. Mol. Catal. B Enzym."},{"issue":"1","key":"pone.0314556.ref060","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1186\/1754-6834-6-70","article-title":"Dieselzymes: development of a stable and methanol tolerant lipase for biodiesel production by directed evolution","volume":"6","author":"T. P. Korman","year":"2013","journal-title":"Biotechnol. Biofuels"},{"issue":"1","key":"pone.0314556.ref061","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1590\/S1517-83822011000100003","article-title":"Characterization of a novel lipase from Bacillus sp. isolated from tannery wastes","volume":"42","author":"M. I. Ghori","year":"2011","journal-title":"Braz. J. Microbiol."},{"issue":"3","key":"pone.0314556.ref062","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1007\/BF03175143","article-title":"Screening and identification of a novel organic solvent-stable lipase producer","volume":"59","author":"S. Liu","year":"2009","journal-title":"Ann. Microbiol."},{"issue":"6817","key":"pone.0314556.ref063","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1038\/35051719","article-title":"Improving enzymes by using them in organic solvents","volume":"409","author":"A. M. Klibanov","year":"2001","journal-title":"Nature"},{"key":"pone.0314556.ref064","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2014\/625258","article-title":"Organic Solvent Tolerant Lipases and Applications.","volume":"2014","author":"S. Sharma","year":"2014","journal-title":"Sci. World J."},{"issue":"37","key":"pone.0314556.ref065","doi-asserted-by":"crossref","first-page":"28434","DOI":"10.1074\/jbc.M110.136200","article-title":"Analysis of the conformational stability and activity of Candida antarctica lipase B in organic solvents. Insight from molecular dynamics and quantum mechanics\/simulations","volume":"285","author":"C. Li","year":"2010","journal-title":"J. Biol. Chem."},{"key":"pone.0314556.ref066","first-page":"2","article-title":"Up-to-date insight on industrial enzymes applications and global market.","volume":"S4","author":"B. Sarrouh","year":"2012","journal-title":"Bioprocessing & Biotech.,"},{"issue":"3","key":"pone.0314556.ref067","first-page":"308","article-title":"Bacillus subtilis Lipase A\u2014Lipase or Esterase?","volume":"10","author":"P. Bracco","year":"2020","journal-title":"Catal."},{"issue":"6","key":"pone.0314556.ref068","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1007\/s00894-020-04396-3","article-title":"Understanding thermal and organic solvent stability of thermoalkalophilic lipases: insights from computational predictions and experiments","volume":"26","author":"M. Shehata","year":"2020","journal-title":"J. Mol. Model."},{"issue":"2","key":"pone.0314556.ref069","doi-asserted-by":"crossref","first-page":"71","DOI":"10.14710\/reaktor.18.2.71-75","article-title":"Performance of Various Organic Solvents as Reaction Media in Plant Oil Lipolysis with Plant Lipase.","volume":"18","author":"A. N. Istyami","year":"2018","journal-title":"Reaktor"},{"issue":"1","key":"pone.0314556.ref070","doi-asserted-by":"crossref","first-page":"9754","DOI":"10.1038\/s41598-019-45118-x","article-title":"Enhancement of laccase activity by pre-incubation with organic solvents","volume":"9","author":"M.-H. Wu","year":"2019","journal-title":"Sci. Rep."},{"issue":"10","key":"pone.0314556.ref071","doi-asserted-by":"crossref","DOI":"10.1002\/biot.202300120","article-title":"Enhancing the organic solvent resistance of \u03c9\u2010amine transaminase for enantioselective synthesis of (R) \u2010(+)\u20101(1\u2010naphthyl)\u2010ethylamine.","volume":"18","author":"C. Wang","year":"2023","journal-title":"Biotechnol. J.,"},{"issue":"7","key":"pone.0314556.ref072","first-page":"761","article-title":"Different Effects of Salt Bridges near the Active Site of Cold-Adapted Proteus mirabilis Lipase on Thermal and Organic Solvent Stabilities","volume":"12","author":"V. Dachuri","year":"2022","journal-title":"Catal."},{"key":"pone.0314556.ref073","first-page":"3738","article-title":"Purification and characterization of organic solvent and detergent tolerant lipase from thermotolerant Bacillus sp","volume":"11","author":"P. Kanjanavas","year":"2010","journal-title":"RN2. Int. J. Mol. Sci."},{"key":"pone.0314556.ref074","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1016\/j.biotechadv.2010.05.012","article-title":"Biodiesel production with immobilized lipase: A review","volume":"28","author":"T. Tan","year":"2010","journal-title":"Biotechnol. Adv."},{"key":"pone.0314556.ref075","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/S0009-3084(98)00030-9","article-title":"Anatomy of lipase binding sites: the scissile fatty acid binding site","volume":"93","author":"J. Pleiss","year":"1998","journal-title":"Chem. Phys. Lipids"},{"key":"pone.0314556.ref076","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1007\/s00253-008-1656-2","article-title":"Cloning and characterization of a new cold-active lipase from a deep-sea sediment metagenome","volume":"8","author":"J. H. Jeon","year":"2009","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"pone.0314556.ref077","article-title":"Improvement of medium chain fatty acid content and antimicrobial activity of coconut oil via solid-state fermentation using a Malaysian Geotrichum candidum","author":"A. Khoramnia","year":"2013","journal-title":"BioMed Res. Int"},{"issue":"2","key":"pone.0314556.ref078","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1080\/15422119.2018.1564328","article-title":"Lipases: from production to applications","volume":"49","author":"N. B. Melani","year":"2020","journal-title":"Sep. Purif. Rev."},{"issue":"24","key":"pone.0314556.ref079","doi-asserted-by":"crossref","first-page":"6653","DOI":"10.1080\/10408398.2022.2038076","article-title":"Sources, purification, immobilization and industrial applications of microbial lipases: An overview","volume":"63","author":"C. P. Enespa","year":"2023","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"pone.0314556.ref080","doi-asserted-by":"crossref","first-page":"474","DOI":"10.3923\/jm.2008.474.481","article-title":"Enzymatic hydrolysis of palm oil mill effluent solid using mixed cellulases from locally isolated fungi","volume":"3","author":"W. K. Mun","year":"2008","journal-title":"Res. J. Microbiol."},{"issue":"4","key":"pone.0314556.ref081","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1016\/j.foodchem.2006.05.051","article-title":"Determination of free fatty acids in palm oil samples using non-aqueous flowinjection titrimetric method","volume":"102","author":"B. Saad","year":"2007","journal-title":"Food Chem."},{"issue":"8","key":"pone.0314556.ref082","doi-asserted-by":"crossref","first-page":"2143","DOI":"10.1007\/s13197-022-05499-w","article-title":"Triglycerides of medium-chain fatty acids: A concise review","volume":"60","author":"H. B. Jadhav","year":"2023","journal-title":"J. Food Sci. Technol."},{"issue":"5","key":"pone.0314556.ref083","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1002\/cben.202100050","article-title":"Antimicrobial properties of lauric acid and monolaurin in virgin coconut oil: a review","volume":"9","author":"F. O. Nitbani","year":"2022","journal-title":"ChemBioEng Rev."},{"issue":"2","key":"pone.0314556.ref084","first-page":"416","article-title":"Altering the Regioselectivity of T1 Lipase from Geobacillus zalihae toward sn-3 Acylglycerol Using a Rational Design Approach","volume":"13","author":"S. H. Albayati","year":"2023","journal-title":"Catal."},{"key":"pone.0314556.ref085","doi-asserted-by":"crossref","first-page":"130868","DOI":"10.1016\/j.foodchem.2021.130868","article-title":"Expression and characterization of a novel lipase from Bacillus licheniformis NCU CS-5 for application in enhancing fatty acids flavor release for low-fat cheeses","volume":"368","author":"J. Zhao","year":"2022","journal-title":"Food Chem."},{"issue":"3","key":"pone.0314556.ref086","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":"E. Jo","year":"2021","journal-title":"J. Microbiol. Biotechnol."},{"key":"pone.0314556.ref087","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1155\/2022\/6403090","article-title":"Purification and Optimization of Extracellular Lipase from a Novel Strain Kocuria flava Y4","volume":"2022","author":"A. Barik","year":"2022","journal-title":"Int J Anal. Chem."},{"key":"pone.0314556.ref088","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.gene.2015.10.006","article-title":"Disruption of N terminus long range non covalent interactions shifted temp.opt 25\u00b0C to cold: Evolution of point mutant Bacillus lipase by error prone PCR","volume":"576","author":"S. Goomber","year":"2016","journal-title":"Gene"},{"key":"pone.0314556.ref089","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.bej.2014.08.022","article-title":"Directed evolution of Bacillus licheniformis lipase for improvement of thermostability","volume":"91","author":"B. Madan","year":"2014","journal-title":"Biochem. Eng. J"},{"issue":"3","key":"pone.0314556.ref090","first-page":"22","article-title":"A comparative study on kinetics performances of BSA-gold nanozymes for nanozyme-mediated oxidation of 3, 3\u2019, 5, 5\u2019-Tetramethylbenzidine and 3, 3\u2019-Diaminobenzidine. Biochem.","volume":"9","author":"S. R. H. Jangi","year":"2023","journal-title":"Mol. Biol. J."},{"key":"pone.0314556.ref091","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/S0734-9750(01)00086-6","article-title":"Production, purification, characterization and application of lipases","volume":"19","author":"R. Sharma","year":"2001","journal-title":"Biotechnol. Adv."},{"key":"pone.0314556.ref092","first-page":"8","article-title":"Metal ions in biological systems.","volume":"16","author":"J. P. Glusker","year":"1999","journal-title":"Rigaku J.,"},{"issue":"5","key":"pone.0314556.ref093","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1016\/S0922-338X(97)86981-4","article-title":"Production and stabilization of a solvent-tolerant alkaline lipase from Pseudomonas pseudoalcaligenes F-111","volume":"82","author":"S. F. Lin","year":"1996","journal-title":"J. Ferment. Bioeng."},{"issue":"2","key":"pone.0314556.ref094","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/s10534-022-00373-w","article-title":"Regulation of zinc-dependent enzymes by metal carrier proteins","volume":"35","author":"M. W. Thompson","year":"2022","journal-title":"Biometals"},{"issue":"2","key":"pone.0314556.ref095","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.pep.2009.08.002","article-title":"Secretory expression and characterization of a highly Ca2+-activated thermostable L2 lipase","volume":"68","author":"S. Sabri","year":"2009","journal-title":"Protein Expr. Purif."},{"key":"pone.0314556.ref096","doi-asserted-by":"crossref","first-page":"109408","DOI":"10.1016\/j.enzmictec.2019.109408","article-title":"Self-assembly of lipase hybrid nanoflowers with bifunctional Ca2+ for improved activity and stability","volume":"132","author":"Y. Zhang","year":"2020","journal-title":"Enzyme Microb. Technol."},{"key":"pone.0314556.ref097","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S1381-1177(03)00045-6","article-title":"Purification and properties of thermostable lipase from a thermophilic Bacillus stearothermophilus MC 7","volume":"22","author":"M. Kambourova","year":"2003","journal-title":"J. Mol. Catal. B: Enzym."},{"issue":"6","key":"pone.0314556.ref098","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1080\/10408398.2021.1954873","article-title":"Role of calcium on lipid digestion and serum lipids: A review","volume":"63","author":"A.-I. Mulet-Cabero","year":"2023","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"pone.0314556.ref099","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":"J. Zhao","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"pone.0314556.ref100","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1007\/s40011-015-0612-z","article-title":"Purification and bio-chemical characterization of a solvent-tolerant and highly thermostable lipase of Bacillus licheniformis strain SCD11501","volume":"87","author":"S. Sharma","year":"2017","journal-title":"Proc. Natl. Acad. Sci. India Sect. B Biol. Sci."},{"issue":"4","key":"pone.0314556.ref101","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.foodchem.2008.01.026","article-title":"An extra-cellular alkaline metallolipase from Bacillus licheniformisMTCC 6824: Purification and biochemical characterization","volume":"109","author":"K. Chakraborty","year":"2008","journal-title":"Food Chem."},{"key":"pone.0314556.ref102","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1007\/s12010-009-8543-x","article-title":"Production and characterization of an alkaline thermostable crude lipase from an isolated strain of Bacillus cereus C7","volume":"159","author":"S. Dutta","year":"2009","journal-title":"Appl. Biochem. Biotechnol."},{"key":"pone.0314556.ref103","doi-asserted-by":"crossref","first-page":"2917","DOI":"10.3390\/ijms12052917","article-title":"A newly isolated thermostable lipase from Bacillus sp","volume":"12","author":"F. M. Shariff","year":"2011","journal-title":"Int. J. Mol. Sci."},{"key":"pone.0314556.ref104","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/j.nbt.2011.01.002","article-title":"Purification, characterization and thermal inactivation kinetics of a non-regioselective thermostable lipase from a genotypically identified extremophilic Bacillus subtilis NS 8","volume":"28","author":"A. T. Olusesan","year":"2011","journal-title":"New Biotechnol."},{"key":"pone.0314556.ref105","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1111\/j.1470-8744.1999.tb00778.x","article-title":"Purification and characterization of a Pseudomonas sp. lipase and its properties in non-aqueous media","volume":"30","author":"H. Dong","year":"1999","journal-title":"Biotechnol. Appl. Biochem."},{"key":"pone.0314556.ref106","doi-asserted-by":"crossref","first-page":"3461","DOI":"10.1016\/j.febslet.2005.05.016","article-title":"Zinc in lipase L1 from Geobacillus stearothermophilus L1 and structural implications on thermal stability","volume":"579","author":"W. C. Choi","year":"2005","journal-title":"FEBS Lett."},{"issue":"28","key":"pone.0314556.ref107","doi-asserted-by":"crossref","first-page":"33704","DOI":"10.1021\/acsami.1c08809","article-title":"Single-Molecule Study of Thermomyces lanuginosus Lipase in a Detergency Application System Reveals Diffusion Pattern Remodeling by Surfactants and Calcium","volume":"13","author":"M. E. Moses","year":"2021","journal-title":"ACS Appl. Mater. Interfaces"},{"issue":"16","key":"pone.0314556.ref108","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202218162","article-title":"Effector Regulated Catalytic Cyclization of Alkynoic Acids Using Pt 2 L 4 Cages","volume":"62","author":"E. O. Bobylev","year":"2023","journal-title":"Angew. Chem. Int. Ed."},{"issue":"3","key":"pone.0314556.ref109","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/0005-2760(92)90137-K","article-title":"Purification and properties of lipase from Penicillium simplicissimum","volume":"1124","author":"H. Sztajer","year":"1992","journal-title":"Biochim. Biophys. Acta (BBA)\u2014Lipids and Lipid Metabolism,"},{"issue":"61","key":"pone.0314556.ref110","first-page":"13174","article-title":"Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Bacillus cereus BF-3","volume":"10","author":"W. Gang","year":"2011","journal-title":"Afr. J. Biotechnol."},{"issue":"1","key":"pone.0314556.ref111","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1021\/acscatal.6b03222","article-title":"Dual-Surface Functionalization of Metal-Organic Frameworks for Enhancing the Catalytic Activity of Candida antarctica Lipase B","volume":"7","author":"S. Jung","year":"2017","journal-title":"Polar Organic Media. ACS Catal."},{"issue":"3","key":"pone.0314556.ref112","doi-asserted-by":"crossref","first-page":"1669","DOI":"10.1021\/acs.joc.1c01136","article-title":"Effect of Organic Solvents on the Structure and Activity of a Minimal Lipase","volume":"87","author":"K. N. Ingenbosch","year":"2022","journal-title":"J. Org. Chem."},{"issue":"3","key":"pone.0314556.ref113","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1007\/s12010-009-8841-3","article-title":"Purification and Characterization of an Organic Solvent-Tolerant Lipase from Pseudomonas aeruginosa CS-2","volume":"162","author":"R. Peng","year":"2010","journal-title":"Appl. Biochem. Biotechnol."},{"issue":"4","key":"pone.0314556.ref114","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1631\/jzus.B1800213","article-title":"Screening, purification, and characterization of an extracellular lipase from Aureobasidium pullulans isolated from stuffed buns steamers","volume":"20","author":"Y. Li","year":"2019","journal-title":"J. Zhejiang Univ. Sci"},{"issue":"7","key":"pone.0314556.ref115","doi-asserted-by":"crossref","first-page":"1800","DOI":"10.3390\/molecules23071800","article-title":"Purification and Characterization of Lipase Produced by Leuconostoc mesenteroides Subsp. mesenteroides ATCC 8293 Using an Aqueous Two-Phase System (ATPS) Composed of Triton X-100 and Maltitol","volume":"23","author":"N. H. E. Sukohidayat","year":"2018","journal-title":"Mol"},{"issue":"1","key":"pone.0314556.ref116","doi-asserted-by":"crossref","first-page":"15711","DOI":"10.1038\/s41598-017-16036-7","article-title":"Heterologous expression and characterization of a new lipase from Pseudomonas fluorescens Pf0\u20131 and used for biodiesel production","volume":"7","author":"W. Liu","year":"2017","journal-title":"Sci. Rep."},{"issue":"8","key":"pone.0314556.ref117","doi-asserted-by":"crossref","first-page":"4130","DOI":"10.1021\/la062804j","article-title":"Nonionic Surfactants: A Key to Enhance the Enzyme Activity at Cationic Reverse Micellar Interface.","volume":"23","author":"A. Shome","year":"2007","journal-title":"Langmuir"},{"issue":"5","key":"pone.0314556.ref118","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1021\/bp00023a005","article-title":"Increased Activity of Chromobacterium viscosum Lipase in Aerosol OT Reverse Micelles in the Presence of Nonionic Surfactants","volume":"9","author":"Y. Yamada","year":"1993","journal-title":"Biotechnol. Prog."},{"issue":"4","key":"pone.0314556.ref119","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1159\/000365890","article-title":"Rational Design of K173A Substitution Enhances Thermostability Coupled with Catalytic Activity of Enterobacter sp.","volume":"24","author":"P. Farrokh","year":"2014","journal-title":"Bn12 Lipase. Microb. Physiol."},{"issue":"4","key":"pone.0314556.ref120","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1002\/cben.202100045","article-title":"Lipase Catalysis in Mixed Micelles.","volume":"9","author":"D. Goswami","year":"2022","journal-title":"ChemBioEng Rev.,"},{"issue":"1","key":"pone.0314556.ref121","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1590\/S1517-83822012000100004","article-title":"Optimization of extracellular thermophilic highly alkaline lipase from thermophilic Bacillus sp isolated from Hotspring of Arunachal Pradesh","volume":"43","author":"L. Bora","year":"2012","journal-title":"India. Braz. J. Microbiol."},{"issue":"1","key":"pone.0314556.ref122","doi-asserted-by":"crossref","first-page":"237","DOI":"10.3390\/applmicrobiol2010017","article-title":"Enhancing Lipase Production of Bacillus salmalaya Strain 139SI Using Different Carbon Sources and Surfactants","volume":"2","author":"M. Mohaini","year":"2022","journal-title":"Appl. Microbiol."},{"key":"pone.0314556.ref123","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1007\/s11746-008-1259-1","article-title":"Effect of surfactants and polyethylene glycol on the activity and stability of a lipase from oil seeds of Pachira aquatica","volume":"85","author":"P. P. Polizelli","year":"2008","journal-title":"J. Am. Oil Chem. Soc."},{"issue":"10","key":"pone.0314556.ref124","doi-asserted-by":"crossref","first-page":"1673","DOI":"10.1016\/j.procbio.2014.06.007","article-title":"An extracellular solvent stable alkaline lipase from Pseudomonas sp. DMVR46: Partial purification, characterization and application in non-aqueous environment","volume":"49","author":"V. Patel","year":"2014","journal-title":"Process Biochem."}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0314556","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,12,17]],"date-time":"2024-12-17T18:34:31Z","timestamp":1734460471000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0314556"}},"subtitle":[],"editor":[{"given":"Estibaliz","family":"Sansinenea","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2024,12,17]]},"references-count":124,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2024,12,17]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0314556","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,12,17]]}}}