{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,4]],"date-time":"2026-04-04T12:02:26Z","timestamp":1775304146998,"version":"3.50.1"},"reference-count":25,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2014,10,1]],"date-time":"2014-10-01T00:00:00Z","timestamp":1412121600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"crossref","award":["u1170303"],"award-info":[{"award-number":["u1170303"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"crossref","award":["2013QC023"],"award-info":[{"award-number":["2013QC023"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Enzyme and Microbial Technology"],"published-print":{"date-parts":[[2014,10]]},"DOI":"10.1016\/j.enzmictec.2014.06.003","type":"journal-article","created":{"date-parts":[[2014,6,28]],"date-time":"2014-06-28T15:16:00Z","timestamp":1403968560000},"page":"11-16","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":23,"special_numbering":"C","title":["Improved thermostability of esterase from Aspergillus fumigatus by site-directed mutagenesis"],"prefix":"10.1016","volume":"64-65","author":[{"given":"Shanshan","family":"Zhang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gaobing","family":"Wu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shiyu","family":"Feng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ziduo","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.enzmictec.2014.06.003_bib0005","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1111\/j.1574-6976.2002.tb00599.x","article-title":"Microbial carboxyl esterases: classification, properties and application in biocatalysis","volume":"26","author":"Bornscheuer","year":"2002","journal-title":"FEMS Microbiol Rev"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0010","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1007\/s00284-009-9533-5","article-title":"Characterization of a novel thermostable esterase from Thermus scotoductus SA-01: evidence of a new family of lipolytic esterases","volume":"60","author":"du Plessis","year":"2010","journal-title":"Curr Microbiol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0015","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.bbrc.2010.01.070","article-title":"Molecular cloning and characterization of a novel family VIII alkaline esterase from a compost metagenomic library","volume":"393","author":"Kim","year":"2010","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0020","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/s10295-012-1217-7","article-title":"Characterization of three new carboxylic ester hydrolases isolated by functional screening of a forest soil metagenomic library","volume":"40","author":"Biver","year":"2013","journal-title":"J Ind Microbiol Biotechnol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0025","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1007\/s00253-004-1840-y","article-title":"Production and applications of esterases","volume":"67","author":"Panda","year":"2005","journal-title":"Appl Microbiol Biotechnol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0030","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1016\/j.bbagen.2006.01.009","article-title":"A carboxylesterase from the thermoacidophilic archaeon Sulfolobus solfataricus P1; purification, characterization, and expression","volume":"1760","author":"Park","year":"2006","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0035","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1128\/AEM.71.2.817-825.2005","article-title":"New thermophilic and thermostable esterase with sequence similarity to the hormone-sensitive lipase family, cloned from a metagenomic library","volume":"71","author":"Rhee","year":"2005","journal-title":"Appl Environ Microbiol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0040","doi-asserted-by":"crossref","first-page":"2064","DOI":"10.1016\/j.procbio.2012.07.023","article-title":"A thermostable variant of P. aeruginosa cold-adapted LipC obtained by rational design and saturation mutagenesis","volume":"47","author":"Cesarini","year":"2012","journal-title":"Process Biochem"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0045","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.molcatb.2010.07.021","article-title":"Aspergillus sp. lipase: Potential biocatalyst for industrial use","volume":"67","author":"Contesini","year":"2010","journal-title":"J Mol Catal B: Enzym"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0050","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1007\/s12010-011-9311-2","article-title":"Expression and characterization of a novel lipase from Aspergillus fumigatus with high specific activity","volume":"165","author":"Shangguan","year":"2011","journal-title":"Appl Biochem Biotechnol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0055","first-page":"1077","article-title":"A novel pH-stable, bifunctional xylanase isolated from a deep-sea microorganism, Demequina sp. JK4","volume":"19","author":"Meng","year":"2009","journal-title":"J Microbiol Biotechnol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0060","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.enzmictec.2014.01.004","article-title":"Characterization and site-directed mutagenesis of an \u03b1-galactosidase from the deep-sea bacterium Bacillus megaterium","volume":"56","author":"Xu","year":"2014","journal-title":"Enzyme Microb Technol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0065","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1007\/s10295-013-1317-z","article-title":"Isolation and characterization of a thermostable esterase from a metagenomic library","volume":"40","author":"Shao","year":"2013","journal-title":"J Ind Microbiol Biotechnol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0070","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.molcatb.2003.11.010","article-title":"Enhanced thermostability and tolerance of high substrate concentration of an esterase by directed evolution","volume":"27","author":"Kim","year":"2004","journal-title":"J Mol Catal B: Enzym"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0075","doi-asserted-by":"crossref","first-page":"2919","DOI":"10.1007\/s11033-010-9954-z","article-title":"Engineering of Bacillus lipase by directed evolution for enhanced thermal stability: effect of isoleucine to threonine mutation at protein surface","volume":"38","author":"Khurana","year":"2011","journal-title":"Mol Biol Rep"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0080","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S1367-5931(00)00182-4","article-title":"Improved biocatalysts by directed evolution and rational protein design","volume":"5","author":"Bornscheuer","year":"2001","journal-title":"Curr Opin Chem Biol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0085","doi-asserted-by":"crossref","first-page":"1841","DOI":"10.1007\/s10529-011-0635-3","article-title":"Substitution of Asp189 residue alters the activity and thermostability of Geobacillus sp. NTU 03 lipase","volume":"33","author":"Shih","year":"2011","journal-title":"Biotechnol Lett"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0090","doi-asserted-by":"crossref","first-page":"5728","DOI":"10.1128\/AEM.71.10.5728-5734.2005","article-title":"Directed evolution of a thermostable phosphite dehydrogenase for NAD (P) H regeneration","volume":"71","author":"Johannes","year":"2005","journal-title":"Appl Environ Microbiol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0095","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1093\/protein\/15.8.689","article-title":"Improvement of oxidative and thermostability of N-carbamyl-d-amino acid amidohydrolase by directed evolution","volume":"15","author":"Oh","year":"2002","journal-title":"Protein Eng"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0100","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1007\/s00253-002-1215-1","article-title":"Significantly enhanced stability of glucose dehydrogenase by directed evolution","volume":"61","author":"Baik","year":"2003","journal-title":"Appl Microbiol Biotechnol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0105","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/j.jbiotec.2012.08.023","article-title":"Improving the thermostability of lipase Lip2 from Yarrowia lipolytica","volume":"164","author":"Wen","year":"2012","journal-title":"J Biotechnol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0110","doi-asserted-by":"crossref","first-page":"4866","DOI":"10.1128\/AEM.69.8.4866-4874.2003","article-title":"Directed evolution of Thermus maltogenic amylase toward enhanced thermal resistance","volume":"69","author":"Kim","year":"2003","journal-title":"Appl Environ Microbiol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0115","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1007\/s00253-011-3337-9","article-title":"The crystal structure of an esterase from the hyperthermophilic microorganism Pyrobaculum calidifontis VA1 explains its enantioselectivity","volume":"91","author":"Palm","year":"2011","journal-title":"Appl Microbiol Biotechnol"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0120","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1093\/protein\/13.3.179","article-title":"Factors enhancing protein thermostability","volume":"13","author":"Kumar","year":"2000","journal-title":"Protein Eng"},{"key":"10.1016\/j.enzmictec.2014.06.003_bib0125","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1006\/jmbi.1997.1042","article-title":"Protein thermal stability, hydrogen bonds, and ion pairs","volume":"269","author":"Vogt","year":"1997","journal-title":"J Mol Biol"}],"container-title":["Enzyme and Microbial Technology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141022914001197?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141022914001197?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,5,12]],"date-time":"2020-05-12T01:30:29Z","timestamp":1589247029000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141022914001197"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,10]]},"references-count":25,"alternative-id":["S0141022914001197"],"URL":"https:\/\/doi.org\/10.1016\/j.enzmictec.2014.06.003","relation":{},"ISSN":["0141-0229"],"issn-type":[{"value":"0141-0229","type":"print"}],"subject":[],"published":{"date-parts":[[2014,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Improved thermostability of esterase from Aspergillus fumigatus by site-directed mutagenesis","name":"articletitle","label":"Article Title"},{"value":"Enzyme and Microbial Technology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.enzmictec.2014.06.003","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}