Nonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1

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dc.contributor.authorYeo Jin Jung-
dc.contributor.authorJung-Kee Lee-
dc.contributor.authorC G Sung-
dc.contributor.authorTae Kwang Oh-
dc.contributor.authorHyung Kwoun Kim-
dc.date.accessioned2017-04-19T09:00:24Z-
dc.date.available2017-04-19T09:00:24Z-
dc.date.issued2003-
dc.identifier.issn1381-1177-
dc.identifier.uri10.1016/j.molcatb.2003.06.006ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6275-
dc.description.abstractAn esterase-producing Bacillus megaterium strain (20-1) was isolated from a soil sample collected in South Korea. The cloned gene showed that the esterase 20-1 composed of 310 amino acids corresponding to a molecular mass (Mr) of 34,638. Based on the Mr and the protein sequence, the esterase 20-1 belonged to the H lipase/esterase group. The optimum temperature and pH of the purified His-tagged enzyme were 20-35°C and 8.0, respectively. The esterase 20-1 showed a 'nonionic detergent-induced activation' phenomenon, which was a detergent type- and concentration-dependent process. In comparison with the native enzyme, the Tween 80-treated enzyme had relatively a similar kcat value of 274s-1 but a very low Km value of 0.037mM for PNPC (C6), therefore, it showed a 14-fold increase in kcat/Km value.-
dc.publisherElsevier-
dc.titleNonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1-
dc.title.alternativeNonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1-
dc.typeArticle-
dc.citation.titleJournal of Molecular Catalysis B: Enzymatic-
dc.citation.number3-
dc.citation.endPage229-
dc.citation.startPage223-
dc.citation.volume26-
dc.contributor.affiliatedAuthorYeo Jin Jung-
dc.contributor.affiliatedAuthorJung-Kee Lee-
dc.contributor.affiliatedAuthorTae Kwang Oh-
dc.contributor.alternativeName정여진-
dc.contributor.alternativeName이정기-
dc.contributor.alternativeName성창근-
dc.contributor.alternativeName오태광-
dc.contributor.alternativeName김형권-
dc.identifier.bibliographicCitationJournal of Molecular Catalysis B: Enzymatic, vol. 26, no. 3, pp. 223-229-
dc.identifier.doi10.1016/j.molcatb.2003.06.006-
dc.subject.keywordAlicyclobacillus acidocaldarius-
dc.subject.keywordBacillus megaterium-
dc.subject.keywordDetergent-induced activation-
dc.subject.keywordEsterase-
dc.subject.localAlicyclobacillus acidocaldarius-
dc.subject.localBacillus megaterium-
dc.subject.localDetergent-induced activation-
dc.subject.localEsterase-
dc.subject.localesterases-
dc.subject.localesterase-
dc.description.journalClassN-
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Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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