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Identification and characterization of a novel (S)-ketoprofen-specific esterase

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dc.contributor.author윤상영-
dc.contributor.author김승범-
dc.contributor.author유연우-
dc.contributor.author김두헌-
dc.date.accessioned2023-12-18T10:31:46Z-
dc.date.available2023-12-18T10:31:46Z-
dc.date.issued2007-06-
dc.identifier.issn0141-8130-
dc.identifier.issn1879-0003-
dc.identifier.urihttps://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/159246-
dc.description.abstractA new (S)-ketoprofen specific esterase (EST-Y29) was identified from a metagenome library from environmental samples, which showed homologies with class C-beta lactamase, penicillin binding protein, and other lipases/esterases. In order to investigate the biochemical and biophysical properties, the recombinant protein was overexpressed, purified to homogeneity, and characterized. This EST-Y29 has high catalytic activity against p-nitrophenyl esters of short fatty acids (C-2 and C-4) and alpha-naphthyl acetate with activation energy of 30.40/mol. We have further characterized EST-Y29 using high performance liquid chromatography (HPLC), circular dichroism (CD), dynamic light scattering (DLS) and size exclusion chromatography (SEC). (c) 2006 Published by Elsevier B.V.-
dc.format.extent7-
dc.language영어-
dc.language.isoENG-
dc.publisherElsevier BV-
dc.titleIdentification and characterization of a novel (S)-ketoprofen-specific esterase-
dc.typeArticle-
dc.publisher.location네델란드-
dc.identifier.doi10.1016/j.ijbiomac.2006.11.010-
dc.identifier.scopusid2-s2.0-33947519464-
dc.identifier.wosid000246089000001-
dc.identifier.bibliographicCitationInternational Journal of Biological Macromolecules, v.41, no.1, pp 1 - 7-
dc.citation.titleInternational Journal of Biological Macromolecules-
dc.citation.volume41-
dc.citation.number1-
dc.citation.startPage1-
dc.citation.endPage7-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S014181300600328X?via%3Dihub-
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