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김용환

Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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dc.citation.endPage 1533 -
dc.citation.number 5 -
dc.citation.startPage 1530 -
dc.citation.title KOREAN JOURNAL OF CHEMICAL ENGINEERING -
dc.citation.volume 33 -
dc.contributor.author Jeong, Seongwook -
dc.contributor.author Yeon, Young Joo -
dc.contributor.author Choi, Eun-Gyu -
dc.contributor.author Byun, Sungmin -
dc.contributor.author Cho, DaeHaeng -
dc.contributor.author Kim, Il Kwon -
dc.contributor.author Kim, Yong Hwan -
dc.date.accessioned 2023-12-21T23:42:43Z -
dc.date.available 2023-12-21T23:42:43Z -
dc.date.created 2016-09-06 -
dc.date.issued 2016-05 -
dc.description.abstract The enzymatic decarboxylation of L-lysine using lysine decarboxylase is a promising biological approach for producing cadaverine, a versatile platform chemical for bio-polyamides. However, due to the problem with elevated pH in the reaction solution during the enzymatic process, it is desirable to use lysine decarboxylases effectively active in alkaline conditions. In this study, the catalytic properties of three lysine decarboxylases from Selenomonas ruminantium (srLDC), Vibrio vulnificus (vvLDC), and Geobacillus thermodenitrificans (gtLDC) were characterized, and the applicability of the enzymes in alkaline conditions was investigated. Among the three enzymes, only vvLDC exhibited effective activity in alkaline pH conditions. The conversion rate of vvLDC was 1.5-fold higher than that of srLDC and 5.3-fold higher than that of gtLDC in pH 9.0. The results indicate that vvLDC is more advantageous than srLDC and gtLDC for the enzymatic conversion of L-lysine to cadaverine in alkaline conditions. -
dc.identifier.bibliographicCitation KOREAN JOURNAL OF CHEMICAL ENGINEERING, v.33, no.5, pp.1530 - 1533 -
dc.identifier.doi 10.1007/s11814-016-0079-5 -
dc.identifier.issn 0256-1115 -
dc.identifier.scopusid 2-s2.0-84964393683 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/20318 -
dc.identifier.url http://link.springer.com/article/10.1007%2Fs11814-016-0079-5 -
dc.identifier.wosid 000375079500003 -
dc.language 영어 -
dc.publisher KOREAN INSTITUTE CHEMICAL ENGINEERS -
dc.title Alkaliphilic lysine decarboxylases for effective synthesis of cadaverine from L-lysine -
dc.type Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.description.journalRegisteredClass kci -
dc.subject.keywordAuthor Lysine Decarboxylase -
dc.subject.keywordAuthor L-Lysine -
dc.subject.keywordAuthor Cadaverine -
dc.subject.keywordAuthor pH Optimum -
dc.subject.keywordAuthor Alkaline Conditions -
dc.subject.keywordPlus ESCHERICHIA-COLI -
dc.subject.keywordPlus PURIFICATION -
dc.subject.keywordPlus DIRECTIONS -
dc.subject.keywordPlus ACIDS -

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