Optimal expression and characterization of a fusion enzyme having dextransucrase and dextranase activities

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dc.contributor.authorH J Ryu-
dc.contributor.authorX Jin-
dc.contributor.authorJ H Lee-
dc.contributor.authorH J Woo-
dc.contributor.authorYoung Min Kim-
dc.contributor.authorG J Kim-
dc.contributor.authorE S Seo-
dc.contributor.authorH K Kang-
dc.contributor.authorJ Kim-
dc.contributor.authorD L Cho-
dc.contributor.authorA Kimura-
dc.contributor.authorD Kim-
dc.date.accessioned2017-04-19T09:19:32Z-
dc.date.available2017-04-19T09:19:32Z-
dc.date.issued2010-
dc.identifier.issn0141-0229-
dc.identifier.uri10.1016/j.enzmictec.2010.07.006ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9709-
dc.description.abstractLong isomalto-oligosaccharides (IMOs) were generated via an engineered fusion enzyme of dextransucrase and dextranase (DSXR). To increase the expression level, response surface methodology (RSM) was utilized for optimization of protein expression conditions for enhancement of protein production by the effects of three-level-three-factors and their mutual interaction in Escherichia coli. Seventeen experiments were designed and conducted for investigation of cell density to start induction, induction temperature, and induction time. Optimal induction conditions included a cell density to start induction (A600) of 0.76 at 12.16°C for 18h for dextransucrase activity and a cell density to start induction (A600) of 0.75 at 10.5°C for 20.9h for dextranase activity. The produced dextransucrase or dextranase activity was obtained at 120.1±7.2 or 871±58U, respectively, from 1L cultures.-
dc.publisherElsevier-
dc.titleOptimal expression and characterization of a fusion enzyme having dextransucrase and dextranase activities-
dc.title.alternativeOptimal expression and characterization of a fusion enzyme having dextransucrase and dextranase activities-
dc.typeArticle-
dc.citation.titleEnzyme and Microbial Technology-
dc.citation.number5-
dc.citation.endPage215-
dc.citation.startPage212-
dc.citation.volume47-
dc.contributor.affiliatedAuthorYoung Min Kim-
dc.contributor.alternativeName류화자-
dc.contributor.alternativeNameJin-
dc.contributor.alternativeName이진하-
dc.contributor.alternativeName우혜진-
dc.contributor.alternativeName김영민-
dc.contributor.alternativeName김가현-
dc.contributor.alternativeName서은성-
dc.contributor.alternativeName강희경-
dc.contributor.alternativeName김종호-
dc.contributor.alternativeName조동련-
dc.contributor.alternativeNameKimura-
dc.contributor.alternativeName김도만-
dc.identifier.bibliographicCitationEnzyme and Microbial Technology, vol. 47, no. 5, pp. 212-215-
dc.identifier.doi10.1016/j.enzmictec.2010.07.006-
dc.subject.keywordDextranase-
dc.subject.keywordDextransucrase-
dc.subject.keywordFusion enzyme-
dc.subject.keywordIsomalto-oligosaccharide-
dc.subject.keywordResponse surface methodology-
dc.subject.localdextranase-
dc.subject.localDextranase-
dc.subject.localDextransucrase-
dc.subject.localFusion enzyme-
dc.subject.localIsomalto-oligosacchardies-
dc.subject.localIsomalto-oligosaccharide-
dc.subject.localResponse-surface methodology-
dc.subject.localresponse surface methodology-
dc.subject.localResponse surface methodology-
dc.subject.localResponse Surface Methodology (RSM)-
dc.description.journalClassY-
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