Bioconversion of ginsenosides Rb1, Rb2, Rc and Rd by novel beta-glucosidase hydrolyzing outer 3-O glycoside from Sphingomonas sp. 2F2: Cloning, expression, and enzyme characterization

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dc.contributor.authorL Wang-
dc.contributor.authorQ M Liu-
dc.contributor.authorBong Hyun Sung-
dc.contributor.authorD S An-
dc.contributor.authorHyung Gwan Lee-
dc.contributor.authorSong-Gun Kim-
dc.contributor.authorS C Kim-
dc.contributor.authorS T Lee-
dc.contributor.authorW T Im-
dc.date.accessioned2017-04-19T09:25:45Z-
dc.date.available2017-04-19T09:25:45Z-
dc.date.issued2011-
dc.identifier.issn0168-1656-
dc.identifier.uri10.1016/j.jbiotec.2011.07.024ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10381-
dc.description.abstractA new β-glucosidase gene (bglSp) was cloned from the ginsenoside converting Sphingomonas sp. strain 2F2 isolated from the ginseng cultivating filed. The bglSp consisted of 1344bp (447 amino acid residues) with a predicted molecular mass of 49,399Da. A BLAST search using the bglSp sequence revealed significant homology to that of glycoside hydrolase superfamily 1. This enzyme was overexpressed in Escherichia coli BL21 (DE3) using a pET21-MBP (TEV) vector system. Overexpressed recombinant enzymes which could convert the ginsenosides Rb 1, Rb 2, Rc and Rd to the more pharmacological active rare ginsenosides gypenoside XVII, ginsenoside C-O, ginsenoside C-Mc 1 and ginsenoside F 2, respectively, were purified by two steps with Amylose-affinity and DEAE-Cellulose chromatography and characterized. The kinetic parameters for β-glucosidase showed the apparent K m and V max values of 2.9±0.3mM and 515.4±38.3μmolmin -1mg of protein -1 against p-nitrophenyl-β-d-glucopyranoside. The enzyme could hydrolyze the outer C3 glucose moieties of ginsenosides Rb 1, Rb 2, Rc and Rd into the rare ginsenosides Gyp XVII, C-O, C-Mc 1 and F 2 quickly at optimal conditions of pH 5.0 and 37°C. A little ginsenoside F 2 production from ginsenosides Gyp XVII, C-O, and C-Mc 1 was observed for the lengthy enzyme reaction caused by the side ability of the enzyme.-
dc.publisherElsevier-
dc.titleBioconversion of ginsenosides Rb1, Rb2, Rc and Rd by novel beta-glucosidase hydrolyzing outer 3-O glycoside from Sphingomonas sp. 2F2: Cloning, expression, and enzyme characterization-
dc.title.alternativeBioconversion of ginsenosides Rb1, Rb2, Rc and Rd by novel beta-glucosidase hydrolyzing outer 3-O glycoside from Sphingomonas sp. 2F2: Cloning, expression, and enzyme characterization-
dc.typeArticle-
dc.citation.titleJournal of Biotechnology-
dc.citation.number2-
dc.citation.endPage133-
dc.citation.startPage125-
dc.citation.volume156-
dc.contributor.affiliatedAuthorBong Hyun Sung-
dc.contributor.affiliatedAuthorHyung Gwan Lee-
dc.contributor.affiliatedAuthorSong-Gun Kim-
dc.contributor.alternativeNameWang-
dc.contributor.alternativeNameLiu-
dc.contributor.alternativeName성봉현-
dc.contributor.alternativeName안동선-
dc.contributor.alternativeName이형관-
dc.contributor.alternativeName김성건-
dc.contributor.alternativeName김선창-
dc.contributor.alternativeName이성택-
dc.contributor.alternativeName임완택-
dc.identifier.bibliographicCitationJournal of Biotechnology, vol. 156, no. 2, pp. 125-133-
dc.identifier.doi10.1016/j.jbiotec.2011.07.024-
dc.subject.keywordβ-Glucosidase-
dc.subject.keywordBioconversion-
dc.subject.keywordGinsenoside-
dc.subject.keywordSphingomonas-
dc.subject.localβ-Glucosidase-
dc.subject.localβ-glucosidase-
dc.subject.localΒ-glucosidase-
dc.subject.localBio-conversion-
dc.subject.localbioconversion-
dc.subject.localBioconversion-
dc.subject.localginsenoside-
dc.subject.localGinsenoside-
dc.subject.localGinsenosides-
dc.subject.localsphingomonas-
dc.subject.localSphingomonas-
dc.description.journalClassY-
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > Synthetic Biology Research Center > 1. Journal Articles
Synthetic Biology and Bioengineering Research Institute > Cell Factory Research Center > 1. Journal Articles
Jeonbuk Branch Institute > Biological Resource Center > 1. Journal Articles
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