Novel alkali-tolerant GH10 endo-β-1,4-xylanase with broad substrate specificity from Microbacterium trichothecenolyticum HY-17, a gut bacterium of the mole cricket Gryllotalpa orientalis

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dc.contributor.authorDo Young Kim-
dc.contributor.authorD H Shin-
dc.contributor.authorSora Jung-
dc.contributor.authorHyangmi Kim-
dc.contributor.authorJ S Lee-
dc.contributor.authorHan Young Cho-
dc.contributor.authorKyung Sook Bae-
dc.contributor.authorC K Sung-
dc.contributor.authorY H Rhee-
dc.contributor.authorKwang- Hee Son-
dc.contributor.authorHo Yong Park-
dc.date.accessioned2017-04-19T09:54:40Z-
dc.date.available2017-04-19T09:54:40Z-
dc.date.issued2014-
dc.identifier.issn1017-7825-
dc.identifier.uri10.4014/jmb.1405.05032ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/12053-
dc.description.abstractThe XylH gene (1167-bp) encoding a novel hemicellulase (41,584 Da) was identified from the genome of Microbacterium trichothecenolyticum HY-17, a gastrointestinal bacterium of Gryllotalpa orientalis. The enzyme consisted of a single catalytic domain, which is 74% identical to that ofof an endo-β-1,4-xylanase (GH10) from Isoptericola variabilis 225. Unlike other endo-β-1,4-xylanases from invertebrate-symbiotic bacteria, rXylH was an alkali-tolerant multi-functional enzyme possessing endo-beta-1,4-xylanase activity together with beta-1,3/beta-1,4-glucanase activity, which exhibited its highest xylanolytic activity at pH 9.0 and 60oC, and was relatively stable within a broad pH range of 5.0-10.0. The susceptibilities of different xylose-based polysaccharides to the XylH were assessed to be as follows: oat spelts xylan > beechwood xylan > birchwood xylan > wheat arabinoxylan. rXylH was also able to readily cleave p-nitrophenyl (pNP) cellobioside and pNP-xylopyranoside but did not hydrolyze other pNP-sugar derivatives, xylobiose, or hexose-based materials. Enzymatic hydrolysis of birchwood xylan resulted in the product composition of xylobiose (71.2%) and xylotriose (28.8%) as end products.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleNovel alkali-tolerant GH10 endo-β-1,4-xylanase with broad substrate specificity from Microbacterium trichothecenolyticum HY-17, a gut bacterium of the mole cricket Gryllotalpa orientalis-
dc.title.alternativeNovel alkali-tolerant GH10 endo-β-1,4-xylanase with broad substrate specificity from Microbacterium trichothecenolyticum HY-17, a gut bacterium of the mole cricket Gryllotalpa orientalis-
dc.typeArticle-
dc.citation.titleJournal of Microbiology and Biotechnology-
dc.citation.number7-
dc.citation.endPage953-
dc.citation.startPage943-
dc.citation.volume24-
dc.contributor.affiliatedAuthorDo Young Kim-
dc.contributor.affiliatedAuthorSora Jung-
dc.contributor.affiliatedAuthorHyangmi Kim-
dc.contributor.affiliatedAuthorHan Young Cho-
dc.contributor.affiliatedAuthorKyung Sook Bae-
dc.contributor.affiliatedAuthorKwang- Hee Son-
dc.contributor.affiliatedAuthorHo Yong Park-
dc.contributor.alternativeName김도영-
dc.contributor.alternativeName신동하-
dc.contributor.alternativeName정소라-
dc.contributor.alternativeName김향미-
dc.contributor.alternativeName이종석-
dc.contributor.alternativeName조한영-
dc.contributor.alternativeName배경숙-
dc.contributor.alternativeName성창근-
dc.contributor.alternativeName이영하-
dc.contributor.alternativeName손광희-
dc.contributor.alternativeName박호용-
dc.identifier.bibliographicCitationJournal of Microbiology and Biotechnology, vol. 24, no. 7, pp. 943-953-
dc.identifier.doi10.4014/jmb.1405.05032-
dc.subject.keyword4-xylanase-
dc.subject.keywordEndo-β-1-
dc.subject.keywordGH10 enzyme-
dc.subject.keywordGut bacterium-
dc.subject.keywordMicrobacterium trichothecenolyticum HY-17-
dc.subject.keywordMole cricket-
dc.subject.local4-xylanase-
dc.subject.localEndo-β-1-
dc.subject.localGH10 enzyme-
dc.subject.localGut bacterium-
dc.subject.localMicrobacterium trichothecenolyticum HY-17-
dc.subject.localMole cricket-
dc.description.journalClassY-
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Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
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