Biochemical characterization and sequence analysis of a xylanase produced by an exo-symbiotic bacterium of Gryllotalpa orientalis, Cellulosimicrobium sp. HY-12

Cited 24 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorHyun Woo Oh-
dc.contributor.authorSun Yeon Heo-
dc.contributor.authorDo Young Kim-
dc.contributor.authorDoo Sang Park-
dc.contributor.authorKyung Sook Bae-
dc.contributor.authorHo Yong Park-
dc.date.accessioned2017-04-19T09:09:55Z-
dc.date.available2017-04-19T09:09:55Z-
dc.date.issued2008-
dc.identifier.issn0003-6072-
dc.identifier.uri10.1007/s10482-007-9210-2ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8372-
dc.description.abstractAn exo-symbiotic bacterium capable of hydrolyzing xylan was isolated from the gut of the mole cricket, Gryllotalpa orientalis, and identified as Cellulosimicrobium sp. HY-12. The xylanase (XylACspHY-12) of this organism bound tightly to both DEAE and mono Q resins, and its molecular mass (Mr) was about 39.0 kDa. The highest xylanase activity was observed at pH 6.0 and 60°C. The enzyme was greatly suppressed by Ca2+, Cu2+, Co2+, and Fe2+ ions but not by Mg2+ and Mn2+. Although XylACspHY-12 was capable of hydrolyzing various types of xylosic compounds, it could not decompose carboxymethyl cellulose or xylobiose. The xylACspHY-12 gene consisted of an 1,188 bp open reading frame that encoded a polypeptide of 395 amino acids with a deduced molecular mass of 42,925 Da. The domain structure of XylACspHY-12 was most similar to those of the glycoside hydrolase (GH) family 10 endoxylanases. However its sequence identity with any of the enzymes in this family was below 52%. The results of this study suggest that the XylACspHY-12 is a new cellulase-free endo-β-1,4-xylanase with some properties that are distinct from those of GH family 10.-
dc.publisherSpringer-
dc.titleBiochemical characterization and sequence analysis of a xylanase produced by an exo-symbiotic bacterium of Gryllotalpa orientalis, Cellulosimicrobium sp. HY-12-
dc.title.alternativeBiochemical characterization and sequence analysis of a xylanase produced by an exo-symbiotic bacterium of Gryllotalpa orientalis, Cellulosimicrobium sp. HY-12-
dc.typeArticle-
dc.citation.titleAntonie Van Leeuwenhoek International Journal of General and Molecular Microbiology-
dc.citation.number4-
dc.citation.endPage442-
dc.citation.startPage437-
dc.citation.volume93-
dc.contributor.affiliatedAuthorHyun Woo Oh-
dc.contributor.affiliatedAuthorSun Yeon Heo-
dc.contributor.affiliatedAuthorDo Young Kim-
dc.contributor.affiliatedAuthorDoo Sang Park-
dc.contributor.affiliatedAuthorKyung Sook Bae-
dc.contributor.affiliatedAuthorHo Yong Park-
dc.contributor.alternativeName오현우-
dc.contributor.alternativeName허선연-
dc.contributor.alternativeName김도영-
dc.contributor.alternativeName박두상-
dc.contributor.alternativeName배경숙-
dc.contributor.alternativeName박호용-
dc.identifier.bibliographicCitationAntonie Van Leeuwenhoek International Journal of General and Molecular Microbiology, vol. 93, no. 4, pp. 437-442-
dc.identifier.doi10.1007/s10482-007-9210-2-
dc.subject.keywordCellulosimicrobium sp. HY-12-
dc.subject.keywordExo-symbiotic bacterium-
dc.subject.keywordGlycoside hydrolase family 10-
dc.subject.keywordXylanase-
dc.subject.localCellulosimicrobium sp. HY-12-
dc.subject.localExo-symbiotic bacterium-
dc.subject.localGlycoside hydrolase family 10-
dc.subject.localXylanase-
dc.subject.localxylanase-
dc.description.journalClassY-
Appears in Collections:
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
Jeonbuk Branch Institute > Biological Resource Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.