Catalytic properties of a GH10 endo-β-1,4-xylanase from Streptomyces thermocarboxydus HY-15 isolated from the gut of Eisenia fetida

Cited 37 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorDo Young Kim-
dc.contributor.authorMi Kyung Han-
dc.contributor.authorHyun Woo Oh-
dc.contributor.authorDoo Sang Park-
dc.contributor.authorSu Jin Kim-
dc.contributor.authorSeung Goo Lee-
dc.contributor.authorD H Shin-
dc.contributor.authorKwang Hee Son-
dc.contributor.authorKyung Sook Bae-
dc.contributor.authorHo Yong Park-
dc.date.accessioned2017-04-19T09:15:21Z-
dc.date.available2017-04-19T09:15:21Z-
dc.date.issued2010-
dc.identifier.issn1381-1177-
dc.identifier.uri10.1016/j.molcatb.2009.08.015ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9189-
dc.description.abstractA novel GH10 endo-β-1,4-xylanase (XylG) gene from Streptomyces thermocarboxydus HY-15, which was isolated from the gut of Eisenia fetida, was cloned, over-expressed, and characterized. The XylG gene (1182 bp) encoded a polypeptide of 393 amino acids with a deduced molecular mass of 43,962 Da and a calculated pI of 6.74. The primary structure of XylG was 69% similar to that of Thermobifida fusca YX endo-β-1,4-xylanase. It was most active at pH 6.0 and 55 °C. The susceptibilities of xylans to XylG were as follows: oat spelt xylan > birchwood xylan > beechwood xylan. The XylG also showed high activity (474 IU/mg) toward p-nitrophenylcellobioside. Moreover, at pH 6.0 and 50 °C, the Vmax and Km values of the XylG were 127 IU/mg and 2.51 mg/ml, respectively, for oat spelt xylan and 782 IU/mg and 5.26 mM, respectively, for p-nitrophenylcellobioside. A homology model indicated that XylG folded to form a (β/α)8-barrel with two catalytic residues of an acid/base (Glu181) and a nucleophile (Glu289). The formation of a disulfide bond between Cys321 and Cys327 were predicted by homology modeling.-
dc.publisherElsevier-
dc.titleCatalytic properties of a GH10 endo-β-1,4-xylanase from Streptomyces thermocarboxydus HY-15 isolated from the gut of Eisenia fetida-
dc.title.alternativeCatalytic properties of a GH10 endo-β-1,4-xylanase from Streptomyces thermocarboxydus HY-15 isolated from the gut of Eisenia fetida-
dc.typeArticle-
dc.citation.titleJournal of Molecular Catalysis B: Enzymatic-
dc.citation.number1-
dc.citation.endPage39-
dc.citation.startPage32-
dc.citation.volume62-
dc.contributor.affiliatedAuthorDo Young Kim-
dc.contributor.affiliatedAuthorMi Kyung Han-
dc.contributor.affiliatedAuthorHyun Woo Oh-
dc.contributor.affiliatedAuthorDoo Sang Park-
dc.contributor.affiliatedAuthorSu Jin Kim-
dc.contributor.affiliatedAuthorSeung Goo Lee-
dc.contributor.affiliatedAuthorKwang Hee Son-
dc.contributor.affiliatedAuthorKyung Sook Bae-
dc.contributor.affiliatedAuthorHo Yong Park-
dc.contributor.alternativeName김도영-
dc.contributor.alternativeName한미경-
dc.contributor.alternativeName오현우-
dc.contributor.alternativeName박두상-
dc.contributor.alternativeName김수진-
dc.contributor.alternativeName이승구-
dc.contributor.alternativeName신동하-
dc.contributor.alternativeName손광희-
dc.contributor.alternativeName배경숙-
dc.contributor.alternativeName박호용-
dc.identifier.bibliographicCitationJournal of Molecular Catalysis B: Enzymatic, vol. 62, no. 1, pp. 32-39-
dc.identifier.doi10.1016/j.molcatb.2009.08.015-
dc.subject.keywordEndo-β-1,4-xylanase-
dc.subject.keywordGlycoside hydrolase family 10-
dc.subject.keywordp-Nitrophenylcellobioside-
dc.subject.keywordPNP-cellobioside-
dc.subject.keywordStreptomyces thermocarboxydus HY-15-
dc.subject.localEndo-β-1,4-xylanase-
dc.subject.localGlycoside hydrolase family 10-
dc.subject.localp-Nitrophenylcellobioside-
dc.subject.localPNP-cellobioside-
dc.subject.localStreptomyces thermocarboxydus HY-15-
dc.description.journalClassN-
Appears in Collections:
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
Jeonbuk Branch Institute > Biological Resource Center > 1. Journal Articles
Synthetic Biology and Bioengineering Research Institute > 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.