Characterization of an extracellular xylanase from Bacillus sp. HY-20, a bacterium in the gut of Apis mellifera = 꿀벌(Apis mellifera)의 장내 세균인 Bacillus sp. HY-20이 분비하는 Xylanase의 특성

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dc.contributor.authorLan Hee Lee-
dc.contributor.authorKim Do Young-
dc.contributor.authorM K Han-
dc.contributor.authorHyun Woo Oh-
dc.contributor.authorSu Jin Ham-
dc.contributor.authorDoo Sang Park-
dc.contributor.authorKyung Sook Bae-
dc.contributor.authorD E Sok-
dc.contributor.authorD H Shin-
dc.contributor.authorKwang Hee Son-
dc.contributor.authorHo Yong Park-
dc.date.accessioned2017-04-19T09:16:54Z-
dc.date.available2017-04-19T09:16:54Z-
dc.date.issued2009-
dc.identifier.issn0440-2413-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9323-
dc.description.abstractA xylan-decomposing bacterium, HY-20, was isolated from the gut of a honeybee, Apis mellifera, and identified as Bacillus sp. The extracellular GH11 xylanase (XylP) gene (687-bp) of strain HY-20 encoded a protein of 228 amino acids with a deduced molecular mass of 25,522 Da and a calculated pI of 9.33. The primary structure of XylP was 97% identical to that of B. pumilus xylanase (GenBank accession no.: AY526092) that has not been characterized yet. The recombinant His-tagged enzyme (rXylP) overexpressed in Escherichia coli BL21 harboring pET-28a(+)/xylP was purified to electrophoretic homogeneity by cation exchange and gel permeation chromatographies. The purified enzyme exhibited the highest catalytic activity toward birchwood xylan at pH 6.5 and 50°C and retained approximately 50% of its original activity when pre-incubated at 55°C for 15 min. The recombinant enzyme was completely inactivated by Hg2+ (1 mM) and N-bromosuccinimide (5 mM), while its activity was slightly stimulated by approximately 10% in the presence of Mn2+ (1 mM), Fe2+ (1 mM), and sodium azide (5 mM). rXylP was able to efficiently degrade various polymeric xylose-based substrates but PNP-sugar derivatives and glucose-based polymers were not susceptible to the enzyme.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleCharacterization of an extracellular xylanase from Bacillus sp. HY-20, a bacterium in the gut of Apis mellifera = 꿀벌(Apis mellifera)의 장내 세균인 Bacillus sp. HY-20이 분비하는 Xylanase의 특성-
dc.title.alternativeCharacterization of an extracellular xylanase from Bacillus sp. HY-20, a bacterium in the gut of Apis mellifera-
dc.typeArticle-
dc.citation.titleKorean Journal of Microbiology-
dc.citation.number4-
dc.citation.endPage338-
dc.citation.startPage332-
dc.citation.volume45-
dc.contributor.affiliatedAuthorLan Hee Lee-
dc.contributor.affiliatedAuthorKim Do Young-
dc.contributor.affiliatedAuthorHyun Woo Oh-
dc.contributor.affiliatedAuthorSu Jin Ham-
dc.contributor.affiliatedAuthorDoo Sang Park-
dc.contributor.affiliatedAuthorKyung Sook Bae-
dc.contributor.affiliatedAuthorKwang Hee Son-
dc.contributor.affiliatedAuthorHo Yong Park-
dc.contributor.alternativeName이란희-
dc.contributor.alternativeName김도영-
dc.contributor.alternativeName한미경-
dc.contributor.alternativeName오현우-
dc.contributor.alternativeName함수진-
dc.contributor.alternativeName박두상-
dc.contributor.alternativeName배경숙-
dc.contributor.alternativeName석대은-
dc.contributor.alternativeName신동하-
dc.contributor.alternativeName손광희-
dc.contributor.alternativeName박호용-
dc.identifier.bibliographicCitationKorean Journal of Microbiology, vol. 45, no. 4, pp. 332-338-
dc.subject.keywordApis mellifera-
dc.subject.keywordBacillus sp. HY-20-
dc.subject.keywordBee-
dc.subject.keywordGut bacterium-
dc.subject.keywordXylanase-
dc.subject.localApis mellifera-
dc.subject.localBacillus sp. HY-20-
dc.subject.localBee-
dc.subject.localGut bacterium-
dc.subject.localXylanase-
dc.subject.localxylanase-
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
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