Item type |
学術雑誌論文 / Journal Article(1) |
公開日 |
2013-01-18 |
タイトル |
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タイトル |
Isolation of genes coding for chitin-degrading enzymes in the novel chitinolytic bacterium, Chitiniphilus shinanonensis, and characterization of a gene coding for a family 19 chitinase |
言語 |
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言語 |
eng |
DOI |
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関連識別子 |
https://doi.org/10.1016/j.jbiosc.2011.10.018 |
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関連名称 |
10.1016/j.jbiosc.2011.10.018 |
キーワード |
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主題 |
Chitiniphilus shinanonensis, Family 19 chitinase, Chitin-binding domain, Fungal growth inhibition |
資源タイプ |
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資源 |
http://purl.org/coar/resource_type/c_6501 |
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タイプ |
journal article |
著者 |
Huang, Lanxiang
Garbulewska, Ewelina
Sato, Kazuaki
Kato, Yuichi
Nogawa, Masahiro
Taguchi, Goro
Shimosaka, Makoto
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信州大学研究者総覧へのリンク |
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氏名 |
Nogawa, Masahiro |
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URL |
http://soar-rd.shinshu-u.ac.jp/profile/ja.gNcajNnU.html |
信州大学研究者総覧へのリンク |
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氏名 |
Taguchi, Goro |
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URL |
http://soar-rd.shinshu-u.ac.jp/profile/ja.uCDpjekV.html |
信州大学研究者総覧へのリンク |
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氏名 |
Shimosaka, Makoto |
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URL |
http://soar-rd.shinshu-u.ac.jp/profile/ja.ZekmjekV.html |
出版者 |
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出版者 |
SOC BIOSCIENCE BIOENGINEERING JAPAN |
引用 |
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内容記述 |
JOURNAL OF BIOSCIENCE AND BIOENGINEERING. 113(3):293-299 (2012) |
書誌情報 |
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
巻 113,
号 3,
p. 293-299,
発行日 2012-03
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抄録 |
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内容記述 |
Chitiniphilus shinanonensis type strain SAY3(T) is a strongly chitinolytic bacterium, originally isolated from the moat water in Ueda, Japan. To elucidate the chitinolytic activity of this strain, 15 genes (chiA-chiO) coding for putative chitin-degrading enzymes were isolated from a genomic library. Sequence analysis revealed the genes comprised 12 family 18 chitinases, a family 19 chitinase, a family 20 beta-N-acetylglucosaminidase, and a polypeptide with a chitin-binding domain but devoid of a catalytic domain. Two operons were detected among the sequences: chiCDEFG and chiLM. The gene coding for the polypeptide (chiN) showed sequence similarity to family 19 chitinases and was successfully expressed in Escherichia colt. ChiN demonstrated a multi-domain structure, composed of the N-terminal, two chitin-binding domains connected by a Pro- and Thr-rich linker, and a family 19 catalytic domain located at the C-terminus. The recombinant protein rChiN catalyzed an endo-type cleavage of N-acetyl-D-glucosamine oligomers, and also degraded insoluble chitin and soluble chitosan (degree of deacetylation of 80%). rChiN exhibited an inhibitory effect on hyphal growth of the fungus Trichoderma reesei. The chitin-binding domains of ChiN likely play an important role in the degradation of insoluble chitin, and are responsible for a growth inhibitory effect on fungi. (C) 2011, The Society for Biotechnology, Japan. All rights reserved. |
資源タイプ(コンテンツの種類) |
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内容記述 |
Article |
ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
1389-1723 |
書誌レコードID |
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収録物識別子タイプ |
NCID |
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収録物識別子 |
AA11307678 |
PubMed |
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関連識別子 |
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search&DB=pubmed&term=22178339 |
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関連名称 |
22178339 |
権利 |
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権利情報 |
Copyright© 2011, The Society for Biotechnology, Japan. |
出版タイプ |
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出版タイプ |
AM |
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出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |
WoS |
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URL |
http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=ShinshuUniv&SrcApp=ShinshuUniv&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000302505700004 |