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  1. 080 繊維学部
  2. 0801 学術論文

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

http://hdl.handle.net/10091/16192
http://hdl.handle.net/10091/16192
aad1b2ca-1af6-4626-bc9c-53a743d3ce83
名前 / ファイル ライセンス アクション
Isolation_Genes_Coding_Chitin-Degrading_Enzymes.pdf Isolation_Genes_Coding_Chitin-Degrading_Enzymes.pdf (2.3 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2013-01-18
タイトル
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
言語 eng
DOI
関連識別子 https://doi.org/10.1016/j.jbiosc.2011.10.018
関連名称 10.1016/j.jbiosc.2011.10.018
キーワード
主題 Chitiniphilus shinanonensis, Family 19 chitinase, Chitin-binding domain, Fungal growth inhibition
資源タイプ
資源 http://purl.org/coar/resource_type/c_6501
タイプ journal article
著者 Huang, Lanxiang

× Huang, Lanxiang

Huang, Lanxiang

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Garbulewska, Ewelina

× Garbulewska, Ewelina

Garbulewska, Ewelina

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Sato, Kazuaki

× Sato, Kazuaki

Sato, Kazuaki

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Kato, Yuichi

× Kato, Yuichi

Kato, Yuichi

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Nogawa, Masahiro

× Nogawa, Masahiro

Nogawa, Masahiro

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Taguchi, Goro

× Taguchi, Goro

Taguchi, Goro

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Shimosaka, Makoto

× Shimosaka, Makoto

Shimosaka, Makoto

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信州大学研究者総覧へのリンク
氏名 Nogawa, Masahiro
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
氏名 Taguchi, Goro
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
氏名 Shimosaka, Makoto
URL http://soar-rd.shinshu-u.ac.jp/profile/ja.ZekmjekV.html
出版者
出版者 SOC BIOSCIENCE BIOENGINEERING JAPAN
引用
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
抄録
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)
ISSN
収録物識別子タイプ ISSN
収録物識別子 1389-1723
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA11307678
PubMed
識別子タイプ PMID
関連識別子 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search&DB=pubmed&term=22178339
関連名称 22178339
権利
権利情報 Copyright© 2011, The Society for Biotechnology, Japan.
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
WoS
URL http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=ShinshuUniv&SrcApp=ShinshuUniv&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000302505700004
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