WEKO3
アイテム
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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. 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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. 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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/10091/16192aad1b2ca-1af6-4626-bc9c-53a743d3ce83
名前 / ファイル | ライセンス | アクション |
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Isolation_Genes_Coding_Chitin-Degrading_Enzymes.pdf (2.3 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2013-01-18 | |||||
タイトル | ||||||
言語 | en | |||||
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 | ||||||
識別子タイプ | 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× 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 | ||||||
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 | ||||||
内容記述タイプ | Other | |||||
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 | ||||||
内容記述タイプ | Abstract | |||||
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) | ||||||
内容記述タイプ | Other | |||||
内容記述 | Article | |||||
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 | ||||||
表示名 | Web of Science | |||||
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