Purification, Cloning, and Sequence Analysis of β-N-Acetylglucosaminidase from the Chitinolytic Bacterium Aeromonas hydrophila Strain SUWA-9
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- LAN Xiqian
- Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University
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- OZAWA Naomi
- Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University
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- NISHIWAKI Naohide
- Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University
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- KODAIRA Ritsuko
- Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University
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- OKAZAKI Mitsuo
- Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University
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- SHIMOSAKA Makoto
- Department of Applied Biology, Faculty of Textile Science and Technology, Shinshu University
書誌事項
- タイトル別名
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- Purification, Cloning, and Sequence Analysis of .BETA.-N-Acetylglucosaminidase from the Chitinolytic Bacterium Aeromonas hydrophila Strain SUWA-9
- Purification Cloning and Sequence Analysis of ベータ N Acetylglucosaminidase from the Chitinolytic Bacterium Aeromonas hydrophila Strain SUWA 9
- Purification, Cloning, and Sequence Analysis of β-<i>N</i>-Acetylglucosaminidase from the Chitinolytic Bacterium<i>Aeromonas hydrophila</i>Strain SUWA-9
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抄録
A chitinolytic bacterium was isolated from Lake Suwa and identified as Aeromonas hydrophila strain SUWA-9. The strain grew well on a synthetic medium containing colloidal chitin as sole carbon source. Chitin-degrading activity was induced by colloidal chitin or N-acetylglucosamine (GlcNAc). Most of the activity, however, was not detected in culture fluid but was associated with cells. A β-N-acetylglucosaminidase was purified after it was solubilized from cells by sonication. The purified enzyme hydrolyzed N-acetylchitooligomers from dimer to pentamer and produced GlcNAc as a final product. The enzyme also hydrolyzed synthetic substrates such as p-nitrophenyl (pNP)-N-acetyl-β-D-glucosaminide and pNP-N-acetyl-β-D-galactosaminide. A gene coding for the purified β-N-acetylglucosaminidase was isolated. The ORF identified is 2,661 nucleotides long and encodes a precursor protein of 887 amino acids including a signal peptide of 22 amino acid residues. The amino acid sequence deduced showed a high similarity to those of bacterial β-N-acetylhexosaminidases classified in family 20 of glycosyl hydrolases.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 68 (5), 1082-1090, 2004
公益社団法人 日本農芸化学会
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詳細情報
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- CRID
- 1390001206473923072
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- NII論文ID
- 10013144750
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
- http://id.crossref.org/issn/00032697
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- NDL書誌ID
- 6957467
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- PubMed
- 15170113
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可