Characterization and Kinetics of 45 kDa Chitosanase from<i>Bacillus</i>sp. P16
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- JO You-Young
- <i>Department of Agricultural Chemistry, Chonnam National University</i> Present address: <i>Department of Biological Science, Institute of Bioscience and Biotechnology, Myong Ji University</i>
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- JO Kyu-Jong
- <i>Department of Agricultural Chemistry, Chonnam National University</i>
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- JIN Yu-Lan
- <i>Department of Agricultural Chemistry, Chonnam National University</i>
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- KIM Kil-Yong
- <i>Department of Agricultural Chemistry, Chonnam National University</i> <i>Institute of Agricultural Science and Technology, Chonnam National University</i>
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- SHIM Jae-Han
- <i>Department of Agricultural Chemistry, Chonnam National University</i> <i>Institute of Agricultural Science and Technology, Chonnam National University</i>
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- KIM Yong-Woong
- <i>Department of Agricultural Chemistry, Chonnam National University</i>
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- PARK Ro-Dong
- <i>Department of Agricultural Chemistry, Chonnam National University</i> <i>Institute of Agricultural Science and Technology, Chonnam National University</i>
書誌事項
- タイトル別名
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- Characterization and Kinetics of 45 kDa Chitosanase from Bacillus sp. P16
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説明
An extracellular 45 kDa endochitosanase was purified and characterized from the culture supernatant of Bacillus sp. P16. The purified enzyme showed an optimum pH of 5.5 and optimum temperature of 60°C, and was stable between pH 4.5-10.0 and under 50°C. The Km and Vmax were measured with a chitosan of a D.A. of 20.2% as 0.52 mg/ml and 7.71×10−6 mol/sec/mg protein, respectively. The enzyme did not degrade chitin, cellulose, or starch. The chitosanase digested partially N-acetylated chitosans, with maximum activity for 15-30% and lesser activity for 0-15% acetylated chitosan. The chitosanase rapidly reduced the viscosity of chitosan solutions at a very early stage of reaction, suggesting the endotype of cleavage in polymeric chitosan chains. The chitosanase hydrolyzed (GlcN)7 in an endo-splitting manner producing a mixture of (GlcN)2-5. Time course studies showed a decrease in the rate of substrate degradation from (GlcN)7 to (GlcN)6 to (GlcN)5, as indicated by the apparent first order rate constants, k1 values, of 4.98×10−4, 2.3×10−4, and 9.3×10−6 sec−1, respectively. The enzyme hardly catalyzed degradation of chitooligomers smaller than the pentamer.<br>
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 67 (9), 1875-1882, 2003
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206475199232
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- NII論文ID
- 110002694321
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 6697925
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- PubMed
- 14519970
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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
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- 使用不可