Purification and Characterization of an ε-Poly-L-Lysine-Degrading Enzyme from the ε-Poly-L-Lysine-Tolerant Chryseobacterium sp. OJ7 (ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
スポンサーリンク
概要
- 論文の詳細を見る
The ε-poly-L-lysine-degrading enzyme of the ε-poly-L-lysine-tolerant Chryseobacterium sp. OJ7 was purified and characterized. The bacterium excreted the enzyme into the culture filtrate. The purified enzyme has a molecular mass of approximately 38.4kDa and consists of two identical subunits with a molecular mass of 19.5kDa. The enzyme catalyzed the endo-type degradation of ε-poly-L-lysine. A correlation between the ε-poly-L-lysine tolerance of the bacterium and the high ε-poly-L-lysine-degrading activity was suggested.
- 公益社団法人日本生物工学会の論文
- 2003-07-25
著者
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Nagasawa Toru
Department of Biomolecular Science, Gifu University
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Nagasawa Toru
Department Of Biomolecular Science Gifu University
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Nagasawa Toru
Department Of Agricultural Chemistry Kyoto University
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Onji Yuichi
Yokohama Research Center Chisso Corporation
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KITO MITSUAKI
Department of Biomolecular Science, Gifu University
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TAKIMOTO RIKA
Department of Biomolecular Science, Gifu University
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YOSHIDA TOYOKAZAU
Department of Biomolecular Science, Gifu University
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Takimoto Rika
Department Of Biomolecular Science Gifu University
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Kito Mitsuaki
Department Of Biomolecular Science Gifu University
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Yoshida Toyokazau
Department Of Biomolecular Science Gifu University
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