Purification and Some Properties of an Endo-1,4-β-D-mannanase from a Marine Mollusc,Littorina brevicula
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概要
- 論文の詳細を見る
An endo-1,4-β-D-mannanase (EC 3.2.1.78) was purified from viscera of a marine mollusc, Littorina brevicula. The purified enzyme, with a molecular weight of 42,000, was homogeneous by SDS-PAGE. The amino-terminal sequence starting with Gly was analyzed up to the 30th amino acid. The enzyme was stable from pH about 4.0 to about 9.0 and had its maximum activity at pH about 6.5. The purified enzyme produced M2, M3, M4, and M5 from Codium β-1,4-mannan. The enzyme activity was greatly inhibited by Ag^+, Hg^<2+>, Cu^<2+> , and N-bromosuccinimide at 1 mM concentration.
- 社団法人日本農芸化学会の論文
- 1996-04-23
著者
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YAMAZAKI Isao
Yayoi Kagaku Kogyo Co., Ltd.
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KATO Tetsuo
Department of Applied Microbial Technology, Kumamoto Institute of Technology
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NOZAKI Yuji
Department of Nephrology and Rheumatology, Kinki University Faculty of Medicine
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Kato T
Food Research Institute Aichi Prefectural Government
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MATSUMOTO Toshihiko
Department of Applied Microbial Technology, Kumamoto Institute of Technology
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YAMAURA Izumi
Department of Applied Microbial Technology, Kumamoto Institute of Technology
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Matsumoto T
Applied Biological Chemistry University Of Tokyo
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Kato T
Shizuoka Univ. Shizuoka Jpn
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Nozaki Yuji
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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Yamaura I
Yayoi Kagaku Kogyo Co. Ltd.
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Yamaura Izumi
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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Yamazaki Isao
Yayoi Kagaku Kogyo Co. Ltd. Fukuoka-machi
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Matsumoto Toshihiko
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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Yamaura I
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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