Purification and Some Properties of Endo-1,4-β-D-mannanase from a Mud Snail, Pomacea insularus (de Ordigny)
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概要
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Endo-1, 4-β-D-mannanase (1, 4-β-D-mannanohydrolase, EC 3.2.1.78) was purified from viscera of a mud snail, Pomacea insularus (de Ordigny). The purified enzyme gave a single protein band in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight of the purified enzyme was estimated to be 44,000. The amino-terminal sequence was H・Gly-X-Leu-Arg-Arg-Gln-Gly-Thr-Asn-Ile-Val-Asp-Ser-His-Gly-His-Lys-Val-Phe-Leu-Ser-Gly-Ala-Asn-Thr-Ala-Trp-Val-Ala-Tyr-Gly-Tyr-Asp-. The enzyme was stable from pH about 5.0 to about 10.5 and had its maximum activity at pH about 5.5. The purified enzyme produced M2, M3, M4, and M5 from β-1, 4-mannan. Enzyme activity was greatly inhibited by Ag^+, Hg^<2+>, Cu^<2+> , and dithiothreitol at 1 mM concentration. In addition, N-bromosuccinimide completely inhibited the enzyme activity.
- 社団法人日本農芸化学会の論文
- 1993-08-23
著者
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YAMAZAKI Isao
Yayoi Kagaku Kogyo Co., Ltd.
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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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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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