Purification and Some Properties of Agarase from Pseudomonas sp. PT-5(Biological Chemistry)
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概要
- 論文の詳細を見る
An agarase (agarose 4-glycanohydrolase, EC 3.2.1.81) was purified from the culture fluid of Pseudomonas sp. PT-5 by ammonium sulfate precipitation followed by Cellulofine GC-700m, Hydroxyapatite, Butyl-Toyopearl 650M, and Toyopearl-HW 508 column chromatography. The purified enzyme gave a single band on polyacrylamide gel disc electrophoresis and its molecular weight was 31, 000 by SDS-polyacrylamide gel electrophoresis. The isoelectric point of the enzyme was 3.6. The amino-terminal sequence was H・Ala-Asp-Trp-Asp-Gly-Leu-Ala-Val-Pro-Ala-Asp-Ala-Gly-Asp-Gly-. The enzyme was stable from pH 6 to 9 and had its maximum activity at pH 8.5. The enzyme rapidly reduced the viscosity of agarose solution and its activity was greatly inhibited by metal ions such as Zn^<2+>, Cu^<2+>, Co^<2+>, Fe^<2+>, and Al^<3+> at 1 mM concentration. The enzyme activity was elevated by 75% in the presence of 0.1 M NaCl.
- 社団法人日本農芸化学会の論文
- 1991-10-23
著者
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Yamaura Izumi
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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Funatsu Masaru
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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NATSUMOTO Toshihiko
Department of Applied Microbial Technology, The Kumamoto Institute of Technology
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SHIGEIRI Hisaji
Central Research Laboratory, Koasa Shoji Co., Ltd.
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SHIBATA Teruhiko
Central Research Laboratory, Koasa Shoji Co., Ltd.
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Shigeiri Hisaji
Central Research Laboratory Koasa Shoji Co. Ltd.
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Shibata Teruhiko
Central Research Laboratory Koasa Shoji Co. Ltd.
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Natsumoto Toshihiko
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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