Purification and Some Properties of Trehalase from Chatomium aureum MS-27
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概要
- 論文の詳細を見る
The trehalase of Chaetomium aureum was purified about 196-fold with a yield of 51% from the culture filtrate by ammonium sulfate fractionation, DEAE-collulose column chromatography, acetone fractionation, and Sephadex G-100 gel filtration. The enzyme preparation was homogeneous on disc electrophoresis. The enzyme was most active at pH 4.0 and 50℃. The enzyme was stable from pH 4.0 to 9.0 on 12h incubation at 37℃. The molecular weight of the enzyme was estimated to be 450,000 by gel feltarion on a column of Sepharose 6B, and 115,000 by SDS polyacrylamide gel electrophoresis. This indicated that the enzyme might consist of 4 subunits. The isoelectrec point of the enzyme was pH 4.0. The enzyme was active specifically on trehalose and not active on the other disaccharides tested.
- 公益社団法人日本生物工学会の論文
- 1989-02-25
著者
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Murao S
Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology
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Arai Motoo
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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SUMIDA MITSUO
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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OGURA SEI
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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MIYATA SHIGEKAZU
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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MURAO SAWAO
(Present address)Kumamoto Institute of Technology
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Ogura Sei
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Miyata Shigekazu
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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