Purification and Some Properties of an Erythrose Reductase from an Aureobasidium sp. Mutant
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概要
- 論文の詳細を見る
An erythrose reductase was obtained from the cells of an Aureobasidium sp. mutant having high erythritol-producing activity. This enzyme was purified 600-fold over the cell-free extract by ammonium sulfate precipitation, ion exchange chromatography, affinity chromatography, and hydrophobic chromatography. It gave a single band on polyacrylamide gel electrophoresis, and had a molecular weight of 37,000 and an isoelectric point of 4.8. This enzyme had maximum reductive activity at 45℃ and pH 6.5. The optimum pH of the oxidative reaction was 9.5. It was stable at pH 6.0-8.0 and below 40℃. The enzyme showed the maximum activity to D-erythrose. D-Glyceraldehyde was reduced at a rate 66% of that for D-erythrose. p-Nitrobenzaldehyde, L-erythrulose, dihydroxyacetone, and D-glucuronate were also reduced, although at shower rates. The oxidative activity was less than 0.1% of the reductive one.
- 社団法人日本農芸化学会の論文
- 1992-06-23
著者
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Sasaki Takashi
National Food Research Institute
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Taniguchi Hajime
National Food Research Institute
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Ishizuka H
Nikken Chemicals Co. Ltd.
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ISHIZUKA Hiroaki
Nikken Chemicals Co., Ltd.
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Taniguchi Hajime
National Food Research Institute Ministry Of Agriculture Forestry And Fisheries
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Sasaki Takashi
National Food Research Institute Ministry Of Agriculture Forestry And Fisheries
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Taniguchi Hajime
National Food Research Insitute, Ministry of Agricultuer, Forestry and Fisheries
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SASAKI Takashi
National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries
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