Purification and Properties of 5-Keto-D-Fructose Reductase from a Mutant Strain Derived from Corynebacterium sp.
スポンサーリンク
概要
- 論文の詳細を見る
5-Keto-D-fructose reductase was purified about 300-fold from a mutant strain derived from Corynebacterium sp sp. SHS 0007 (ATCC 31090). The enzyme appeared to be homogeneous by SDS-polyacrylamide gel electrophoresis. THe enzyme converted 5-keto-D-fructose to L-sorbose in the prosence of NADPH. The reduction did not occur in the presence of NADH. The reverse reaction was not observed. The molecular weight of the enzyme was estimated to be about 33,000 by gel filtration and SDS-polyacrylamide gel electrophoresis. The enzyme appeared to be monomeric. The optimum pH was 6.0-7.0 for the reductase. The K_m value (pH 7.0,30℃) of the enzyme for 5-keto-D-fructose was 5.9 mM. The enzyme was relatively inactive on 2,5-diketo-D-gluconate in the presence of NADPH.
- 社団法人日本生物工学会の論文
- 1989-03-25
著者
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Kobayashi K
Department Of Chemical And Biological Sciences Faculty Of Science Japan Women's University
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Kobayashi K
Laboratory Of Molecular Biotechnology Graduate School Of Biological & Agricultural Sciences Nago
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Kobayashi K
Shizuoka Univ. Shizuoka Jpn
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YAGI SHIGEO
Biotechnology Development, Department of Production, Shionogi & Co., Ltd.,
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KOBAYASHI KOBEI
Biotechnology Development, Department of Production, Shionogi & Co., Ltd.,
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SONOYAMA TAKAYASU
Biotechnology Development, Department of Production, Shionogi & Co., Ltd.,
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Yagi Shigeo
Bioprocess Program Process R&d Laboratories Shionogi & Co.ltd.
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Yagi Shigeo
Biotechnology Development Department Of Production Shionogi & Co. Ltd.
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Sonoyama Takayasu
Biotechnology Development Department Of Production Shionogi & Co. Ltd.
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