Properties of Maltose Phosphorylase from Propionibacterium freudenreichii
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概要
- 論文の詳細を見る
Maltose phosphorylase (EC 2.4.1.8) from Propionibacterium freudenreichii was purified and characterized. The enzyme catalyzed both the phosphorolysis and the synthesis of maltose. In particular, in the synthetic reaction, the enzyme could use any of nine sugars other than D-glucose as a sugar acceptor, which resulted in the formation of new disaccharides, in which the first carbon of D-glucose and the fourth carbon of the other sugar were connected by an α-glycosidic linkage.
- 社団法人日本生物工学会の論文
- 1996-08-25
著者
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Masuda Tomomi
Tokyo Research Laboratories Kyowa Hakko Kogyo Co.ltd.
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AISAKA KAZUO
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co.Ltd.
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CHIKAMUNE TADASHI
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co.Ltd.
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Aisaka K
Biofrontier Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Aisaka K
Japan Tobacco Inc. Osaka Jpn
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Aisaka Kazuo
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Chikamune Tadashi
Tokyo Research Laboratories Kyowa Hakko Kogyo Co.ltd.
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