Purification and Characterization of a Carbohydrate:Acceptor Oxidoreductase from Paraconiothyrium sp. That Produces Lactobionic Acid Efficiently

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概要

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• A carbohydrate:acceptor oxidoreductase from Paraconiothyrium sp. was purified and characterized. The enzyme efficiently oxidized β-(1→4) linked sugars, such as lactose, xylobiose, and cellooligosaccharides. The enzyme also oxidized maltooligosaccharides, D-glucose, D-xylose, D-galactose, L-arabinose, and 6-deoxy-D-glucose. It specifically oxidized the β-anomer of lactose. Molecular oxygen and 2,6-dichlorophenol indophenol were reduced by the enzyme as electron acceptors. The Paraconiothyrium enzyme was identified as a carbohydrate:acceptor oxidoreductase according to its specificity for electron donors and acceptors, and its molecular properties, as well as the N-terminal amino acid sequence. Further comparison of the amino acid sequences of lactose oxidizing enzymes indicated that carbohydrate:acceptor oxidoreductases belong to the same group as glucooligosaccharide oxidase, while they differ from cellobiose dehydrogenases and cellobiose:quinone oxidoreductases.

著者

• Murakami Hiromi

  Osaka Municipal Technical Res. Inst.

• KISO TARO

  Osaka Municipal Technical Research Institute

• NAKANO HIROFUMI

  Osaka Municipal Technical Research Institute, and Yashiro Co, Ltd.,

• Kiso Taro

  Department Of Biochemistry Osaka Municipal Technical Research Institute

• KIRYU Takaaki

  Osaka Municipal Technical Research Institute

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