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

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書誌事項

タイトル別名
  • Purification and Characterization of a Carbohydrate:Acceptor Oxidoreductase from Paraconiothyrium sp. That Produces Lactobionic Acid Efficiently
公開日
2008
DOI
  • 10.1271/bbb.70701
公開者
公益社団法人 日本農芸化学会

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説明

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.

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