Purification and Characterization of a Carbohydrate : Acceptor Oxidoreductase from Paraconiothyrium sp. That Produces Lactobionic Acid Efficiently
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概要
- 論文の詳細を見る
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.
- 社団法人 日本農芸化学会の論文
- 2008-03-23
著者
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Murakami Hiromi
Osaka Municipal Technical Res. Inst.
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KISO TARO
Osaka Municipal Technical Research Institute
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Murakami H
Laboratory Of Cellular Regulation Technology Graduate School Of Genetic Resources Technology Kyushu
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NAKANO HIROFUMI
Osaka Municipal Technical Research Institute, and Yashiro Co, Ltd.,
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Kiso Taro
Department Of Biochemistry Osaka Municipal Technical Research Institute
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Murakami H
Osaka Municipal Technical Res. Inst.
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KIRYU Takaaki
Osaka Municipal Technical Research Institute
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Nakano H
Department Of Biochemistry Osaka Municipal Technical Research Institute
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Nakano H
Kyoto Prefectural Univ. Kyoto Jpn
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Nakano Hirofumi
Osaka Municipal Technical Research Institute
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Nakano Hirofumi
Department Of Chemistry Faculty Of Science Osaka University
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Kiryu Takaaki
Osaka Municipal Technical Res. Inst.
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