Transgalactosylation Catalyzed by α-Galactosidase from Candida guilliermondii H-404
スポンサーリンク
概要
- 論文の詳細を見る
The thermostable α-galactosidase from Candida guilliermondii H-404 synthesized self transfer products in the absence of a suitable acceptor. The main self transfer product, using melibiose as a donor substrate, was O-α-D-galactosyl-(1, 6)-O-α-D-galactosyl-(1, 6)-D-glucose. This enzyme had a wide acceptor specificity. D-Glucose, D-galactose, maltose, maltitol, and 1, 4-butandiol were the most effective acceptors in the transgalactosylation catalyzed by this enzyme. The enzyme could also transfer α-galactosyl residues to pentoses (L-arabinose, D-xylose, and D-ribose) and methyl pentoses (D-fucose and L-rhamnose). The main transfer products to lactose, maltose, and sucrose as acceptors were identified as O-α-D-galactosyl-(1, 6)-O-β-D-galactosyl-(1, 4)-D-glucose, O-α-D-galactosyl-(1, 6)-O-α-D-glucosyl-(1, 4)-D-glucose, and O-α-D-ga-lactosyl-(1, 6)-O-α-D-glucosyl-(1, 2)-β-D-fructoside (raffinose), respectively.
- 社団法人日本農芸化学会の論文
- 1995-04-23
著者
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Goto Machio
Hitachi Instrument Engineering Co. Ltd.
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Goto M
Mie Univ. Tsu Jpn
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KITAHATA Sumio
Osaka Municipal Technical Research Institute
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Kitahata S
Department Of Bioscience And Biotecnology Shinshu University
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Hashimoto Hiroyuki
Sugiyama Chemical and lndustrial Laboratory
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Katayama Chie
Honen Corporation
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Goto Masaru
Honen Corporation
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Okinaga Tatsuyuki
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of.Technology
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Hashimoto H
Kyoto Inst. Technol. Kyoto Jpn
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Okinaga Tatsuyuki
Department Of Life Science Faculty Of Bioscience And Biotechnology Tokyo Institute Of Technology
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HASHIMOTO Hiroyuki
Sugiyama Chemical and Industrial Laboratory
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