Purification and Some Properties of α-Galactosidase from Candida guilliermondii H-404
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概要
- 論文の詳細を見る
Candida guilliermondii H-404, isolated from soil, produced thermostable α-galactosidase, but small amounts of other glycosidases (such as β-galactosidase, α-glucosidase, and β-glucosidase). The enzyme was separated into two fractions by DEAE-Toyopearl 650M chromatography, and the two enzymes were designated galactosidase I and II. These two enzymes had the same molecular weight (270,000 by gel filtration, 64,000 by SDS-PAGE). The isoelectric points of α-galactosidase I and II were 6.16 and 6.21, respectively. These two enzymes were different from each other in pH stability, temperature stability, and effects of Fe^<2+> and Cu^<2+> ion on α-galactosidase activity. The enzyme had stronger transfer activity and wider acceptor specificity than α-galactosidases which have been reported.
- 社団法人日本農芸化学会の論文
- 1993-03-23
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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Hashimoto H
Kyoto Inst. Technol. Kyoto Jpn
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HASHIMOTO Hiroyuki
Sugiyama Chemical and Industrial Laboratory
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