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β-Glucosidase Involved in the Antioxidant Formation in Tempeh, Fermented Soybeans
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- EBATA Junko
- Faculty of the Science of Living, Osaka City University
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- FUKUDA Yasuko
- Faculty of the Science of Living, Osaka City University
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- HIRAI Kazuko
- Faculty of the Science of Living, Osaka City University
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- MURATA Kiku
- Faculty of the Science of Living, Osaka City University
Bibliographic Information
- Other Title
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- テンペイの抗酸化性物質の生成に関与するβ-グルコシダーゼ
- テンペイ ノ コウサンカセイ ブッシツ ノ セイセイ ニ カンヨ スル ベータ-グルコシダーゼ
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Description
The β-glucosidase involved in formation of antioxidants (some isoflavones) from fermented soybeans with Rhizopus oligosporus was investigated.<br> The results were as follows:<br> 1. Genistin was hydrolysed with the crude enzyme which was obtained by ammonium sulfate fractionation from water extract of Rhizopus oligosporus cultivated in the medium containing soybean paste. The reaction mixture showed antihemolytic activity corresponding to the proposed amount of its aglucone, 5, 7, 4'-trihydroxyisoflavone.<br> 2. The β-glucosidase was isolated by the purification procedures of acetone precipitation, Amberlite CG-50 column chromatography and concentration with collodion bag. The enzyme was purified about 1400 folds and the yield was 43%.<br> 3. The purified enzyme showed maximum activity at pH 5.0 and 60°C, and was stable between pH 2 and 9 at 20°C. The enzyme activity was markedly inhibited by heavy metal ions and SH reagents, and recovered by cysteine. The Km values of the enzyme were 6.25×10-5M for genistin, 1.98×10-4M for NPG, 4.57×10-4M for phenyl-β-D-glucoside and 6.72×10-4M for arbutin. Methyl-α-D-glucoside was not attacked by the enzyme.
Journal
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- Nippon Nōgeikagaku Kaishi
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Nippon Nōgeikagaku Kaishi 46 (7), 323-329, 1972
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390282679484112640
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- NII Article ID
- 130001222758
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- NII Book ID
- AN00196191
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- COI
- 1:CAS:528:DyaE3sXmvVKhsw%3D%3D
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- ISSN
- 18836844
- 00021407
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- NDL BIB ID
- 7622778
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL Search
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed