Purification and Characteristics of .BETA.-Galactosidase from Alternaria alternate.
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- KIKUCHI Toshihiko
- Showa Wemen's University
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- ISHIWATA Naoko
- Showa Wemen's University
Bibliographic Information
- Other Title
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- Alternaria alternateβ‐ガラクトシダーゼの精製とその酵素特性
Abstract
Alternaria alternate β-galactosidase was purified and its characteristics were examined. Water extract of crude enzyme obtained from wheat bran culture was purified by salting-out of ammonium sulfate, and by column chromatographies of Sephacryl S-200, DEAETOYOPEARL 650M and Hydroxyapatite. At the final stage, the enzyme was purified to 174-fold activity in comparison with its crude extract and shown unique activity band. Its character were followings; molecular weight was 125000, optimum reaction pH was 4.0-4.5 for ONPG and 5.0-5.5 for lactose, and its stability was kept in the pH range 4.0-8.5. Optimum reaction temperature was about 60°C and heat stability was below 55°C in 1 hour. Km values were indicated respectively 1.56mM for ONPG and 13.9mM for lactose. Inhibitory actions were not observed in the tested reagents.
Journal
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- NIPPON SHOKUHIN KOGYO GAKKAISHI
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NIPPON SHOKUHIN KOGYO GAKKAISHI 39 (11), 1023-1029, 1992
Japanese Society for Food Science and Technology
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Details 詳細情報について
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- CRID
- 1390001206406814720
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- NII Article ID
- 130003967937
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- ISSN
- 00290394
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- Text Lang
- ja
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- Data Source
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- JaLC
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed