Purification and Characterization of Pectinesterase from Ficus awkeotsang(Biological Chemistry)
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概要
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A pectinesterase (EC 3.1.1.11) isolated from red tepals of Ficus awkeotsang was purified to a single band of protein on SDS-PAGE by column chromatography on QAE-Sephadex A-25, Q-Sepharose, hydroxylapatite, and Sephacryl S-200. The molecular weight of the enzyme was 42,000 by SDS-PAGE. The pi was 4.4. The purified enzyme activity was stimulated in the presence of low concentrations of metal ions, in the order of Ca^<2+>>Mg^<2+>>K^+>Na^+. The Km and V_<max> for awkeotsang polygalacturonide were 2.94 mg/ml, 66.67 μmol/min/mg protein at pH 5.4 in the absence of metal ion, and 2.78 mg/ml, 86.96μmol/min/mg protein at pH 7.5 in the presence of 50 mM KCI, respectively.
- 1990-06-23
著者
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KOMAE Kozo
Department of Wheat and Barley Research, National Institute of Crop Science
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SONE Yoshiaki
Department of Food and Nutrition, Graduate School of Osaka City University
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Misaki Akira
Department of Food and Nutrition, Faculty of Science of Living, Osaka City University
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Komae Kozo
Department Of Food And Nutrition Faculty Oj Science Of Living Osaka City University:(present Office)
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KAKUTA Mariko
Konan Women's College
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Misaki A
Osaka City Univ. Osaka Jpn
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Misaki Akira
Department Of Food And Nutrition Faculty Of Living Osaka City University
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Kakuta M
Konan Women's Univ. Kobe Jpn
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Kakuta Mariko
Konan Women's University
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Sone Y
Dep. Food & Nutrition Fac. Science Of Living Osaka City Univ.
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Sone Y
Osaka City Univ. Osaka Jpn
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Sone Yoshiaki
Department Of Food And Nutrition Faculty Of Human Life Science
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Komae K
National Agriculture Research Center Tsukuba Jpn
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Komae Kozo
Department Of Food And Nutrition Faculty Of Science Of Living Osaka City University
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Misaki Akira
Department Of Food And Nutrition Faculty Of Human Life Science Osaka City University
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