Purification and Characterization of Soymilk-clotting Enzymes from Bacillus sp. K-295G-7
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概要
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Enzymes I and II, which have a high soymilk-clotting activity, produced from K-295G-7 were purified by chromatographies on Sephadex G-100, CM-cellulose, hydroxylapatite, and 2nd Sephadex G-100. The two purified enzymes were found to be homogeneous by polyacrylamide gel electrophoresis (PAGE) at pH 4.3. The molecular weights of enzymes I and II were 28, 000 and 29, 500 by SDS-PAGE, and their isoelectric points were 9.22 and 9.45, respectively. Enzymes I and II coagulated soymilk optimally at 65°C and were stable up to 45°C. Both enzymes were most active at pH 5.8, for soymilk coagulation between pH 5.8 to 6.7, and were stable with about 50-100% of the original activity from pH 5 to 10. Each of the purified enzymes was a serine protease with an optimum pH of 9.0 for soy protein isolate (SPI) and casein digestions, because these enzymes were inhibited completely by diisopropylfluoro-phosphate (DFP). The soymilk-clotting activity to proteolytic activity ratio of the enzyme II was 3 times higher than that of enzyme I. Enzymes I and II were more sensitive to the calcium ion concentration in soymilk than bromelain is.
- 社団法人 日本農芸化学会の論文
著者
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Murakami K
Research And Development Department Kibun Food Chemifa Co. Ltd.
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Kusakabe Isao
Institute of Applied Biochemistry, University of Tsukuba
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Murakami Kazuo
Institute of Applied Biochemistry, University of Tsukuba
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PARK Yang
Institute of Applied Biochemistry, University of Tsukuba
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KOBAYASHI Hideyuki
Institute of Applied Biochemistry, University of Tsukuba
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Park Yang
Institute Of Applied Biochemistry University Of Tsukuba
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Kusakabe Isao
Institute Of Applied Biochemistry University Of Tsukuba
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Murakami Kazuo
Institute Of Applied Biochemistry University Of Tsukuba
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Kobayashi Hideyuki
Institute Of Applied Biochemistry The University Of Tsukuba
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