Purification and Characterization, of Rice Bran Lipase II
Purification and Characterization, of Rice Bran Lipase II
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DOI：
10.1080/00021369.1976.10862049
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发表时间：
1976-02
期刊：
影响因子：
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通讯作者：
Y. Aizono;M. Funatsu;Y. Fujiki;M. Watanabe
中科院分区：
文献类型：
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作者：
Y. Aizono;M. Funatsu;Y. Fujiki;M. Watanabe
通过硫酸铵沉淀纯化一种米糠脂肪酶（脂肪酶 II），然后在 DEAE-纤维素、Sephadex G-75 和 CH-Sephadex C-50 上进行连续色谱分析。聚丙烯酰胺圆盘电泳和超速离心均证明酶蛋白是均质的。双酚电泳检测该酶的等电点为9.10。根据Archbald法测得该酶的沉降系数为2.60S，分子量为33,300。该酶的最适pH值在7.5至8.0之间，最适温度约为27°C。它在 pH 值 5 至 9.5 范围内以及低于 30°C 时保持稳定。在底物特异性方面，该酶对具有短碳链脂肪酸的甘油三酯表现出高特异性，尽管它能够水解大米和橄榄油中的酯键。
A species of rice bran lipase (lipase II) was purified by ammonium sulfate precipitation, followed by successive chromatographies on DEAE-cellulose, Sephadex G–75 and CH-Sephadex C–50. Both polyacrylamide disc electrophoresis and ultracentrifugation demonstrated that the enzyme protein is homogeneous. The isoelectric point of the enzyme was 9.10 by ampholine electrophoresis. The sedimentation coefficient of the enzyme was evaluated to be 2.60 S, and the molecular weight to be 33,300 according to Archbald’s method. The enzyme showed the optimum pH between 7.5 and 8.0, and the optimum temperature at about 27°C. It was stable over the pH range from 5 to 9.5 and below 30°C. In substrate specificity, the enzyme exhibited a high specificity toward triglycerides having short-carbon chain fatty acids, although it was capable of hydrolyzing the ester bonds in the rice and olive oil.