| 海参自溶酶的分离纯化和部分性质研究 |
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| 引用本文： | 朱蓓薇,韩冰. 海参自溶酶的分离纯化和部分性质研究[J]. 食品与发酵工业, 2004, 30(4): 132-134,137 |
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| 作者姓名： | 朱蓓薇 韩冰 |
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| 作者单位： | 大连轻工业学院,大连,116034 |
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| 基金项目： | 大连市科技攻关项目 (No.2 0 0 3BINS1 2 3) |
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| 摘 要： | 采用硫酸铵分级盐析 ,Sephadex 1 0 0分子筛柱层析从新鲜海参肠中分离纯化海参自溶酶。研究发现 ,所纯化的酶为酸性蛋白酶 ,分子质量约为 68 5ku ;最适作用温度为 3 5℃ ,对热不稳定 ;酶的最适作用pH为 7 0 ;金属离子Pb2 + 、Hg2 + 、Cd2 + 、Mn2 + 对酶的活性有抑制作用 ;Zn2 + 、Mg2 + 、Cu2 +则对酶有不同程度的激活作用
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| 关 键 词： | 海参自溶酶 盐析 纯化 |
Characterization and Purification of Holothurians Autoenzyme |
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| Zhu Beiwei Han Bing. Characterization and Purification of Holothurians Autoenzyme[J]. Food and Fermentation Industries, 2004, 30(4): 132-134,137 |
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| Authors: | Zhu Beiwei Han Bing |
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| Abstract: | The holothurians autoenzyme from fresh holothurians had been purified by ammonium sulfate precipition and Sephadex 100 column chromatography The experiment result indicate that the enzyme was an acidic protease and its molecular weight is 68 5 ku, the optimal temperature and pH of the enzyme are 35℃ and 7 respectively The enzyme was not stable in heat and its catalytic activity is strongly inhibited by the metal ions Pb 2+ , Hg 2+ , Cd 2+ , Mn 2+ and is activated by Zn 2+ , Mg 2+ , Cu 2+ . |
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| Keywords: | holothurians autoenzyme ammonium sulfate precipition purification |
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