| 斑点叉尾鮰鱼肠蛋白酶的分离纯化及其酶学性质 |
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| 引用本文： | 黄丽洋,丁建君,姜山,杨杰,陈炜,胡建恩. 斑点叉尾鮰鱼肠蛋白酶的分离纯化及其酶学性质[J]. 大连水产学院学报, 2012, 27(1): 83-85 |
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| 作者姓名： | 黄丽洋 丁建君 姜山 杨杰 陈炜 胡建恩 |
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| 作者单位： | 大连海洋大学食品科学与工程学院,辽宁大连,116023 |
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| 摘 要： | 以斑点叉尾鮰Ictalurus punctatus鱼肠道为原料提取蛋白酶,对分离条件进行了优化,并对部分酶学性质进行了研究。结果表明：鱼肠内的蛋白酶在硫酸铵饱和度为70%时,所得沉淀中酶活力最高。经过阴离子交换层析分离后,蛋白酶的纯化倍数达到了218倍。该蛋白酶的最适温度为55℃,最适pH为7.5,具有良好的低温稳定性和酸碱稳定性,米氏常数为5.4 g/L。K^＋和Ca^2＋离子对该蛋白酶活性有较弱的激活作用,Mg^2＋则能显著激活蛋白酶活性;Na＋和Zn2＋对蛋白酶的活性有较弱抑制作用,而Cu^2＋和EDTA能显著抑制蛋白酶活性。
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| 关 键 词： | 斑点叉尾鮰 鱼肠 蛋白酶 分离纯化 |
Purification and characterization of protease from intestines of Ictalurus punctatus |
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| HUANG Li-yang , DING Jian-jun , JIANG Shan , YANG Jie , CHEN Wei , HU Jian-en. Purification and characterization of protease from intestines of Ictalurus punctatus[J]. Journal of Dalian Fisheries University, 2012, 27(1): 83-85 |
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| Authors: | HUANG Li-yang DING Jian-jun JIANG Shan YANG Jie CHEN Wei HU Jian-en |
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| Affiliation: | (College of Food Science and Engineering, Oalian Ocean University, Dalian 116023, China) |
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| Abstract: | The paper studies purification and characterization of protease from intestines of Ictalurus punctatus.The result demonstrates that protease has the maximum activity with 70% saturation（NH4）2SO4 in crude extraction solution.By using ion exchange chromatography,protease is purified 218-fold.It further shows that the optimal temperature and pH is 55 ℃ and 7.5 respectively for protease with optimal stability,and that Michaelis constant is 5.4 g/L.K^＋,Mg^2＋and Ca^2＋ may enhance protease activity.Na^＋,Zn^2＋,Cu^2＋ and EDTA may reduce protease activity. |
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| Keywords: | Ictalurus punctatus intestine protease purification |
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