草鱼卵中蛋白酶抑制剂的初步分离及性质研究 |
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引用本文: | 郭强,王亮亮,张业妹,顾婷婷,韩曜平.草鱼卵中蛋白酶抑制剂的初步分离及性质研究[J].安徽农业科学,2012,40(26):12899-12902. |
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作者姓名: | 郭强 王亮亮 张业妹 顾婷婷 韩曜平 |
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作者单位: | 苏州大学基础医学与生物科学学院,江苏苏州215123;常熟理工学院生物与食品工程学院,江苏常熟215500;常熟理工学院生物与食品工程学院,江苏常熟,215500 |
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摘 要: | 目的]草鱼卵匀浆液中纯化获得蛋白酶抑制剂。方法]采用Sephadex凝胶层析技术和发色底物检测,经分离与纯化获得具有专一性抑制活性的蛋白酶抑制剂。在不同温度(30~100℃)和酸碱(pH 2~11)条件下研究该抑制剂稳定性。结果]从草鱼卵中分离到表观分子量50 kD的蛋白酶抑制剂,其对胰蛋白酶的最低抑制浓度约为500μg/ml,抑制常数为14.6 nmol/L。该蛋白酶抑制剂还具有高度的热稳定和酸碱稳定性。结论]该研究可为淡水鱼卵的高效利用提供理论依据。
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关 键 词: | 蛋白酶抑制剂 抑制活性 热稳定性 酸碱稳定性 |
Purification and Characteristics of a Trypsin Inhibitor from Ctenopharyngodon idellus Eggs |
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Institution: | GUO Qiang et al(School of Biology and Basic Medical Sciences,Soochow University,Suzhou,Jiangsu 215123) |
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Abstract: | Objective] To obtain a protease inhibitor from eggs of Ctenopharyngodon idellus.Method] By gel filtration chromatography and chromogenic substrate detection,a protease inhibitor which has specific inhibitory activity was obtained,and then its stability was studied through the change of temperature(30-100 ℃) and acid-base(pH 2-11) conditions.Result] The purified inhibitor showed an apparent molecular weight of 50 kDa,and it potently inhibited trypsin with minimum inhibitory concentration of 500 μg/ml and a Ki value of 14.6 nmol/L,and also with a high degree of thermal stability and acid-base stability.Conclusion] This study provides a theoretical basis for the efficient use of freshwater fish eggs. |
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Keywords: | Proteinase inhibitor Inhibitory activity Thermal stability Acid-base stability |
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