2024年7月21日 星期日
元宝枫蛋白酶的分离纯化及其生化性质
Isolation and biochemical properties of a protease from Acer truncatum Bunge
2005年 第14卷 第1期 页码[6-9]    下载全文[0.5MB]  
摘要

采用有机溶剂沉淀和柱层析方法,从元宝枫(Ace rtruncatum Bunge)叶片中提取并纯化了叶蛋白酶。该蛋白酶的比活性为 1408. 04U·mg-1,纯化倍数 50.77。以酪蛋白为底物时,该蛋白酶最适pH 7.5,最适温度 60℃;该蛋白酶在pH5.0~pH10.0范围内以及在 60℃以下较为稳定。该酶的活力能被半胱氨酸和EDTA激活,但受HgCl2抑制,具有巯基蛋白酶的特性。

Abstract

A protease was extracted and purified from the fresh leaves of Acer truncatum Bunge by means of Sephadex A-50, Sephadex G-200 column chromatography. The specific activity of the protease was 1408.04U·mg-1, the purification times was 50.77. The optimal pH value of the protease taking casein as a substrate was about pH 7.5, and the optimal temperature 60℃ .It was relatively stableat the ranging from pH 5.0 to pH 10.0 and at the temperature below 60℃ . The protease has the properties of mercaptoproteinase, it could be activated by cysteine and EDTA, but inhibited by HgCl2.

关键词元宝枫蛋白酶; 酶活力; 最适pH; 最适温度; 抑制剂;
Key wordsAcer truncatum Bunge protease; enzyme activity; optimalp H; optimal temperature; inhibiter
作者马丽1,邱业先2,杨进军3,杜天真4
所在单位1.安徽工业大学,安徽马鞍山243002;
2.仲恺农业技术学院,广东广州510225;
3.天津理工学院,天津300191;
4.江西农业大学,江西南昌330045
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基金项目国家自然科学基金 ( 30060010 ); 江西省自然科学基金(0030032)资助项目;