【作者】 邱业先； 马丽； 汪金莲； 杨进军； 杜天真；

【Author】 qiu yexian, Mali,Wangjinlian, Yangjinjian ,Tu Tianzhen(zhong kai Agrotechnical college ,Guangzhou 510225: jiong xi Agricuture university Nachang 330045 Tianjing university of scienceand Technology,Tianjing300191)

【机构】 仲恺农业技术学院； 江西农业大学林学院； 天津理工学院环境科学与安全工程；

【摘要】 采用Sephadex A-50,Sephadex G-200柱层析的方法,从槭树科槭树属元宝枫(AcertruncatumBunge)的叶片中提取并纯化了叶蛋白酶.酶的纯化程度达到1408.04U/mg蛋白,纯化倍数为50.77.对该酶的理化性质进行研究表明,该酶以酪蛋白为底物时,最适PH为7.5,最适温度为60℃;抗酸碱性能试验表明,该酶在PH5.0-10.0范围内稳定,热稳定性试验表明,该酶在60℃以下较为稳定.该酶具有巯基蛋白酶的特性,能被半胱氨酸和EDTA激活,而被HgCl2抑制.更多还原

【Abstract】 A protease purified from the fresh leaves of Acer truncatum Bunge by means of Sephadex A-50, Sephadex G-200 column chromatography.The puration exhibited 1408.04U/mg protein,the purification times was 50.77.The study on its physicochemical properties showed that the optimal PH of the enzyme for casein was about 7.5,and the optimal temperature was about 60℃.It was relatively stable at the PH ranging from 5.0 to 10.0 and at the temperature below 50℃ .The emzyme had the properties of mercaptoproteinase.lt could be activated by Cysteine and EDTA,but inhibited by HgCl2.更多还原