元宝枫叶蛋白酶的动力学特征  

Study on kinetic characteristics ofprotease from Acer truncatum Bunge

作　　者：马丽[1] 邱业先[2] 杜天真[3] 

机构地区：[1]安徽工业大学化学化工学院,安徽马鞍山243002 [2]仲恺农业技术学院,广东广州510225 [3]江西农业大学,江西南昌330045

出　　处：《植物资源与环境学报》2006年第1期70-71,共2页Journal of Plant Resources and Environment

基　　金：国家自然科学基金(30060010);江西省自然科学基金(0030032)资助项目

摘　　要：Using casein as a substrate,the kinetic characteristics of protease from Acer truncatum Bunge leaf was studied.Michaelis-Menten constant(Km) and the maximal reaction rate(Vmax) of the protease were determined under different temperatures(40℃-80℃) and different pH values(pH 6.5-pH 8.5).The results indicated that the Km decreased and the Vmax increased when temperature increased from 40℃ to 80℃.The Km decreased and Vmax increased with pH values rising from pH 6.5 to pH 7.5,but the Km increased and Vmax decreased with pH values rising from pH 7.5 to pH 8.5.The results show that the proper pH of enzymatic reaction of the protease is pH 7.5.Using casein as a substrate, the kinetic characteristics of protease from Acer truncatum Bunge leaf was studied. Michaelis-Menten constant （Km） and the maximal reaction rate （Vmax） of the protease were determined under different temperatures （40% - 80% ） and different pH values （ pH 6. 5 - pH 8.5 ）. The results indicated that the Km decreased and the Vmax increased when temperature increased from 40℃to 80℃. The Km decreased and Vmax increased with pH values rising from pH 6.5 to pH 7.5, but the Km increased and Vmax decreased with pH values rising from pH 7.5 to pH 8.5. The results show that the proper pH of enzymatic reaction of the protease is pH 7.5.

关 键 词：元宝枫 蛋白酶 酶动力学 

分 类 号：Q949.755.3[生物学—植物学] Q946.5