毛霉蛋白酶的催化特性及动力学研究  

Catalytic and kinetic properties of one protease from Mucor

作　　者：潘进权[1] 

机构地区：[1]湛江师范学院生命科学与技术学院,湛江524048

出　　处：《食品科技》2010年第11期36-40,共5页Food Science and Technology

基　　金：广东省自然科学基金项目(9452404801001943)

摘　　要：从雅致放射毛霉胞外分离纯化出一蛋白酶组分,以酪蛋白为底物对其催化特性及动力学进行了分析。结果表明:该蛋白酶组分是一种碱性丝氨酸蛋白酶;在pH8.5～9.5、60℃具有最大催化活性,在pH6～9和低于45℃具有很好的稳定性;在40℃该蛋白酶水解酪蛋白的反应符合米氏方程:V=(22.85/S+8.857);在4～45℃的范围内,该蛋白酶水解酪蛋白反应的活化能Ea为44.09kJ;该蛋白酶在50℃不稳定,其热失活规律符合一级指数衰减动力学模型:a=exp(-0.218t)。One protease was purified from extracellular of Actinomucor elegans AS3.2778 and its catalytic and kinetic properties were also investigated.The results show that the purified protease was one alkaline serine protease,which has relatively higher activity at pH8.5～9.5 and 60 ℃,and is stable at pH6.0~9.0 at 45 ℃.At 40 ℃,the kinetics of casein hydrolysis by the protease fit the Mchaelis-Mentonequation： V=（22.85/S＋8.857）,and the energy of activation（Ea） of this hydrolysis reaction below 45 ℃ is 44.09 kJ.The protease was unstable at 50 ℃,and the kinetics of deactivation fit the model： a=exp（-0.218t）.

关 键 词：雅致放射毛霉 蛋白酶 催化特性 动力学 

分 类 号：TS201.2[轻工技术与工程—食品科学]