食品工业科技Issue(12)：103-105,109,4.
mPEG-SS修饰对DHPM去折叠胰蛋白酶相对活性、热稳定性和动力学参数的影响
Effect of mPEG-SS modification on relative activity,thermal stability and kinetic parameters of DHPM unfolding trypsin
摘要
Abstract
DHPM unfolding trypsin was modified by mPEG-SS. The relative activity,thermal stability and kinetic parameters（Km, Vmax）of trypsin were measured. Results showed that mPEG - SS modification did not change the relative activities of native and DHPM unfolding trypsin. mPEG-SS modification enhanced the thermal stability of unfolded trypsin more obviously than native trypsin. When incubated at 55℃ or incubated at 45℃ 180min,the values of mPEG-SS modification enhancing the relative activity of native and unfolded trypsin were 2%,7% and 19%,30% respectively. The Km and Vmax of native and unfolded trypsin modified by mPEG-SS were 4. 67,3. 24mg/mL and 0. 042,0. 034U/min respectively,which were lower than native and unfolded trypsin. The Km of unfolded trypsin modified by mPEG-SS was lower than native trypsin modified by mPEG-SS,which meant that the former would affine casein easier than later.关键词
胰蛋白酶/mPEG-SS/相对活性/热稳定性/动力学参数Key words
trypsin/mPEG-SS/relative activity/thermal stability/kinetic parameters分类
轻工纺织引用本文复制引用
邹立强,刘伟,刘军平,刘成梅..mPEG-SS修饰对DHPM去折叠胰蛋白酶相对活性、热稳定性和动力学参数的影响[J].食品工业科技,2011,(12):103-105,109,4.基金项目
国家自然科学基金项目 （）
国家重点实验室重点青年骨干研究基金 （）
