陕西师范大学学报：自然科学版2011，Vol.39Issue(6)：49-53,5.
氯过氧化物酶的化学修饰及其在溶液中结构与催化性能的关系
The chemical modification of chloroperoxidase and the relationship between its structure and function in solution
摘要
Abstract
Chloroperoxidase（CPO） was modified by TMA and PMDA.Compared to native CPO,the chlorinated activity increased by 54% and 34% respectiviely,the thermostability and the tolerance of organic solvents also were enhanced;Enzyme protein molecules structure in solution was studied by UV-vis spectroscopy,fluorescence and circular dichroism（CD）.The results show that heme in the modified CPO is more exposed for easy access of substrate and alpha helix in the modified CPO is enhanced resulting in improvement of the enzyme protein deactivation ability.Enzyme kinetics analysis shows that the decrese of Km and the increase of kcat/Km proved that an increase of the affinity and selectivity of CPO to substrate,this is the main reason why the modified enzymes activity can be increased.关键词
氯过氧化物酶/化学修饰/光谱分析/动力学Key words
chloroperoxidase/chemical modifiy/spectroscopy assay/kinetic parameters分类
化学化工引用本文复制引用
李超男,蒋育澄,胡满成..氯过氧化物酶的化学修饰及其在溶液中结构与催化性能的关系[J].陕西师范大学学报：自然科学版,2011,39(6):49-53,5.基金项目
国家自然科学基金资助项目 （）
中央高校基本科研业务费专项资金项目 （）
