摘要
采用各种类型的聚乙二醇衍生物修饰胰蛋白酶,对所修饰酶的酶学性质进行了评价并与原酶比较.结果表明:修饰酶的残存活力受修饰剂的结构、分子量和修饰化度的影响较大,其中分子量为5 000或6 000的2种聚乙二醇衍生物所修饰的酶活力升高.所有修饰酶的热稳定性显著改善,其最适pH值没有发生变化,修饰酶的Km值有所增加.实验表明采用合适的修饰剂对胰蛋白酶进行适度地修饰不会降低酶的活性和改变酶性能.
Trypsin was modified by a series of PEG derivatives, then the properties of modified enzymes were evaluated and were compared with native enzyme. The results show that the activity of modified enzymes depended on the structure, molecular weight of PEG derivatives and the degreed of modification, and the activity of enzyme modified by PEG derivatives ( M = 5 000 or 6 000) was enhanced. The thermal stability of all modified enzymes was improved significantly. The modification does not change the opti- mum pH value of trypsin. The Km values of the conjugates are slightly higher than the native enzyme. The temperate modification did not reduce enzyme' s activity.
出处
《南京师大学报(自然科学版)》
CAS
CSCD
北大核心
2006年第3期53-57,共5页
Journal of Nanjing Normal University(Natural Science Edition)
基金
江苏省高校高新技术发展资助项目(JHB04-037)