摘要
对经 6 α 葡糖基 β 环糊精 (G β CD)修饰后的辣根过氧化物酶 (HRP)的热力学稳定性进行了研究。实验结果显示 ,在G β CD与HRP的摩尔比为 5 ,pH 7.5条件下经低温混合处理 2 .5h后的修饰HRP获得较好的热稳定性综合改善作用。与天然酶相比 ,修饰酶活力约为 94% ,表观热失活常数k降低至原来的 2 7%。经 75℃经
The effects of 6\|α\|glucosyl\|β\|cyclodextrin (G\|β\|CD) on the thermodynamic stability of horseradish peroxidase were studied using the residual activity method. The results indicated that the mole ratio between G\|β\|CD and HRP, system pH and the time of modifying treatment were of the main factors. The optimum comprehensive parameters were achieved under the condition of \[G\|β\|CD\]/\=5 in mole concentration, pH 7.5, for 2.5 h treating at \%t\%≤20 ℃, which gave the results that enzyme gained 94% of the native activity, and apparent inactivation rate constant, \%k\%, dropped to 27% of the native enzyme. The activity recovery extent of the enzyme after thermal inactivation at 75 ℃ for 30 min was improved obviously.
出处
《浙江工业大学学报》
CAS
2001年第2期200-203,共4页
Journal of Zhejiang University of Technology