中文摘要：

目的 研究辣根过氧化物酶（HRP）在盐酸胍中的变性过程,并建立荧光参数与酶活力的函数模型。方法 采用可见光谱法,荧光光谱法及荧光相图法对盐酸胍诱导的HRP变性过程进行研究,并采用SPSS和Origin软件对变性过程中的构象参数与酶活力参数进行函数模型拟合。结果 盐酸胍诱导的HRP去折叠经历了一个三态过程,其中,引起酶分子从部分折叠中间态向去折叠态转变,导致其疏水内核构象剧烈变化,酶活性中心结构及酶活力开始变化的临界盐酸胍浓度为1.5 mol·L-1;同时建立了构象参数与酶活力的函数模型。结论 所建模型可以表征HRP的变性过程并用于酶活力的预测。

英文摘要：

OBJECTIVE To analyze the denaturation process of horseradish peroxidase（HRP） induced by guanidine hydrochloride,and to establish the relationship between the conformational parameters and the activity of the enzyme.METHODS Visible spectroscopy,fluorescence spectroscopy and fluorescence phase diagram method were selected to study the denaturation process of HRP induced by guanidine hydrochloride.Then SPSS and Origin software were used to fit the relationship model between the conformational parameters and the activity of the enzyme.RESULTS The unfolding process of HRP experienced to a typical three-state model.As the result showed that 1.5 mol·L-1was the critical concentration which caused the conformational transition from the intermediate to the unfolded state and led to the dramatic changes of the hydrophobic core.That meaned both the structure of enzyme active center and the enzyme activity began to change in 1.5 mol·L-1guanidine hydrochloride.In addition,the conformation-activity relationship model was established.CONCLUSION The relationship model could be used to characterize the denaturation process of HRP and predict the enzyme activity.