摘要
本研究采用二态假说模型,利用热力学原理从宏观角度对辣根过氧化物酶(HRP)的热变性进行研究,通过相关的计算得到表征该酶蛋白变性的热力学参数:变性自由能、变性焓、变性熵和解链温度.研究结果显示,邻苯二甲酸酐修饰后的HRP蛋白酶的解链温度为69.2℃,高于天然HRP的解链温度62.2℃,反映了邻苯二酸酐修饰可以明显的提高HRP的热稳定性。
In order to investigate the thermal denaturation process of the horseradish peroxidase （HRP）, native HRP and HRP modified by phthalic anhydride （PA-HRP） were studied using two-state model, Using the methods of thermodynamics, we can study the problems of protein denaturation from themacroscopic aspects, The thermodynamic parameters which are Gibbs free energy, enthalpy, entropy and the temperature of unfolding can be obtained in the study. The temperature of PA-HPR unfolding was 69.2℃, which was higher than 62.2℃ of native HRP. These results indicated that the PA modification of HRP Increased the stabilization from thermodynamics.
出处
《广东化工》
CAS
2009年第5期124-126,221,共4页
Guangdong Chemical Industry
基金
国家自然科学基金(40803038)
广东省自然科学基金(06300843)
关键词
辣根过氧化物酶
邻苯二甲酸酐
热变性
二态模型
horseradish peroxidase
phthalic anhydride
thermal denaturation
two-state model
