Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases
Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases
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DOI：
10.1042/bj20020695
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发表时间：
2002-11-01
影响因子：
4.1
通讯作者：
Manco, G
中科院分区：
文献类型：
--
作者：
Del Vecchio, P;Graziano, G;Manco, G
本文用稳态荧光和圆二色性测定方法研究了两种嗜热酯酶--闪烁古生球菌（Archaeoglobusfulgidus）的AFEST和酸热脂环酸芽孢杆菌（Alicyclobacillusacidocaldarius）的EST_2对尿素和盐酸胍变性作用的稳定性。实验结果表明，这两种酶，即使非常耐温度和尿素，盐酸胍的耐药性弱于预期的基础上收集到的数据，迄今为止的一大组球状蛋白质。AFEST和EST 2的结构信息以及从嗜热菌的更大热稳定性的分子起源研究中出现的想法允许提出可靠的理由。目前的结果可能是，一个指示，在蛋白质表面上的电荷-电荷相互作用的优化是两种酯酶的稳定性的关键因素。
The stability of two thermophilic esterases, AFEST from Archaeoglobus fulgidus and EST2 from Alicyclobacillus acidocaldarius, against the denaturing action of urea and guanidine hydrochloride has been investigated by means of steady-state fluorescence and circular dichroism measurements. Experimental results indicate that the two enzymes, even though very resistant to temperature and urea, show a resistance to guanidine hydrochloride weaker than expected on the basis of data collected so far for a large set of globular proteins. Structural information available for AFEST and EST2 and ideas that emerged from studies on the molecular origin of the greater thermal stability of thermophiles allow the suggestion of a reliable rationale. The present results may be ,an indication that the optimization of charge-charge interactions on the protein surface is a key factor for the stability of the two esterases.