角质酶
化学
差示扫描量热法
圆二色性
吸附
等温微量热法
热稳定性
蛋白质吸附
蛋白质二级结构
结晶学
糜蛋白酶
分子
蛋白质结构
酶
有机化学
焓
胰蛋白酶
生物化学
量子力学
热力学
物理
作者
T. Zoungrana,Gerhard H. Findenegg,Willem Norde
标识
DOI:10.1006/jcis.1997.4895
摘要
A proteolytic enzyme, alpha-chymotrypsin, and a lipolytic enzyme, cutinase, were adsorbed from aqueous solution onto a hydrophobic Teflon surface and a hydrophilic silica surface. We investigated the influence of adsorption on the structure, the structure thermal stability and the activity of these enzymes. Probing the protein structure by circular dichroism spectroscopy indicates that Teflon promotes the formation of helical structure in alpha-chymotrypsin, but the reverse effect is found with cutinase. The perturbed protein structures on Teflon are remarkably stable, showing no heat-induced structural transitions up to 100°C, as monitored by differential scanning calorimetry. Contact with the hydrophilic silica surface leads to a loss in the helix content of both proteins. Differential scanning calorimetry points to a heterogeneous population of adsorbed protein molecules with respect to their conformational states. The fraction of the native-like conformation in the adsorbed layer increases with increasing coverage of the silica surface by the proteins. The specific enzymatic activity in the adsorbed state qualitatively correlates with the fraction of proteins in the native-like conformation.
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