Influence of stabilizers cosolutes on catalase conformation
Influence of stabilizers cosolutes on catalase conformation
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DOI：
10.1016/j.ijbiomac.2011.08.012
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发表时间：
2011-12-01
影响因子：
8.2
通讯作者：
Pico, Guillermo
中科院分区：
文献类型：
--
作者：
Belluzo, Soledad;Boeris, Valeria;Pico, Guillermo
分析了蔗糖、甘露醇和甜菜碱对过氧化氢酶的热力学稳定性和构象状态的影响，以了解溶质稳定酶的分子机制。选择过氧化氢酶作为模型酶，因为它用于几种生物技术过程。在每个共溶质的存在下，我们的数据表明，有一个显着增加过氧化氢酶的热稳定性。在酶的二级结构中的一个小的稳定性诱导这些共溶质，在远紫外区的圆二色性已经证明。此外，我们的研究结果支持的想法，过氧化氢酶的整体天然结构变得更加刚性，至少在某些表面区域，在存在的测定的稳定剂。这最后一个发现可以合理地解释从蛋白质表面的共溶质的排斥机制，这增加了该地区周围的结构水。(C)2011爱思唯尔有限公司版权所有。
The effects of sucrose, mannitol and betaine on the thermodynamic stability and the conformational state of the catalase enzyme were analyzed in order to understand the molecular mechanism whereby the solutes stabilized the enzyme. Catalase was selected as the model enzyme because it is used in several biotechnological processes. In the presence of each cosolute, our data have shown that there was a significant increase in the thermal stability of catalase. A minor stabilization in the enzyme secondary structure were induced by these cosolutes, as circular dichroism in the far UV region has demonstrated. Furthermore, our results support the idea that the overall native structure of catalase becomes more rigid, at least in certain surface areas, in the presence of the assayed stabilizers. This last finding can be reasonably explained by the exclusion mechanism of cosolutes from the protein surface which increases the structured water around this area. (C) 2011 Elsevier B.V. All rights reserved.