Natural methods of protein stabilization: thermostable biocatalysts
Natural methods of protein stabilization: thermostable biocatalysts
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DOI：
10.1042/bst0351558
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发表时间：
2007-12-01
影响因子：
3.9
通讯作者：
Isupov, M.
中科院分区：
文献类型：
--
作者：
Littlechild, J. A.;Guy, J.;Isupov, M.
在嗜热和超嗜热生物中天然存在的酶在精细化工和制药工业中被用作稳健的生物催化剂。它们在这些工业中具有重要用途，因为它们增加了在商业反应条件下通常需要的稳定性。在这些研究中使用的方法是了解大自然如何利用其生化特性和三维结构的详细知识来稳定这些蛋白质。埃克塞特研究的几种不同类型的酶说明了这一点。这些酶包括醇脱氢酶、氨基酰化酶、焦谷氨酰羧肽酶、γ-内酰胺酶、脱卤酶和溶血磷脂酶。
Enzymes that are naturally found in thermophilic and hyperthermophilic organisms are being used as robust biocatalysts in the fine chemical and pharmaceutical industries. They have important use in these industries due to their increased stability which is often required during commercial reaction conditions. The approach used in these studies is to learn how nature has managed to stabilize these proteins using a detailed knowledge of their biochemical properties and three-dimensional structures. This is illustrated with several different classes of enzyme that have been studied at Exeter. These include alcohol dehydrogenase, aminoacylase, pyroglutamyl carboxypeptidase, gamma-lactamase, dehalogenase and lysophospholipase.