Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution

被引：233

作者：

Lehmann, M ^{[1
]}

Wyss, M ^{[1
]}

机构：

[1] F Hoffmann La Roche & Co Ltd, Vitamins & Fine Chem Div, Dept VFB, CH-4070 Basel, Switzerland

来源：

CURRENT OPINION IN BIOTECHNOLOGY | 2001年 / 12卷 / 04期

关键词：

D O I：

10.1016/S0958-1669(00)00229-9

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

With the advent of directed evolution techniques, protein engineering has received a fresh impetus. Engineering proteins for thermostability is a particularly exciting and challenging field, as it is crucial for broadening the industrial use of recombinant proteins. In addition to directed evolution, a variety of partially successful rational concepts for engineering thermostability have been developed in the past. Recent results suggest that amino acid sequence comparisons of mesophilic proteins alone can be used efficiently to engineer thermostable proteins. The potential benefits of the underlying, semirational 'consensus concept' are compared with those of rational design and directed evolution approaches.

引用

页码：371 / 375

页数：5

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