Directed evolution and rational design

被引:3
|
作者
Kourist, R. [1 ]
Hoehne, M. [1 ]
Bornscheuer, U. T. [1 ]
机构
[1] Ernst Moritz Arndt Univ Greifswald, Inst Biochem, Abt Biotechnol & Enzymkatalyse, D-17487 Greifswald, Germany
关键词
MUTANT;
D O I
10.1002/ciuz.200900478
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
While most enzymes are highly adapted to their natural role, few biocatalysts meet the requirements for industrial applications such as high activity, high stability and excellent selectivity. Modern methods of protein evolution allow the optimisation of enzymes by the alteration of the amino acid sequence and hence the modification of chemical and catalytic properties. This article gives an overview about the strategies rational protein design and directed evolution. The scope and limitations of both methods are outlined by the discussion of very recent examples on the optimisation of stability and selectivity and the creation of novel biocatalysts.
引用
收藏
页码:132 / 142
页数:11
相关论文
共 50 条
  • [1] Structure-based design approach to rational site-directed mutagenesis of β-lactoglobulin
    Bonarek, Piotr
    Loch, Joanna, I
    Tworzydlo, Magdalena
    Cooper, David R.
    Milto, Katazyna
    Wrobel, Paulina
    Kurpiewska, Katarzyna
    Lewinski, Krzysztof
    JOURNAL OF STRUCTURAL BIOLOGY, 2020, 210 (02)
  • [2] Development of chimeric laccases by directed evolution
    Pardo, Isabel
    Isabel Vicente, Ana
    Mate, Diana M.
    Alcalde, Miguel
    Camarero, Susana
    BIOTECHNOLOGY AND BIOENGINEERING, 2012, 109 (12) : 2978 - 2986
  • [3] Natural Diversity to Guide Focused Directed Evolution
    Jochens, Helge
    Bornscheuer, Uwe T.
    CHEMBIOCHEM, 2010, 11 (13) : 1861 - 1866
  • [4] Widening the pH Activity Profile of a Fungal Laccase by Directed Evolution
    Torres-Salas, Pamela
    Mate, Diana M.
    Ghazi, Iraj
    Plou, Francisco J.
    Ballesteros, Antonio O.
    Alcalde, Miguel
    CHEMBIOCHEM, 2013, 14 (08) : 934 - 937
  • [5] Directed Evolution of an Enantioselective Lipase with Broad Substrate Scope for Hydrolysis of α-Substituted Esters
    Engstrom, Karin
    Nyhlen, Jonas
    Sandstrom, Anders G.
    Backvall, Jan-E.
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2010, 132 (20) : 7038 - 7042
  • [6] Obtaining a mutant of Bacillus amyloliquefaciens xylanase A with improved catalytic activity by directed evolution
    Xu, Xin
    Liu, Ming-qi
    Huo, Wen-kang
    Dai, Xian-jun
    ENZYME AND MICROBIAL TECHNOLOGY, 2016, 86 : 59 - 66
  • [7] Directed enzyme evolution: climbing fitness peaks one amino acid at a time
    Tracewell, Cara A.
    Arnold, Frances H.
    CURRENT OPINION IN CHEMICAL BIOLOGY, 2009, 13 (01) : 3 - 9
  • [8] Improving the catalytic efficiency of Pseudomonas aeruginosa lipoxygenase by semi-rational design
    Pang, Cuiping
    Liu, Song
    Zhang, Guoqiang
    Zhou, Jingwen
    Du, Guocheng
    Li, Jianghua
    ENZYME AND MICROBIAL TECHNOLOGY, 2023, 162
  • [9] Semirational Directed Evolution of Loop Regions in Aspergillus japonicus β-Fructofuranosidase for Improved Fructooligosaccharide Production
    Trollope, K. M.
    Goergens, J. F.
    Volschenk, H.
    APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2015, 81 (20) : 7319 - 7329
  • [10] A comparison of whole cell directed evolution approaches in breeding of industrial strain of Saccharomyces cerevisiae
    Hou, Li-hua
    Meng, Meng
    Guo, Lin
    He, Jing-yu
    BIOTECHNOLOGY LETTERS, 2015, 37 (07) : 1393 - 1398