Molecular and Cellular Biochemistry

, Volume 224, Issue 1, pp 159–168

Improving the quality of industrially important enzymes by directed evolution

Authors

  • Rajendra Rani Chirumamilla
    • Biotechnology Research GroupUniversity of Ulster at Coleraine, N
  • Reddivari Muralidhar
    • Biotechnology Research GroupUniversity of Ulster at Coleraine, N
  • Roger Marchant
    • Biotechnology Research GroupUniversity of Ulster at Coleraine, N
    • Biotechnology Research GroupUniversity of Ulster at Coleraine, N
Article

DOI: 10.1023/A:1011904405002

Cite this article as:
Chirumamilla, R.R., Muralidhar, R., Marchant, R. et al. Mol Cell Biochem (2001) 224: 159. doi:10.1023/A:1011904405002

Abstract

Directed evolution is a new process for developing industrially viable biocatalysts. This technique does not require a comprehensive knowledge of the relationships between sequence structure and function of proteins as required by protein engineering. It mimics the process of Darwinian evolution in a test tube combining random mutagenesis and recombination with screening or selection for enzyme variants that have the desired properties. Directed evolution helps in enhancing the enzyme performance both in natural and synthetic environments. This article reviews the process of directed evolution and its application to improve substrate specificity, activity, enantioselectivity and thermal stability.

directed evolutionsubstrate specificityactivityenantioselectivitythermal stabilitymutagenesis

Copyright information

© Kluwer Academic Publishers 2001