Enantioselective biocatalysis optimized by directed evolution

Curr Opin Biotechnol. 2004 Aug;15(4):305-13. doi: 10.1016/j.copbio.2004.06.007.

Abstract

Directed evolution methods are now widely used for the optimization of diverse enzyme properties, which include biotechnologically relevant characteristics like stability, regioselectivity and, in particular, enantioselectivity. In principle, three different approaches are followed to optimize enantioselective reactions: the development of whole-cell biocatalysts through the creation of designer organisms; the optimization of enzymes with existing enantioselectivity for process conditions; and the evolution of novel enantioselective biocatalysts starting from non-selective wild-type enzymes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Algorithms
  • Biotechnology / methods
  • Catalysis*
  • Directed Molecular Evolution / methods*
  • Drug Design
  • Enzymes / biosynthesis*
  • Enzymes / chemistry
  • Enzymes / genetics*
  • Evolution, Molecular
  • Gene Expression Profiling / methods
  • Isomerism
  • Models, Genetic*
  • Mutagenesis, Site-Directed / genetics
  • Protein Engineering / methods*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Sequence Analysis, Protein / methods*

Substances

  • Enzymes
  • Recombinant Proteins