Lipase Congeners Designed by Genetic Code Engineering

Michael G. Hoesl, Carlos G. Acevedo-Rocha, Sebastian Nehring, Marina Royter, Christina Wolschner, Birgit Wiltschi, Nediljko Budisa*, Garabed Antranikian

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Classical enzyme optimization exploits the chemistry confined to the 20 canonical amino acids encoded by the standard genetic code. 'Genetic code engineering' allows the global substitution of particular residues with synthetic analogues, endowing proteins with chemical diversity not found in nature. These proteins are congeners of the parent protein because they originate from the same gene sequence, but contain a fraction of noncanonical amino acids. Global substitutions of methionine, proline, phenylalanine, and tyrosine have been carried out with related analogues in Thermoanaerobacter thermohydrosulfuricus lipase. This study represents the first extensive report of an important biocatalyst substituted with a high number of noncanonical amino acids. The generated lipase congeners displayed special features such as enhanced activation, elevated enzyme activity (by up to 25%) and substrate tolerance (by up to 40%), and changes in optimal temperature (by up to 20°C) and pH (by up to 3). These emergent features achieved by genetic code engineering might be important not only for academic research, but also for numerous economical applications in the food, detergent, chemical, pharmaceutical, leather, textile, cosmetic, and paper industries.

Original languageEnglish
Pages (from-to)213-221
Number of pages9
JournalChemCatChem
Volume3
Issue number1
DOIs
Publication statusPublished - 10 Jan 2011
Externally publishedYes

Keywords

  • Amino acids
  • Biotechnology
  • Enzyme catalysis
  • Genetic code engineering
  • Lipases

ASJC Scopus subject areas

  • Catalysis
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

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