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Lipase Congeners Designed by Genetic Code Engineering
Citation key 078.2011.hoesl
Author Hoesl, M. G. and Acevedo Rocha, C. and Nehring, S. and Wolschner, C. and Royter, M. and Wiltschi, B. and Budisa, N. and Antranikian, G.
Pages 213-221
Year 2011
DOI 10.1002/cctc.201000253
Journal ChemCatChem
Volume 3
Number 1
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.
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