Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method

Manfred T Reetz; Pankaj Soni; Layla Fernández; Yosephine Gumulya; José D Carballeira

doi:10.1039/c0cc02657c

Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method

Chem Commun (Camb). 2010 Dec 7;46(45):8657-8. doi: 10.1039/c0cc02657c. Epub 2010 Oct 18.

Authors

Manfred T Reetz¹, Pankaj Soni, Layla Fernández, Yosephine Gumulya, José D Carballeira

Affiliation

¹ Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany. reetz@mpi-muelheim.mpg

PMID: 20957255
DOI: 10.1039/c0cc02657c

Abstract

Mutants of the lipase from Bacillus subtilis, previously engineered for enhanced thermostability using directed evolution based on the B-FIT method, show significantly increased tolerance to hostile organic solvents.

MeSH terms

Bacillus subtilis / enzymology
Directed Molecular Evolution / methods*
Enzyme Stability / drug effects
Enzyme Stability / genetics
Lipase / chemistry*
Lipase / genetics*
Mutagenesis*
Organic Chemicals / pharmacology*
Solvents / pharmacology*

Substances

Organic Chemicals
Solvents
Lipase