Improved biocatalysts by directed evolution and rational protein design.
The efficient application of biocatalysts requires the availability of suitable enzymes with high activity and stability under process conditions, desired substrate selectivity and high enantioselectivity. However, wild-type enzymes often need to be optimized to fulfill these requirements. Two rather contradictory tools can be used on a molecular level to create tailor-made biocatalysts: directed evolution and rational protein design.
Bornscheuer
U T
UT
Institute for Chemistry & Biochemistry, Department of Technical Chemistry & Biotechnology, Greifswald University, Germany. bornsche@mail.uni-greifswald.de
Pohl
M
M
D002384:Catalysis; D019020:Directed Molecular Evolution / Q000379:methods* / Q000639:trends; D004789:Enzyme Activation / Q000502:physiology; D004795:Enzyme Stability / Q000502:physiology; D004798:Enzymes / Q000378:metabolism*; D004950:Esterases / Q000235:genetics; D015723:Gene Library; D016297:Mutagenesis, Site-Directed / Q000235:genetics; D015202:Protein Engineering / Q000379:methods* / Q000639:trends; D011551:Pseudomonas fluorescens / Q000201:enzymology; D013237:Stereoisomerism; D013379:Substrate Specificity / Q000502:physiology
D004798:Enzymes; D004950:Esterases