Enantioselective biocatalysis optimized by directed evolution.
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.
Jaeger
Karl-Erich
KE
Institut für Molekulare Enzymtechnologie, Heinrich-Heine-Universität Duesseldorf, Forschungszentrum Juelich, D-52426 Juelich, Germany. karl-erich.jaeger@fz-juelich.de
Eggert
Thorsten
T
D000465:Algorithms; D001709:Biotechnology / Q000379:methods; D002384:Catalysis; D019020:Directed Molecular Evolution / Q000379:methods*; D015195:Drug Design; D004798:Enzymes / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics*; D019143:Evolution, Molecular; D020869:Gene Expression Profiling / Q000379:methods; D007536:Isomerism; D008957:Models, Genetic; D016297:Mutagenesis, Site-Directed / Q000235:genetics; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D020539:Sequence Analysis, Protein / Q000379:methods*
D004798:Enzymes; D011994:Recombinant Proteins