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Novel biocatalytic enzymes by directed evolution

2001; Elsevier BV; Volume: 19; Issue: 10 Linguagem: Inglês

10.1016/s0167-7799(01)01736-x

0167-9430

Alan Wiseman, Peter S. Goldfarb, Len Woods, Tim Ridgway,

Chemical Synthesis and Analysis

Microbial biosynthesis of an induced enzyme appropriate for the hydrolysis of an added growth substrate, such as lactose or maltose, is well understood in terms of gene regulation by proteins binding to DNA. Alternatively, clonal selection of site-directed mutants can be achieved by growth on defined media that is lacking a particular amino acid. This can be on a culture plate or in continuous culture chemostat fermenters in parameter-controlled large-scale production of specified enzymes for application in industry, analysis, biosynthesis, environment or therapy, as appropriate. Such directed (forced) evolution of microorganisms is the result of the biosynthesis of the enzyme required for the growth of recombinant DNA mutants. However, enzyme catalysts with enhanced activity could be designed that mimic and improve on the active site conformation of the enzyme originally participating in that amino acid biosynthetic pathway 1 Ball, P. (ed) (2001) Nature Insight Biocatalysis. Nature 409, 225–268 Google Scholar .