TAILOR-MADE BIOCATALYSTS: COMBINING THERMODYNAMICS, ORGANIC SYNTHESIS, MOLECULAR BIOLOGY, BIOCHEMISTRY AND MICROBIOLOGY FOR THE DESIGN OF ENZYME SELECTIONS

Abstract

A general strategy for the isolation of catalysts for given chemical reactions was designed. A first link between genes and their corresponding proteins was established by phage display: using Darwin's principles on evolution based on selection and amplification, rare protein molecules can then be selected for function from a large repertoire prior to their characterization by sequencing of their genes. A second link was created between enzymes and their products. By making use of the chelate effect and of Inovirus particles as a chemical, affinity chromatography for the reaction product is then sufficient to isolate among 106 to 1011 proteins and their genes, the rare ones coding for catalysts of interest. The strategy for the parallel processing of information on the catalytic activity of variants from a large protein repertoire is highlighted in this review.