Search for biocatalysts by the exploration of enzymatic diversity

LCAB project
LCAB group members

It is now well-established that biocatalysts provide interesting alternatives to chemical synthesis for industry.

A large majority of enzymatic activities described in prokaryotes have been demonstrated and experimentally characterized in bacteria which can be cultivated in the laboratory. It is estimated, however, that the “cultivable” bacteria only represent 1% of all bacteria. The appearance of data from the sequencing of DNA from bacterial metagenomes (consortia of bacteria) starting a few years ago has provided access to a vast unexplored resource of enzymes from bacteria which have not been cultivated in the laboratory, and thus enzymatic activities which are potentially new. Due to the amelioration of the tools of molecular biology, several strategies have been developed to explore this resource of enzymes from bacterial genomic and metagenomic sequences. These functional studies should enable us not only to enrich our knowledge of the diversity of bacterial metabolism, but also provide us with an extraordinary source of biocatalysts.

Projects:

• Enzymes capable of forming C-C bonds In living cells the formation or breaking of C-C bonds is essential for the catabolism and anabolism of a great variety of carbohydrates and of some keto-acids. Numerous enzymes are thus produced in nature which are capable of breaking or creating C-C bonds (Samland and Sprenger, 2006). These enzymes have aroused the interest of chemists; as for example in the production of monosaccharides which requires numerous stages of protection and deprotection using traditional chemical synthesis.

• ”Thiamine enzymes” project Collaboration: Isthmus, Laboratoire de Valorisation et Applications (Genoscope)

• ”GenoZyme” ANR project Partners: Biocatalysis and Metabolism Group (SEESIB, Blaise Pascal University), Isthmus

• ”Nitrilases” project Collaboration: Anne Zaparucha (LCOB)

• ”Baeyer-Villigerases” Project Collaboration: Veronique Alphand (Biosciences Group; iSm2; Cezanne University)