In many industrial fields such as fine chemistry, pharmacy, cosmetology, agriculture, food,etc., the need for safer and purer products leads to the use of exquisite selective processes. This goal may be achieved by exploiting enzymes as catalysts since their excellent properties. Enzyme technology in the last decades has enabled the enzyme to catalyze industrial reaction due to the numerous advances in enzyme isolation, production, purification, stabilization, as well as the great efforts done on process design to optimize their use. Dehydrogenases (DHs), which depend on nicotinamide cofactors, are among the most interesting enzymes in biocatalysis because they perform selective reductions and specific oxidations that may be key steps in the synthesis routes for fine chemicals, such as pharmaceuticals, food additives, etc. The search of new DHs has been enormously encouraged in the last times resulting in an increased number of available ones. On the other hand, due to the high costs of the nicotinamide cofactors, their stoichiometric use is not acceptable from an economical point of view. For these reasons industrial application of these enzymes requires efficient in situ replenishment of the concomitant cofactor in its right oxidation state. Therefore, the use of simple and low cost purification systems, the use of enzymes from thermophilic microorganisms and the development of cost-effective systems for nicotinamide cofactors regeneration would overcome some of the limitation of DHs in order to apply them industrially.

Peer reviewed

274 pg.