Microbial Thermostable lipases. Comparative study of three lipases, biochemical and structural characteristics

      Аннотация: The development of new biotechnology and bio-industry is a major challenge for the future. However, this development requires the focus of biocatalysts more efficient but also suitable for Implementation in industrial conditions. Lipases which have been found in many species, plants, bacteria, yeasts and fungi, represent a large group of enzymes in biotechnology. The enzymes of microbial origin are the most interesting, because of their potential applications in different sectors such as food, pharmaceuticals, detergents, biodiesel and cosmetic industries, also the improvement of the effluents biodegradability from high-fat food industry (dairy, meat and seafood). Most of lipases are serine enzymes and there is a hydrogen-bond network in their active site, consisting of the triad of Ser, Asp/Glu, and His. The increase in production of microbial lipases requires not only the techniques of molecular biology which contribute to the overexpression of the corresponding genes, but also the understanding of the molecular and biochemical mechanisms that influence the folding and secretion of these enzymes.

Ключевые слова: Molecular Modeling, Protein Purification, Sequencing, thermostability, microbial lipase