Analyse in silico de glucoamylase de Pseudomonas fragi

Abstract

Glucoamylase (E.C. 3.2.1.3) are enzymes capable of hydrolyzing both α-1, 4 and α-1, 6-glucosidic linkages, producing glucose monomers, maltose disaccharides, and oligosaccharides. These enzymes possess the potential to release glucose as a primary end product for various applications in the food and beverage industries. The structure of glucoamylase, conserved across species, allows it to hydrolyze processed and unprocessed starch to β-D-glucose, giving it global industrial importance. However, glucoamylase from bacterial strains are the least studied compared to those from fungal strains. In this study, various physicochemical analyses, analysis of secondary structure, structural properties including homology modeling, refinement and validation of model quality, as well as functional analyzes of glucoamylase from the bacterium Pseudomonas fragi were carried out using several bioinformatics tools. This analysis is the first in silico study to explore the structural and functional properties of this enzyme in P. fragi, which could improve its production and use in various industrial sectors