Structural and functional studies of carbohydrate-active enzymes involved in the degradation of plant biomass with potential biotechnological applications

From target selection to three-dimensional structures, a pioneer approach in terms of Brazilian universities has take place at Molecular Biotechnology Group IFSC/USP. Our Structural Genomic Pipeline has to date delivered more than 20 novel structures to the community and a number of articles. Applying modern scientific approaches in macromolecular crystallography associated with biophysical and biochemical studies will foster a deeper understanding of the hydrolysis of vegetal biomass allowing systematic studies of the relationships between structure and function of carbohydrate-active enzymes. Among them, transferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The fructosyltransferases are responsible for transferring a fructose unit from one sucrose to another and involved in the production of fructooligosaccharide or fructan. They consist in a homologous series of oligo and polysaccharides non-reducing wherein each part of the series is composed of one molecule of glucose and one residue of fructose longer than the previous part. Those products have a largely technological application especially in food industries and bioenergy. In the search for elucidating different characteristics of substrates synthesis for bacteria and fungi, we show the structural and functional analyses of two enzymes belonging to families 32 and 68 of glycosyl hydrolases. The structural information will form the basis for further studies in site-directed mutagenesis aiming the production of novel enzymes and cocktails with better hydrolytic properties to be used in Biorefineries. The success of these studies will provide its contribution toward a sustainable and environmentally friendly bioenergy production.