Purification and characterization of glycoside hydrolases produced by the filament...
| Grant number: | 17/16291-5 |
| Support type: | Regular Research Grants |
| Duration: | October 01, 2017 - September 30, 2019 |
| Field of knowledge: | Biological Sciences - Biophysics |
| Principal Investigator: | João Renato Carvalho Muniz |
| Grantee: | João Renato Carvalho Muniz |
| Home Institution: | Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil |
Abstract
The conversion of lignocellulosic biomass into fermentable sugars represents a viable alternative for the production of renewable fuels, such as ethanol. However, the recalcitrance and complexity of this material make it challenging to develop cost-effective processes, making it imperative to apply more efficient enzymes. Most of the cellulases and hemicellulases used in biotechnological and bioindustrial processes are produced by fungi of genus Trichoderma, Aspergillus and Penicilium. However, these enzymes are generally stable at low temperatures (40-50 °C). The investigation and development of enzymes that present greater thermal stability, high rate of hydrolysis and mass transfer by reducing the viscosity of the medium and, on the other hand, being able to guarantee a reduction of the reactors contamination, and also resulting in a more efficient and economical process of biomass bioconversion. Enzymes with these characteristics can be obtained from thermophilic organisms. Preliminary results, carried out in our laboratory, evidenced some proteins of interest and participants in the enzymatic arsenal for biomass degradation, produced by the thermophilic fungus Thielavia terrestris, under different carbon sources such as sugarcane bagasse in natura (BCIN), Sugarcane bagasse (BCEV) and kraft pulp (CEL). From the identified enzymes, the current project aims to obtain functional and structural information of the "auxiliary" enzymes from families: AA1, AA3, AA7 and AA9, in addition to other carbohydrates-active enzymes such as: GH3, GH5, GH7, GH10, GH43, GH45, GH74 and GH114, using modern scientific methods in enzymology and biochemistry of macromolecules, together with biophysical studies. The characterization of the enzymes, combined with the structural information, will support the production of enzymatic cocktails with better hydrolytic properties that can be used in biorefineries for the degradation of lignocellulosic biomass and biotechnology. (AU)