Structural and biophysical characterization of thermophilic enzymes prospected from the fungus Thielavia terrestris for biomass degradation and biotechnological products generation

• Grant number: 17/16291-5
• Support type: Regular Research Grants
• Duration: October 01, 2017 - September 30, 2019
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal researcher: 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)

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

DE LIMA, MARIANA Z. T.; DE ALMEIDA, LEONARDO R.; MERA, ALAIN M.; BERNARDES, AMANDA; GARCIA, WANIUS; MUNIZ, JOAO R. C. Crystal Structure of a Sucrose-6-phosphate Hydrolase from Lactobacillus gasseri with Potential Applications in Fructan Production and the Food Industry. Journal of Agricultural and Food Chemistry, v. 69, n. 35, p. 10223-10234, SEP 8 2021. Web of Science Citations: 0.

DA SILVA, VIVIAM M.; CABRAL, ALINE D.; SPERANCA, MARCIA A.; SQUINA, FABIO M.; MUNIZ, JOAO RENATO C.; MARTIN, LYDIE; NICOLET, YVAIN; GARCIA, WANIUS. High-resolution structure of a modular hyperthermostable endo-beta-1,4-mannanase from Thermotoga petrophila: The ancillary immunoglobulin-like module is a thermostabilizing domain. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v. 1868, n. 8 AUG 2020. Web of Science Citations: 0.

MERA, ALAIN; THEODORO DE LIMA, MARIANA ZULIANI; BERNARDES, AMANDA; GARCIA, WANIUS; CARVALHO MUNIZ, JOAO RENATO. Low-resolution structure, oligomerization and its role on the enzymatic activity of a sucrose-6-phosphate hydrolase from Bacillus licheniformis. Amino Acids, v. 51, n. 4, p. 599-610, APR 2019. Web of Science Citations: 0.