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Substrate specificity, unusual enzymatic activity, and synergistic relationships of beta-glucosidases from Trichoderma harzianum

Grant number: 17/17390-7
Support type:Scholarships abroad - Research Internship - Post-doctor
Effective date (Start): November 01, 2017
Effective date (End): October 31, 2018
Field of knowledge:Biological Sciences - Genetics
Principal Investigator:Anete Pereira de Souza
Grantee:Clelton Aparecido dos Santos
Supervisor abroad: Paul Dupree
Home Institution: Centro de Biologia Molecular e Engenharia Genética (CBMEG). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
Local de pesquisa : University of Cambridge, England  
Associated to the scholarship:16/19775-0 - Development and/or improvement of enzymatic cocktails designed for plant biomass hydrolysis: use of site-directed mutagenesis and chimeric proteins design, BP.PD

Abstract

Current efforts to unravel the secrets of efficient fungal biomass conversion are hampered by the bottleneck that exists in our limited knowledge about the molecular interaction networks between the proteins/enzymes and the plant cell wall components. On the other hand, the majority of the studies, with few exceptions, use artificial substrates, focusing particularly on a specific enzymatic activity, disregarding the global protein networks, which are universally used in all metabolic pathways. In a previous study, our laboratory has reported the structural and functional characterisation of a recombinant beta-glucosidase of Trichoderma harzianum (rThBgl), which was overexpressed by this fungus under biomass degradation conditions. Attempting to improve the rThBgl catalytic properties, including thermostability and high glucose-tolerance, ThBgl-derived mutants were constructed based on structural alignment/prediction using high resolution beta-glucosidase structures available in Protein Data Bank. However, a recent data obtained by our group pointed to a possible extended activity of this enzyme; leading to some questions about the role of beta-glucosidases in the degradation of biomass. In this context, the present project aims to investigate the non-canonical enzymatic activity and synergistic relationships of ²-glucosidase from T. harzianum with other lignocellulose degrading enzymes using several substrates, including sugarcane bagasse and biomass-derived from different plant mutants affected in cell wall synthesis (altered cellulose structure, lignin composition, and xylan structure), beside others substrates available in the Plant Biochemistry Lab, Cambridge, to try work out how the enzymatic activity can be modulated by xylan interaction with cellulose microbribrils.

Matéria(s) publicada(s) na Agência FAPESP sobre a bolsa:
Modified enzyme can increase second-generation ethanol production 
Articles published in other midia outlets: (24 total)
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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)
SANTOS, CLELTON A.; MORAIS, MARIANA A. B.; TERRETT, OLIVER M.; LYCZAKOWSKI, JAN J.; ZANPHORLIN, LETICIA M.; FERREIRA, JAIRE A.; TONOLI, CELISA C. C.; MURAKAMI, MARIO T.; DUPREE, PAUL; SOUZA, ANETE P. An engineered GH1 ss-glucosidase displays enhanced glucose tolerance and increased sugar release from lignocellulosic materials. SCIENTIFIC REPORTS, v. 9, MAR 20 2019. Web of Science Citations: 0.

Please report errors in scientific publications list by writing to: cdi@fapesp.br.
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