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Functional and Structural Studies of Carbohydrate Binding Modules of Glycosil Hydrolases

Grant number: 12/22802-9
Support Opportunities:Scholarships in Brazil - Post-Doctoral
Effective date (Start): December 01, 2013
Effective date (End): September 30, 2016
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal Investigator:Igor Polikarpov
Grantee:Amanda Bernardes Muniz
Host Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil
Associated research grant:09/52840-7 - Center of Biological and Industrial Processes for Biofuels - CeProBIO, AP.BIOEN.TEM


The diversification of energy production through the use of renewable resources is a major goal of contemporary society. Although Brazil has exponent advances in ethanol production, the utilization of residual lignocellulosic biomass could ensure better energy efficiency within the second-generation ethanol (E2G) production. However, the cost of E2G is relatively high, and the elevated price of enzyme preparations used in the hydrolysis process contributes to this. In this context, a detailed understanding of enzymatic hydrolysis of carbohydrates can help optimize the process of plant biomass saccharification. The recognition of cellulose polymers by cellulases is frequently mediated by carbohydrate-binding modules (CBMs), which considerably increase the enzymatic activity of these enzymes in polymeric and insoluble substrates. Our purpose in this project is to conduct systematic studies of the relationship between the structure and function of CBMs, by combining techniques and modern scientific methods in macromolecular crystallography, biophysical, biochemical and functional studies, aiming to better understand the role of these domains in the recognition and saccharification of insoluble carbohydrate polymers and usually recalcitrant. The understanding of the mechanisms involved in the recognition of polymeric substrates by cellulases (and glycoside hydrolases in general) will provide a strong platform for the development of new technologies in recognition of carbohydrates, which will yield bases for finer manipulations of these interactions. This project will be supported by the experience of the Molecular Biotechnology Group (IFSC-USP) in the structural and functional studies of glycoside hydrolases, and envisage the consolidation of important national and international collaborations.

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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)
BERNARDES, AMANDA; TEXTOR, LARISSA C.; SANTOS, JADEMILSON C.; CUADRADO, NAZARET HIDALGO; KOSTETSKY, EDUARD YA.; ROIG, MANUEL G.; BAVRO, VASSILIY N.; MUNIZ, JOAO R. C.; SHNYROV, VALERY L.; POLIKARPOV, IGOR. Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa. Biochimie, v. 111, p. 58-69, . (12/22802-9, 10/52362-5, 08/56255-9, 09/05349-6)
MIOTTO, LIS SCHWARTZ; DE REZENDE, CAMILA ALVES; BERNARDES, AMANDA; SERPA, VIVIANE ISABEL; TSANG, ADRIAN; POLIKARPOV, IGOR. The Characterization of the Endoglucanase Cel12A from Gloeophyllum trabeum Reveals an Enzyme Highly Active on beta-Glucan. PLoS One, v. 9, n. 9, . (09/52840-7, 08/56255-9, 12/22802-9, 10/52362-5, 09/08233-9)
PELLEGRINI, VANESSA O. A.; BERNARDES, AMANDA; REZENDE, CAMILA A.; POLIKARPOV, IGOR. Cellulose fiber size defines efficiency of enzymatic hydrolysis and impacts degree of synergy between endo- and exoglucanases. Cellulose, v. 25, n. 3, p. 1865-1881, . (12/22802-9, 10/18773-8, 15/13684-0, 16/13602-7)

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