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Catalytic dynamics study of the endo-1,4-beta-xylanase from Bacillus subtilis by fluorescence correlation spectroscopy

Grant number: 14/06319-1
Support Opportunities:Scholarships in Brazil - Master
Start date: June 01, 2014
End date: February 29, 2016
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Agreement: Coordination of Improvement of Higher Education Personnel (CAPES)
Principal Investigator:Richard John Ward
Grantee:Gustavo Avelar Molina
Host Institution: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto (FFCLRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
Associated research grant:10/18850-2 - Identification, characterization and engineering of plant cell wall degrading enzymes, AP.TEM

Abstract

The endo-1,4-beta-xylanases are endo glycoside hydrolases that catalyzes the xylan hydrolysis. Due the applications multiplicity of these enzymes in production of economically relevant riches, the interest for these and others glycoside hydrolases is growing not only in academia, but also in industry, highlighting the environmental benefits brought by its use in biobleaching of the paper pulp in the paper and pulp industry and by providing means to produce biofuels, improving the use of biomass and contributing to a sustainable, socially and environmentally friendly and responsible economy. However, the xylanases are not robust enough to withstand the industrial environment and, thus, their application is not economically viable yet. Thereby, the elucidation of the catalytic dynamics of these enzymes to the proposition of more refined and robust models than those that currently exist probably will constitute an important step in their improvement through protein engineering techniques. Therefore, this project has the general objective to obtain new information about the catalytic dynamics and kinetics in one molecule level of a GH11 xylanase, inaccessible by other spectroscopic and molecular dynamics simulation techniques, through analysis of FCS measurements by autocorrelation mode and one photon excitation of a fluorophore attached at different positions of the enzyme and under different environmental e reactional conditions. (AU)

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Academic Publications
(References retrieved automatically from State of São Paulo Research Institutions)
MOLINA, Gustavo Avelar. Biophysical characterization of the catalytic dynamics of a GH11 xylanase. 2016. Master's Dissertation - Universidade de São Paulo (USP). Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto (PCARP/BC) Ribeirão Preto.