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Insights into the molecular basis for specificity and thermal stability in modular bacterial glycoside hydrolases belonging to GH5 family: Bacillus subtilis cellulase and Thermotoga petrophila mannanase.

Grant number: 13/01583-0
Support Opportunities:Scholarships in Brazil - Post-Doctoral
Start date: August 01, 2013
End date: July 31, 2016
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal Investigator:Mário Tyago Murakami
Grantee:Diego Mario Ruiz
Host Institution:Centro Nacional de Pesquisa em Energia e Materiais (CNPEM). Campinas , SP, Brazil

Abstract

The high cost to degrade complex polysaccharides from lignocellulosic biomass to fermentable sugars remains the main obstacle for the large-scale production of cellulosic ethanol. The costs with cellulases and hemicellulases contribute substantially to the price of ethanol and, therefore, further studies aiming at understanding and improving the efficiency and stability of these enzymes are of fundamental importance. The detailed rendering of biophysical and structural properties of these enzymes are crucial information for rational molecular engineering in order to make them more stable and highly active under conditions imposed by industry.The main goal of this project is to advance into the characterization of bacterial modular glycoside hydrolases belonging to GH5 family using as model the hemicellulase from Thermotoga petrophila (endo-1,4-B-mannanase, TpMan) and the cellulase from Bacillus subtilis (endo-1,4-B-glucanase, BsCel5A). The focus of this project is to learn at molecular level the effects of different modules and linkers on the activity and thermal stability of these two enzymes. These studies together with the recently results published by the Dr. Murakami's lab about BsCl5A (Biochem J, 2012. 441: 95-104) and TpMan (J Struct Biol, 2012. 177: 469-476) will allow us to perform functional changes in these enzymes based on the rational design of the active site. In addition, the results obtained in this research will contribute to develop more efficient and robust biocatalysts with potential applications in biotechnology.

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Scientific publications
(The scientific publications listed on this page originate from the Web of Science or SciELO databases. Their authors have cited FAPESP grant or fellowship project numbers awarded to Principal Investigators or Fellowship Recipients, whether or not they are among the authors. This information is collected automatically and retrieved directly from those bibliometric databases.)
RUIZ, DIEGO M.; TUROWSKI, VALERIA R.; MURAKAMI, MARIO T.. Effects of the linker region on the structure and function of modular GH5 cellulases. SCIENTIFIC REPORTS, v. 6, . (13/13309-0, 13/01583-0)