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.
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.
News published in Agência FAPESP Newsletter about the scholarship: