| Grant number: | 16/13998-8 |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| Start date: | January 01, 2017 |
| End date: | June 17, 2021 |
| Field of knowledge: | Biological Sciences - Biophysics - Molecular Biophysics |
| Agreement: | Coordination of Improvement of Higher Education Personnel (CAPES) |
| Principal Investigator: | Vitor Barbanti Pereira Leite |
| Grantee: | Vinícius de Godoi Contessoto |
| Host Institution: | Instituto de Biociências, Letras e Ciências Exatas (IBILCE). Universidade Estadual Paulista (UNESP). Campus de São José do Rio Preto. São José do Rio Preto , SP, Brazil |
| Associated scholarship(s): | 17/09662-7 - Rational Evolution by Computational Methods Applied in Enzymes Related to Bioethanol Production, BE.EP.PD |
Abstract One of the most difficult challenges in science is to find clean and cheap energy sources. The second generation bioethanol seems to be viable a solution to substitute fossil fuel usage. The bioethanol production makes use of sugarcane biomass residues not used directly in fermentation process. This process involves the degradation of cellulose by specific enzymatic hydrolysis. The technological challenge now is to obtain and optimize the enzymes to perform the hydrolysis process with more efficiency. Recent results from CTBE group on Xylanase A enzyme from Bacillus subtilis have shown a group of mutations that improves the thermostability and the catalytic activity. Understanding the effect of each mutation in protein is an important step to be able to develop efficient methods to design optimized enzymes. The motivation of this project is to work on enzymes thermostability optimization, suggesting mutations to be tested experimentaly. This ongoing project seeks to evaluate and optimize enzyme cocktails for second generation bioethanol production. The focus of the optimization is to increase the catalytic activity, the thermostability and pH control, adapting the enzymes to have the optimum activity at the reactor operation conditions. Theoretical methods based on optimization of charge-charge interaction in enzyme surface and based on consensus and ancestral reconstruction sequence will be used. The suggested mutations will be experimentally validated by the CTBE group. (AU) | |
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