Modular Hyperthermostable endo-beta-1,4-mannanase: determination of the three-dime...
| Grant number: | 14/02065-5 |
| Support type: | Scholarships in Brazil - Doctorate |
| Effective date (Start): | August 01, 2014 |
| Effective date (End): | March 31, 2018 |
| Field of knowledge: | Biological Sciences - Biophysics |
| Cooperation agreement: | Coordination of Improvement of Higher Education Personnel (CAPES) |
| Principal Investigator: | Wanius José Garcia da Silva |
| Grantee: | Viviam Moura da Silva |
| Home Institution: | Centro de Ciências Naturais e Humanas (CCNH). Universidade Federal do ABC (UFABC). Ministério da Educação (Brasil). Santo André , SP, Brazil |
| Associated scholarship(s): | 16/15836-5 - Modular Hyperthermostable endo-beta-1,4-mannanase: determination of the three-dimensional structure of the central domain and its role in the thermostabilization of whole enzyme, BE.EP.DR |
Abstract Endo-beta-1,4-mannanase from Thermotoga petrophila (TpMan) is a hyperthermostable enzyme that catalyzes the hydrolysis of beta-1,4-mannoside linkages in various mannan-containing polysaccharides. The biodegradation of mannan represents a key step for various industrial applications including delignification of kraft pulps, food processing and production of second-generation biofuels. A recent study reported that TpMan is composed of a GH5 catalytic domain joined by a linker to a carbohydrate-binding domain. However, at this moment, there is no three-dimensional structure determined for TpMan. The main objectives of this project are: I) determine the three-dimensional structure of the central domain (linker) and II) elucidate and characterize their role in the thermostabilization of the whole enzyme. The high-resolution three-dimensional structures of the central domain (linker) and C-terminal CBM27 will be determined employing X-ray crystallography. Also, the thermostability of each domain will be analyzed using biophysical techniques and compared with the whole enzyme. (AU) | |