Modular Hyperthermostable endo-beta-1,4-mannanase: determination of the three-dimensional structure of the Central Domain an its role in the thermostabilization of whole enzyme

• 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 - Molecular Biophysics
• Cooperation agreement: Coordination of Improvement of Higher Education Personnel (CAPES)
• Principal researcher: 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)

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

DA SILVA, VIVIAM M.; CABRAL, ALINE D.; SPERANCA, MARCIA A.; SQUINA, FABIO M.; MUNIZ, JOAO RENATO C.; MARTIN, LYDIE; NICOLET, YVAIN; GARCIA, WANIUS. High-resolution structure of a modular hyperthermostable endo-beta-1,4-mannanase from Thermotoga petrophila: The ancillary immunoglobulin-like module is a thermostabilizing domain. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v. 1868, n. 8 AUG 2020. Web of Science Citations: 0.

ARAUJO, JUSCEMACIA N.; TOFANELLO, ARYANE; DA SILVA, VIVIAM M.; SATO, JULIANA A. P.; SQUINA, FABIO M.; NANTES, ISELI L.; GARCIA, WANIUS. Photobiosynthesis of stable and functional silver/silver chloride nanoparticles with hydrolytic activity using hyperthermophilic beta-glucosidases with industrial potential. International Journal of Biological Macromolecules, v. 102, p. 84-91, SEP 2017. Web of Science Citations: 7.

DA SILVA, VIVIAM M.; DE SOUZA, ANDERSON S.; NEGRAO, DJANIRA R.; POLIKARPOV, IGOR; SQUINA, FABIO M.; DE OLIVEIRA NETO, MARIO; MUNIZ, JOAO R. C.; GARCIA, WANIUS. Non-productive adsorption of bacterial beta-glucosidases on lignins is electrostatically modulated and depends on the presence of fibronection type III-like domain. Enzyme and Microbial Technology, v. 87-88, p. 1-8, JUN 2016. Web of Science Citations: 3.