Studies of stability, flexibility and enzymatic activity of the beta-mannanase from hyperthermophilic bacterium Thermotoga petrophila

• Grant number: 12/03503-0
• Support Opportunities: Scholarships in Brazil - Master
• Start date: June 01, 2012
• End date: May 31, 2014
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal Investigator: Wanius José Garcia da Silva
• Grantee: Viviam Moura da Silva
• Host Institution: Centro de Ciências Naturais e Humanas (CCNH). Universidade Federal do ABC (UFABC). Ministério da Educação (Brasil). Santo André , SP, Brazil

Abstract

Biotechnological processes, such as biomass pre-treatments, are performed under extreme environmental conditions regarding pH, osmolarity and temperature. Thus, hyperthermophilic enzymes that are stable and functional at high temperatures offer substantial techno-economical advantages. The enzyme ²-mannanase from hyperthermophilic bacterium Thermotoga petrophila (TpMan) catalyzes the hydrolysis of ²-1,4-mannoside linkages in various mannan-containing polysaccharides, such as glucomannans and galactomannans. Degradation of these polysaccharides represents a key step for a number of industrial applications including delignification of kraft pulps, food processing and production of second-generation biofuels. In this context, the main objective of this project is to make a study of the relationship between stability, degree of flexibility and enzymatic activity of the protein TpMan. For this purpose, biophysical and biochemical tools are employed.

Scientific publications

(4)

(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)

MURILLO, JULIANA LONDONO; CABRAL, ALINE DINIZ; UEHARA, MABEL; DA SILVA, VIVIAM MOURA; DOS SANTOS, JULIETE VITORINO; CARVALHO MUNIZ, JOAO RENATO; ESTROZI, LEANDRO FARIAS; FENEL, DAPHNA; GARCIA, WANIUS; SPERANCA, MARCIA APARECIDA. Nucleoprotein from the unique human infecting Orthobunyavirus of Simbu serogroup (Oropouche virus) forms higher order oligomers in complex with nucleic acids in vitro. Amino Acids, v. 50, n. 6, p. 711-721, JUN 2018. (13/26096-4, 09/11347-6, 12/03503-0, 15/02897-3)

DA SILVA, VIVIAM M.; COLUSSI, FRANCIELI; NETO, MARIO DE OLIVEIRA; BRAZ, ANTONIO S. K.; SQUINA, FABIO M.; OLIVEIRA, CRISTIANO L. P.; GARCIA, WANIUS. Modular Hyperthermostable Bacterial Endo-beta-1, 4-Mannanase: Molecular Shape, Flexibility and Temperature-Dependent Conformational Changes. PLoS One, v. 9, n. 3, MAR 26 2014. (12/21054-9, 12/03503-0)

DE OLIVEIRA, LEANDRO C.; DA SILVA, VIVIAM M.; COLUSSI, FRANCIELI; CABRAL, ALINE D.; DE OLIVEIRA NETO, MARIO; SQUINA, FABIO M.; GARCIA, WANIUS. Conformational Changes in a Hyperthermostable Glycoside Hydrolase: Enzymatic Activity Is a Consequence of the Loop Dynamics and Protonation Balance. PLoS One, v. 10, n. 2, FEB 27 2015. (12/21054-9, 08/58037-9, 12/03503-0, 11/13242-7)

COLUSSI, FRANCIELI; DA SILVA, VIVIAM M.; MILLER, IAN; COTA, JUNIO; DE OLIVEIRA, LEANDRO C.; DE OLIVEIRA NETO, MARIO; SQUINA, FABIO M.; GARCIA, WANIUS. Oligomeric state and structural stability of two hyperthermophilic beta-glucosidases from Thermotoga petrophila. Amino Acids, v. 47, n. 5, p. 937-948, MAY 2015. (12/21054-9, 08/58037-9, 12/03503-0, 11/13242-7)