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Biophysical studies and of the synergistic action of thermophilics enzymes involved in the hydrolysis of mannans

Abstract

Cellulases and xylanases have been extensively studied and have found significant industrial application due to their key contributions relating to biorefineries. However, mannan-degrading enzymes have enjoyed less attention. With the increasing number of heterologous strains producing mannan-degrading enzymes their application is gaining importance. A number of studies report production of enzyme in the g/L range which would allow for commercially viable mannanase production using those host strains. In this research project, we propose to perform the cloning, expression and purification of enzymes beta-mannanase, beta-mannosidase and beta-glucosidase from hiperthermophilic bacterium T. petrophila for subsequent biophysical and biochemical studies. Beta-mannanase, beta-mannosidase and beta-glucosidase are major enzymes involved in the hydrolysis of mannans and glucomannans into molecules of fermentable sugars. The relation structure/function and the synergistic action of these enzymes in the hydrolysis of polysaccharides mannan and glucomannan will be analyzed at different physicochemical conditions. Degradation of these polysaccharides represents a key step for a number of industrial applications including production of second-generation biofuels, delignification kraft pulps and food processing. Using these studies, we want to better understand and improve the synergistic action of the enzymes beta-mannanase, beta-mannosidase and beta-glucosidase, from bacterium T. petrophila, in the hydrolysis of mannans and glucomannans into molecules of fermentable sugars. (AU)

Articles published in Agência FAPESP Newsletter about the research grant:
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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)
COTA, JUNIO; CORREA, THAMY L. R.; DAMASIO, ANDRE R. L.; DIOGO, JOSE A.; HOFFMAM, ZAIRA B.; GARCIA, WANIUS; OLIVEIRA, LEANDRO C.; PRADE, ROLF A.; SQUINA, FABIO M.. Comparative analysis of three hyperthermophilic GH1 and GH3 family members with industrial potential. NEW BIOTECHNOLOGY, v. 32, n. 1, p. 13-20, . (12/21054-9, 11/13242-7, 08/58037-9, 10/18198-3)
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, . (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, . (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, . (12/21054-9, 08/58037-9, 12/03503-0, 11/13242-7)