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URI permanente para esta coleçãohttps://locus.ufv.br/handle/123456789/11847

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    Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
    (International Journal of Biological Macromolecules, 2010-04-01) Rezende, Sebastião T.; Viana, Pollyanna A.; Meza, Andreia N.; Gomide, Felipe T.F.; Nagem, Ronaldo A.P.; Santos, Alexandre M.C.; Santoro, Marcelo M.; Guimarães, Valéria M.
    Spectroscopic and thermodynamic properties were determined for Debaryomyces hansenii UFV-1 extracellular and intracellular α-galactosidases. α-Galactosidases showed similar secondary structure compositions (α-helix, β-sheet parallel and β-turn). Effects of pH and temperature on the structure of α-galactosidases were investigated using circular dichroism spectroscopy. It was more pronounced at low pH. Microcalorimetry was employed for the determination of thermodynamic parameters. Immediate thermal denaturation reversibility was not observed for α-galactosidases; it occurred as a thermodynamically driven process. Extracellular α-galactosidase, at pH 5.5, showed lower Tm when compared to the intracellular enzyme. The CD and DSC data suggest that D. hansenii α-galactosidases have different behaviors although they possess some similar secondary structures.
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    Activity of Debaryomyces hansenii UFV-1 a-galactosidases against a-D-galactopyranoside derivatives
    (Carbohydrate Research, 2011-04-01) Rezende, Sebastião T. de; Viana, Pollyanna A.; Alves, Arianne de A.; Manfrini, Rozângela M.; Alves, Ricardo J.; Bemquerer, Marcelo P.; Santoro, Marcelo M.; Guimarães, Valéria M.
    α-d-Galactopyranosides were synthesized and their inhibitory activities toward the Debaryomyces hansenii UFV-1 extracellular and intracellular α-galactosidases were evaluated. Methyl α-d-galactopyranoside was the most potent inhibitor compared to the others tested, with values of 0.82 and 1.12 mmol L−1, for extracellular and intracellular enzymes, respectively. These results indicate that the presence of a hydroxyl group in the C-6 position of α-d-galactopyranoside derivatives is important for the recognition by D. hansenii UFV-1 α-galactosidases.