Spectroscopic and thermodynamic properties of Debaryomyces hansenii UFV-1 α-galactosidases
| Autor: | Sebastião Tavares de Rezende, Pollyanna Amaral Viana, F. T. F. Gomide, Ronaldo Alves Pinto Nagem, Alexandre Martins Costa Santos, Valéria Monteze Guimarães, Andreia N. Meza, Marcelo M. Santoro |
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| Rok vydání: | 2010 |
| Předmět: |
Isothermal microcalorimetry
Protein Denaturation Circular dichroism Debaryomyces Biochemistry Protein Structure Secondary Differential scanning calorimetry Structural Biology α-Galactosidases Debaryomyces hansenii Extracellular Transition Temperature Debaryomyces hansenii UFV-1 Molecular Biology Protein secondary structure chemistry.chemical_classification Calorimetry Differential Scanning biology Chemistry Circular Dichroism Temperature General Medicine Hydrogen-Ion Concentration biology.organism_classification Crystallography Enzyme alpha-Galactosidase Thermodynamics Extracellular Space Stability Intracellular |
| Zdroj: | LOCUS Repositório Institucional da UFV Universidade Federal de Viçosa (UFV) instacron:UFV |
| ISSN: | 0141-8130 |
| Popis: | Spectroscopic and thermodynamic properties were determined for Debaryomyces hansenii UFV-1 extracellular and intracellular alpha-galactosidases. alpha-Galactosidases showed similar secondary structure compositions (alpha-helix, beta-sheet parallel and beta-turn). Effects of pH and temperature on the structure of alpha-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 alpha-galactosidases; it occurred as a thermodynamically driven process. Extracellular alpha-galactosidase, at pH 5.5, showed lower T(m) when compared to the intracellular enzyme. The CD and DSC data suggest that D. hansenii alpha-galactosidases have different behaviors although they possess some similar secondary structures. |
| Databáze: | OpenAIRE |
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