Kinetics and Thermodynamics of Thermal Inactivation of β-Galactosidase from Aspergillus oryzae
| Autor: | Voltaire Sant’Ana, Jorge Luiz Ninow, Manuela Poletto Klein, Rafael C. Rodrigues, Plinho Francisco Hertz |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0106 biological sciences
Protein Denaturation lcsh:Biotechnology Kinetics β-Galactosidase Thermodynamics Activation energy Kinetic energy 01 natural sciences Modelling 0404 agricultural biotechnology Mathematical equations Aspergillus oryzae 010608 biotechnology lcsh:TP248.13-248.65 Thermal chemistry.chemical_classification Multidisciplinary biology 04 agricultural and veterinary sciences biology.organism_classification 040401 food science Enzyme structure Enzyme chemistry Enzyme Inactivation Weibull |
| Zdroj: | Brazilian Archives of Biology and Technology, Volume: 61, Article number: e18160489, Published: 13 SEP 2018 Brazilian Archives of Biology and Technology, Vol 61, Iss 0 (2018) Brazilian Archives of Biology and Technology v.61 2018 Brazilian Archives of Biology and Technology Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
| Popis: | For optimization of biochemical processes in food and pharmaceutical industries, the evaluation of enzyme inactivation kinetic models is necessary to allow their adequate use. Kinetic studies of thermal inactivation of β-galactosidase from Aspergillus oryzae were conducted in order to critically evaluate mathematical equations presented in the literature. Statistical analysis showed that Weibull model presented the best adequacy to residual enzymatic activity data through the processing time and its kinetic parameters as a function of the temperature, in the range of 58-66 oC. The investigation suggests the existence of a non-sensitive heat fraction on the enzyme structure, which is relatively stable up to temperatures close to 59 oC. Thermodynamic parameters were evaluated and showed that such β-galactosidase presents activation energy of 277 kJ mol-1 and that the enzyme inactivation is due to molecular structural changes. Results shown that the enzyme is quite stable for biotechnological applications. |
| Databáze: | OpenAIRE |
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