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Influence of Ion Strength and pH on Thermal Stability of Yeast Formate Dehydrogenase

The kinetics of the thermal inactivation of recombinant wild–type formate dehydrogenase from Candida boidinii yeast was studied in the temperature range of 53–61(o)C and pH 6.0, 7.0, and 8.0. It was shown that the loss of the enzyme’s activity proceeds via a monomolecular mechanism. Activation param...

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Detalles Bibliográficos
Autores principales: Tishkov, V.I., Uglanova, S.V., Fedorchuk, V.V., Savin, S.S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: A.I. Gordeyev 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347553/
https://www.ncbi.nlm.nih.gov/pubmed/22649645
Descripción
Sumario:The kinetics of the thermal inactivation of recombinant wild–type formate dehydrogenase from Candida boidinii yeast was studied in the temperature range of 53–61(o)C and pH 6.0, 7.0, and 8.0. It was shown that the loss of the enzyme’s activity proceeds via a monomolecular mechanism. Activation parameters ∆Н(­) and ∆S(­) were calculated based on the temperature relations dependence of inactivation rate constants according to the transition state theory. Both parameters are in a range that corresponds to globular protein denaturation processes. Optimal conditions for the stability of the enzyme were high concentrations of the phosphate buffer or of the enzyme substrate sodium formate at pH = 7.0.