Acta NaturaeActa NaturaeActa Naturae2075-8251Acta Naturae Ltd1076010.32607/20758251-2010-2-2-82-87ArticlesСтатьиResearch ArticleInfluence of Ion Strength and pH on Thermal Stability of Yeast Formate DehydrogenaseInfluence of Ion Strength and pH on Thermal Stability of Yeast Formate DehydrogenaseTishkovV I

Department of Chemical Enzymology, Faculty of Chemistry

vitishkov@gmail.comUglanovaS V

Department of Chemical Enzymology, Faculty of Chemistry

FedorchukV V

Department of Chemical Enzymology, Faculty of Chemistry

SavinS SLomonosov Moscow State UniversityInnovations and High Technologies MSU LtdBach Institute of Biochemistry, Russian Academy of SciencesEmanuel Institute of Biochemical Physics, Russian Academy of SciencesLomonosov Moscow State UniversityInnovations and High Technologies MSU LtdBach Institute of Biochemistry, Russian Academy of Sciences1506201022VOL 2, NO2 (2010)ТОМ 2, №2 (2010)828717012020Copyright ©; 2010, Tishkov V.I., Uglanova S.V., Fedorchuk V.V., Savin S.S.Copyright ©; 2010, Tishkov V.I., Uglanova S.V., Fedorchuk V.V., Savin S.S.2010Tishkov V.I., Uglanova S.V., Fedorchuk V.V., Savin S.S.Tishkov V.I., Uglanova S.V., Fedorchuk V.V., Savin S.S.https://creativecommons.org/licenses/by/4.0https://actanaturae.ru/2075-8251/article/view/10760

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 oC 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 ∆≠ 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.

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