Email this article Influence of Ion Strength and pH on Thermal Stability of Yeast Formate Dehydrogenase
- Authors: Tishkov VI1,2,3, Uglanova SV1,4, Fedorchuk VV1, Savin SS2,3
-
Affiliations:
- Lomonosov Moscow State University
- Innovations and High Technologies MSU Ltd
- Bach Institute of Biochemistry, Russian Academy of Sciences
- Emanuel Institute of Biochemical Physics, Russian Academy of Sciences
- Issue: Vol 2, No 2 (2010)
- Pages: 82-87
- Section: Articles
- URL: https://actanaturae.ru/2075-8251/article/view/10760
- DOI: https://doi.org/10.32607/20758251-2010-2-2-82-87
- ID: 10760
Cite item
Abstract
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.
Full Text
Influence of Ion Strength and pH on Thermal Stability of Yeast Formate Dehydrogenase×
About the authors
V I Tishkov
Lomonosov Moscow State University; Innovations and High Technologies MSU Ltd; Bach Institute of Biochemistry, Russian Academy of Sciences
Email: vitishkov@gmail.com
Department of Chemical Enzymology, Faculty of Chemistry
S V Uglanova
Lomonosov Moscow State University; Emanuel Institute of Biochemical Physics, Russian Academy of SciencesDepartment of Chemical Enzymology, Faculty of Chemistry
V V Fedorchuk
Lomonosov Moscow State UniversityDepartment of Chemical Enzymology, Faculty of Chemistry
S S Savin
Innovations and High Technologies MSU Ltd; Bach Institute of Biochemistry, Russian Academy of Sciences
References
- Vinals C., Depiereux E., Feytmans E. // Biochem. Biophys. Res. Commun. 1993. V. 192. P. 182-188.
- Tishkov V.I., Popov V.O. // Biomol. Eng. 2006. V. 23. P. 89-110.
- Lamzin V.S., Dauter Z., Popov V.O., et al. // J. Mol. Biol. 1994. V. 236. P. 759-785.
- Filippova E.V., Polyakov K.M., Tikhonova T.V., et al. // Kristallographia. 2006. V. 51. P. 627-631.
- Schirwitz K., Schmidt A., Lamzin V.S. // Protein Sci. 2007. V. 16. P. 1146-1156.
- Sadykhov E.G., Serov A.E., Yasnyi I.E, et al. // Vestnik MGU. 2 Ed. Khimia. 2006. V. 47. P. 31-34.
- Shabalin I.G., Serov A.E., Skirello O.E. et al. // Crystallography Reports . 2010. V.55. N5. P.855-859
- Fedorchuk V.V., Galkin A.G., Yasny I.E. et al. // Biochemistry (Moscow). 2002. V. 67. P. 1145-1151.
- Bommarius A.S., Schwarm M., Stingl K., et al. // Tetrahedron-Asymmetry. 1995. V. 6. P. 2851-2888.
- Rojkova A.M., Galkin A.G., Kulakova L.B., et al. // FEBS Lett. 1999. V. 445. P. 183-188.
- Felber S. Optimierung der NAD-abhangigen Formiatdehydrogenase aus Candida boidinii fur den Einsatz in der Biokatalyse: PhD Thesis. Dusseldorf: Heinrich-Heine University of Dusseldorf, 2001. URL: http://diss.ub.uni-duesseldorf.de/ebib/diss/file?dissid=78
- Sadykhov E., Serov A., Voinova N., et al. // Appl. Biochem. Microbiol. 2006. V. 42. P. 236-240.
Supplementary files
