Abstract
It was shown that the presence of magnesium cations in the reaction mixture increases, approximately twofold, the activity of bacterial Escherichia coli and yeast Kluyveromyces lactis β-galactosidases but does not affect the activity of bovine liver and fungous Penicillium canescens β-galactosidases. The catalytic constants for E. coli and yeast K. lactis β-galactosidases in the presence of 0.01 M and in the absence of Mg2+ cations were determined (490 and 220 s−1 and 59.8 and 37.4 s−1, respectively). It was shown that the Michaelis constants for these two enzymes are higher in the presence of Mg2+ cations, that the thermal stability of E. coli and K. Lactis β-galactosidases is higher in the presence of 0.01 M Mg2+, and that the effective rate constants of thermal inactivation of the enzymes are two-to eightfold lower, depending on conditions, in the presence of Mg2+ cations. The maximum stabilizing effect of magnesium cations was observed at weak alkaline pH values (7.5–8.5).
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Original Russian Text © L.F. Atyaksheva, O.S. Pilipenko, O.M. Poltorak, E.S. Chukhrai, 2007, published in Zhurnal Fizicheskoi Khimii, 2007, Vol. 81, No. 7, pp. 1313–1317.
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Atyaksheva, L.F., Pilipenko, O.S., Poltorak, O.M. et al. Effect of magnesium cations on the activity and stability of β-galactosidases. Russ. J. Phys. Chem. 81, 1156–1159 (2007). https://doi.org/10.1134/S0036024407070266
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DOI: https://doi.org/10.1134/S0036024407070266