Activity of periplasmic hydrogenase of the intestinal sulfate-reducing bacteria
Journal Title: Біологія тварин - Year 2014, Vol 16, Issue 2
Abstract
In this paper we present a periplasmic hydrogenase activity of the sulfate-reducing bacteria Desulfovibrio piger Vib-7 and Desulfomicrobium sp. Rod-9 isolated from the human large intestine. The effect of temperature and pH as well as substrate concentration on the hydrogenase activity in the cell-free extracts of the D. piger Vib-7 and Desulfomicrobium sp. Rod-9 was studied. The optimal temperature for hydrogenase reaction is +35 °C and pH 8.0 for extracts of both bacterial strains. Based on experimental data, the analysis of the kinetic properties of the periplasmic hydrogenase by the studied bacteria was carried out. Our experimental data have shown that the kinetic curves of the periplasmic hydrogenase reaction have tendency to saturation. The kinetics of the activity in cell-free extracts of the studied bacteria was consistent to the zero-order reaction in the range of 0–20 min. A monotonic increase in the activity of the enzyme was observed under the influence of hydrogen in concentrations range from 100 until 2000 µM. The periplasmic hydrogenase activity, initial (instantaneous) reaction rate (205.67±18.91 μmol H2/min×mg–1 protein) and maximum rate of the hydrogenase reaction (2500219 μmol H2/min×mg–1 protein) were significantly higher in the cell-free extracts of the D. piger Vib-7 strain than Desulfomicrobium sp. Rod-9. Michaelis constants (Km) of the activity were similar to each other: 864±73 and 669±62 μM for D. piger Vib-7 and Desulfomicrobium sp. Rod-9, respectively. Although values of Km of both enzymes were similar and were not statistically different, they cross the vertical axis at different points.
Authors and Affiliations
I. V. Kushkevych, H. L. Antonyak
Keywords
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