Effect of selected phenolic compounds on the membrane-bound adenosine triphosphatase of Staphylococcus aureus

Abstract

The effect of selected phenolic compounds on the membrane-bound ATPase activity of two strains of Staphylococcus aureus was studied. These phenolic compounds were: butylated hydroxyanisole (BHA), butylated hydroxytoluene (BHT), tertiary butylhydroquinone (TBHQ), propyl gallate (PG), p-coumaric, ferulic, caffeic acids, methyl paraben and propyl paraben. Cytoplasmic membrane-bound ATPase activity was measured in the presence of 0, 150, 300, 600 and 1200 μg ml −1 of each phenolic compound. Among all the compounds studied, only BHA was found to significantly stimulate the activity of the enzyme. In contrast, some of the compounds were found to significantly inhibit the activity of the enzyme as was the case of TBHQ, PG, p-coumaric acid, ferulic acid and caffeic acid. The remaining compounds did not influence the activity of the ATPase at any of the concentrations tested. Strain LP ATPase as stimulated less by BHA and inhibited to a greater extent by TBHQ and PG than was the enzyme from strain A100. In contrast, LP ATPase was less inhibited by p-coumaric acid and not affected by either ferulic or caffeic acid.