Tetracycline inhibition of a lipase from Corynebacterium acnes.

A lipase which hydrolyzes triglycerides (tricaprylin and trilaurin) and naphthyl laurate was obtained from the broth of Corynebacterium acnes cultures by ammonium sulfate fractionation. Ca(2+) and sodium taurocholate stimulated activity of the enzyme. Ethylenediaminetetraacetic acid (EDTA) did not inhibit activity of the Ca(2+)-activated enzyme, but lipolytic activity was inhibited by EDTA in the absence of Ca(2+). Tetracycline (10(-4)m) produced a slight inhibition of the lipase activity with 5 x 10(-5)m or less showing no effect on the lipase activity. However, complete inhibition by tetracycline at 10(-4)m was observed for Ca(2+)-activated enzyme. Tetracycline inhibition of the C. acnes lipase could be demonstrated at concentrations as low as 10(-6)m.