Tetracycline Inhibition of a Lipase from Corynebacterium acnes

Abstract

A lipase which hydrolyzes triglycerides (tricaprylin and trilaurin) and naphthyl laurate was obtained from the broth of Corynebacterium acnes cultures by ammonium sulfate fractionation. Ca²⁺ and sodium taurocholate stimulated activity of the enzyme. Ethylenediaminetetraacetic acid (EDTA) did not inhibit activity of the Ca²⁺-activated enzyme, but lipolytic activity was inhibited by EDTA in the absence of Ca²⁺. Tetracycline (10⁻⁴m) produced a slight inhibition of the lipase activity with 5 × 10⁻⁵m or less showing no effect on the lipase activity. However, complete inhibition by tetracycline at 10⁻⁴m was observed for Ca²⁺-activated enzyme. Tetracycline inhibition of the C. acnes lipase could be demonstrated at concentrations as low as 10⁻⁶m.