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Appl Environ Microbiol. 1971 April; 21(4): 639-642
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Tetracycline Inhibition of a Lipase from Corynebacterium acnes

Eaton Laboratories, The Norwich Pharmacal Company, Norwich, New York 13815

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 x 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.