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. 1985 Apr;27(4):612-4.
doi: 10.1128/AAC.27.4.612.

Biochemical properties of beta-lactamase produced by Flavobacterium odoratum

K Sato, T Fujii, R Okamoto, M Inoue, S Mitsuhashi

Biochemical properties of beta-lactamase produced by Flavobacterium odoratum

K Sato et al. Antimicrob Agents Chemother. 1985 Apr.

Abstract

A constitutively produced beta-lactamase was purified from Flavobacterium odoratum GN14053. The purified enzyme gave a single protein band on polyacrylamide gel electrophoresis. The isoelectric point was 5.8, and the molecular weight was estimated to be about 26,000. The enzyme activity was inhibited by EDTA, iodine, p-chloromercuribenzoate, HgCl2, and CuSO4 but not by clavulanic acid, sulbactam, imipenem, and cephamycin derivatives. The enzyme showed a broad substrate profile, hydrolyzing oxyiminocephalosporins, cephamycins, imipenem, and some penicillins.

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