Biochemical properties of beta-lactamase produced by Flavobacterium odoratum | Zendy

Kenichi Sato | Zendy; Tadashi Fujii | Zendy; R Okamoto | Zendy; Manabu Inoue | Zendy; S Mitsuhashi | Zendy

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Biochemical properties of beta-lactamase produced by Flavobacterium odoratum

Author(s) -

Kenichi Sato,

Tadashi Fujii,

R Okamoto,

Manabu Inoue,

S Mitsuhashi

Publication year - 1985

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.27.4.612

Subject(s) - isoelectric point , sulbactam , imipenem , biochemistry , enzyme , isoelectric focusing , flavobacterium , chemistry , microbiology and biotechnology , biology , antibiotics , bacteria , pseudomonas , antibiotic resistance , genetics

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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