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Bromoperoxidases from Penicillus capitatus, Penicillus lamourouxii and Rhipocephalus phoenix.

ABSTRACT: The isolation and purification of bromoperoxidases from three marine subtropical green algae is described. In the presence of KBr and H2O2, each halide-specific enzyme catalyses the bromination of monochlorodimedone (2-chloro-5,5-dimethylcyclohexane-1,3-dione) to bromochlorodimedone (2-bromo-2-chloro-5,5-dimethylcyclohexane-1,3-dione). The enzymes also catalyse the oxidation of pyrogallol, o-phenylenediamine and I- to I3-. Preliminary characterization of these enzymes reveals acidic pH optima, high thermal stability, sensitivity to higher H2O2 concentrations, and apparent molecular weights ranging from 48000 to 60000.

SUBMITTER: Baden DG

PROVIDER: S-EPMC1162509 | biostudies-other | 1980 Apr

REPOSITORIES: biostudies-other

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Dataset Information

Bromoperoxidases from Penicillus capitatus, Penicillus lamourouxii and Rhipocephalus phoenix.

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