Isolation, Purification, and Characterization of the PR Oxidase from Penicillium roqueforti

AUTOR(ES)
FONTE

American Society for Microbiology

RESUMO

The PR oxidase, an extracellular enzyme, involved in the conversion of PR toxin into PR acid, was purified from the culture broth of Penicillium roqueforti ATCC 48936. The enzyme has a pI of 4.5 and a molecular mass of approximately 88 kDa, and it is a monomer. The optimum pH for this enzyme is ca. 4.0, and the optimum temperature is 50°C.

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