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Isolation, purification, and characterization of the PR oxidase from penicillium roqueforti
1Department of Biochemistry, National Yang-Ming University, Taipei, Taiwan, Republic of China.
Applied and Environmental Microbiology
|December 3, 1998
Abstract:
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 degreesC.
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