Isolation, purification, and characterization of the PR oxidase from penicillium roqueforti
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.
Chang
SC
Department of Biochemistry, National Yang-Ming University, Taipei, Taiwan, Republic of China.
Lei
WY
Tsai
YC
Wei
YH