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