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Applied and Environmental Microbiology, December 1998, p. 5012-5015, Vol. 64, No. 12
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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

Shenq-Chyi Chang,* Wen-Yee Lei, Ying-Chieh Tsai, and Yau-Huei Wei

Department of Biochemistry, National Yang-Ming University, Taipei, Taiwan, Republic of China

Received 4 May 1998/Accepted 15 September 1998

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.

* Corresponding author. Mailing address: Department of Biochemistry, National Yang-Ming University, Taipei 112, Taiwan, Republic of China. Phone: 886-2-28267120. Fax: 886-2-28264843. E-mail: scchang{at}mailsrv.ym.edu.tw.

Applied and Environmental Microbiology, December 1998, p. 5012-5015, Vol. 64, No. 12
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.




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Copyright © 1998 by the American Society for Microbiology. All rights reserved.