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Applied and Environmental Microbiology, April 2000, p. 1754-1758, Vol. 66, No. 4
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Efficient Heterologous Expression in Aspergillus oryzae of a Unique Dye-Decolorizing Peroxidase, DyP, of Geotrichum candidum Dec 1

Yasushi Sugano, Ryosuke Nakano, Katsuya Sasaki, and Makoto Shoda*

Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8503, Japan

Received 22 October 1999/Accepted 31 December 1999

Efficient expression of the dye-decolorizing peroxidase, DyP, from Geotrichum candidum Dec 1 in Aspergillus oryzae M-2-3 was achieved by fusing mature cDNA encoding dyp with the A. oryzae alpha -amylase promoter (amyB). The activity yield of the purified recombinant DyP (rDyP) was 42-fold compared with that of the purified native DyP from Dec 1. No exogenous heme was necessary for the expression of rDyP in A. oryzae. From the N-terminal amino acid sequence analyses of native DyP and rDyP, the absence of a histidine residue in both DyPs, which was considered to be important for heme binding of DyP, was confirmed. These results suggest that rDyP without a typical heme-binding region produced by A. oryzae exhibits a function similar to that of native DyP.

* Corresponding author. Mailing address: Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 226-8503, Japan. Phone: 81-45-924-5274. Fax: 81-45-924-5276. E-mail: mshoda{at}res.titech.ac.jp.

Applied and Environmental Microbiology, April 2000, p. 1754-1758, Vol. 66, No. 4
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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