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Appl. Environ. Microbiol., 03 1996, 860-864, Vol 62, No. 3
Copyright © 1996, American Society for Microbiology

Efficient expression of a Phanerochaete chrysosporium manganese peroxidase gene in Aspergillus oryzae

P Stewart, RE Whitwam, PJ Kersten, D Cullen and M Tien
Department of Bacteriology, University of Wisconsin, Madison 53706, USA.

A manganese peroxidase gene (mnp1) from Phanerochaete chrysosporium was efficiently expressed in Aspergillus oryzae. Expression was achieved by fusing the mature cDNA of mnp1 with the A. oryzae Taka amylase promoter and secretion signal. The 3' untranslated region of the glucoamylase gene of Aspergillus awamori provided the terminator. The recombinant protein (rMnP) was secreted in an active form, permitting rapid detection and purification. Physical and kinetic properties of rMnP were similar to those of the native protein. The A. oryzae expression system is well suited for both mechanistic and site-directed mutagenesis studies.

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