Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1

Efficient expression of the dye-decolorizing peroxidase, DyP, from Geotrich um 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 ac tivity yield of the purified recombinant DyP (rDyP) was 42-fold compared wi th that of the purified native DyP from Dec 1. No exogenous heme was necess ary far 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 resid ue in both DyPs, which was considered to be important for heme binding of D yP, was confirmed. These results suggest that rDyP without a typical heme-b inding region produced by A. oryzae exhibits a function similar to that of native DyP.