Isoenzyme multiplicity and characterization of recombinant manganese peroxidases from Ceriporiopsis subvermispora and Phanerochaete chrysosporium

We expressed cDNAs coding for manganese peroxidases (MnPs! from the basidio mycetes Ceriporiopsis subvermispora (MnP1) and Phanerochaete chrysosporium (H4) under control of the alpha -amylase promoter from. Aspergillus oryzae in Aspergillus nidulans. The recombinant proteins (rMnP1 and rH4) were expr essed at similar Levels and had molecular masses, both before and after deg lycosylation, that were the same as those described For the MnPs isolated f rom the corresponding parental strains. Isoelectric focusing (IEF) analysis of rH4 revealed several isoforms with pls between 4.83 and 4.06, and one o f these pls coincided with the pi described for H4 isolated from P. chrysos porium (pl 4.6). IEF of rMnP1 resolved four isoenzymes with pIs between 3.4 5 and 3.15, and the pattern closely resembled the pattern observed with MnP s isolated from C. subvermispora grown in solid-state cultures. We compared the abilities of recombinant MnPs to use various substrates and found that rH4 could oxidize o-dianisidine and p-anisidine without externally added m anganese, a property not previously reported for this MnP isoenzyme from P. chrysosporium.