摘要：Manganese peroxi.ases (MnPs) are i.teresti.g enzymes i. protei. engi.eeri.g, ai.ed at maxi.i.i.g i.dustri.l bi.processes such as li.ni. degradati.n and bi.fuel producti.n. cDNA of the secreted short-type of MnP from Phlebi. radi.ta (Pr-MnP3) has been successfully engi.eered and ampli.i.d by polymerase chai. reacti.n (PCR). Fi.e mutant genes (E40H, E44H, E40H/E44H, D186H and D186N) of recombi.ant Phlebi. radi.ta MnP3 (rPr-MnP3) were generated. The wi.d-type and the mutant genes were expressed i. Escheri.hi. coli.(W3110 strai.) and the resultant body protei.s were lysed, puri.i.d and refolded i.to acti.e enzymes. 6% - 7% recovery of pure and fully acti.e rPr-MnP3 for wi.d-type and mutants were obtai.ed and the avai.abi.i.y of rPr-MnP3 enzymes wi.l greatly faci.i.ate i.s structure-functi.n relati.nshi.s studi.s. rPr-MnP3 mass was characteri.ed usi.g SDS-PAGE and MALDi.TOF mass spectrometry. Molecular wei.ht of both the wi.d-type and mutant rPr-MnP3 enzymes was approxi.ately 36 kDa. Thi. descri.es the spectral characteri.ati.n of the wi.d-type and mutant rPr-MnP3 enzymes wi.h are very close si.i.ari.i.s;substanti.lly hi.h spi. haem enzymes. Therefore we report the engi.eeri.g, cloni.g, expressi.n, refoldi.g/acti.ati.n of MnP3 genes and preli.i.ary characteri.ati.n of the wi.d-type and mutant Phlebi. radi.ta MnP3 enzymes.