Purification and characterization of lignin peroxidases from Penicillium decumbens P6

Abstract

Peroxidases are essential enzymes in biodegradation of lignin and lignite which have been investigated intensively in the white-rot fungi. This is the first report of purification and characterization of lignin peroxidase from Penicillium sp. P6 as lignite degradation fungus. The results indicated that the lignin peroxidase of Penicillium decumbens P6 had physical and chemical properties and a N-terminal amino acid sequence different from the lignin peroxidases of white-rot fungi. The lignin peroxidase was isolated from a liquid culture of P. decumbens P6. This enzyme had a molecular weight of 46.3 KDa in SDS-PAGE and exhibited greater activity, temperature stability and wider pH range than those previously reported. The isolation procedure involved (NH 4 ) 2 SO 4 precipitation, ion-exchange chromatography on DEAE-cellulose and CM-cellulose, gel filtration on Sephadex G-100, and non-denaturing, discontinuous polyacrylamide gel electrophoresis. The K m and V max values of this enzyme using veratryl alcohol as substrate were 0.565 mmol L )1 and 0.088 mmol (mg protein) )1 min )1 respectively. The optimum pH of P6 lignin peroxidase was 4.0, and 70.6% of the relative activity was remained at pH 9.0. The optimum temperature of the enzyme was 45°C.

Peroxidase from Bacillus sp. VUS and its role in the decolorization of textile dyes

“…VUS was able to degrade dyes [11] and induced the dye-degrading enzymes peroxidase, laccase, and tyrosinase during the degradation of dyes. Two chromatography steps were adequate to purify peroxidase from this species, compared with P. decumbens P6 [14] required four steps. Unique dye-decolorizing peroxidase, DyP, purified from Geotrichum candidum Dec 1 also required three steps for purification [15].…”

Concentration of fungal ligninolytic enzymes by ultrafiltration and their use in distillery effluent decolorization

“…The molecular weight of MnP is reported to be in the range of 44-48 kDa (Hamman et al 1997;Pérez et al 1998). The lignin peroxidase isolated from a liquid culture of Penicillium decumbens had a molecular weight of 46.3 kDa (Yang et al 2005). The subunit molecular weight range of whiterot fungal LiP was 38-47 kDa (Fakoussa and Hofrichter 1999).…”

Enhanced production of ligninolytic enzymes and decolorization of molasses distillery wastewater by fungi under solid state fermentation

“…LiP has been reported from Aspergillus sp., isolated from a mangrove area whose best activity was in coir pith substrate at 3% concentration (Ahammed and Prema 2002). Recently LiP production by Penicillium decumbens was reported (Yang et al 2005). Although the enzymatic system related with decolorization of melanoidins is yet to be completely understood, it seems greatly connected with fungal ligninolytic mechanisms.…”