ObjectiveThe dye-decolorizing peroxidase from Bacillus amyloliquefaciens, BaDyP, was identified to be an efficient catalyst for the degradation of phenolic beta-ether lignin model dimer guaiacylglycerol-beta-guaiacyl ether (GGE) and dyes.ResultsEfeb gene encoding BaDyP from B. amyloliquefaciens MN-13 consisted of 1257 bp and the open reading frame encoded 418 amino acids. The efeb gene was expressed in Escherichia coli BL21 and a recombinant BaDyP of 50 kDa was achieved. The BaDyP exhibited activity in oxidizing GGE and decolorizing azo and triphenylmethane dyes. At pH 4.5 and 30 degrees C the BaDyP not only completely degraded GGE by the cleavage of beta-O-4 ether bond and C alpha-C-beta bond, and C alpha oxidation without any oxidative mediator, but also decolorized four synthetic dyes, including congo red, bromine cresol green, eriochrome black T and crystal violet. This was achieved with decolorization rates of 65.7%, 70.62%, 80.06% and 62.09%, respectively, after 72 h of incubation.ConclusionsBaDyP was identified as a bacteria peroxidase with great potential for the degradation of lignin and bioremediation of dye-contamination.