Title:Characterization of a Solvent-tolerant Manganese Peroxidase from Pleurotus pulmonarius and its Application in Dye Decolorization
VOLUME: 6 ISSUE: 4
Author(s):Bruna Polacchine da Silva, Rubia Carvalho Gomes Correa, Camila Gabriel Kato, Daniela Farani de Souza, Adelar Bracht and Rosane Marina Peralta*
Affiliation:Department of Biochemistry, State University of Maringa, Maringa, Department of Biochemistry, State University of Maringa, Maringa, Department of Biochemistry, State University of Maringa, Maringa, Department of Biochemistry, State University of Maringa, Maringa, Department of Biochemistry, State University of Maringa, Maringa, Department of Biochemistry, State University of Maringa, 87020-900, Maringa
Keywords:Azo dye, anthraquinonic dye, biological decolorization, enzyme purification, manganese peroxidase, Pleurotus
pulmonarius, white-rot fungi.
Abstract:Background: Manganese peroxidase (MnP) is a common extracellular ligninolytic peroxidase produced by
Pleurotus spp. It catalyzes the H2O2-dependent oxidation of Mn2+ into highly reactive Mn3+, which in turn oxidizes
phenolic and nonphenolic compounds including a large list of xenobiotics such as synthetic dyes.
Objective: To purify and characterize the MnP of Pleurotus pulmonarius and to evaluate its capability to decolorize
synthetic dyes.
Methods: P. pulmonarius was cultured for 14 days under solid state conditions using pineapple waste as substrate.
Under this condition, MnP was the main ligninolytic enzyme found in the culture filtrates. The enzyme
was purified to apparent electrophoretic homogeneity through acetone precipitation and gel filtration using a
Sephadex G-100 column.
Results: MnP was purified 12.1-fold with a yield of 28.4% and a specific activity of 135.52 U/mg protein. The
42 kDa-monomeric protein was active over a large range of pH (4.0-6.0) and at a temperature of 50°C. The enzyme
was stable at temperatures up to 40°C. At -20°C, it was stable for at least 6 months. The KM for Mn2+ and
H2O2 at pH 4.5 and 40°C were 19.2 and 16.8 µM, respectively. The enzyme was strictly dependent on Mn2+ for
oxidizing phenolic and nonphenolic compounds. It showed high activity and stability in the presence of organic
solvents such as acetone, ethanol, isopropanol and acetonitrile, and was able to decolorize the anthraquinonic
dye remazol brilliant blue R and the azo dye Congo red in the presence of 1 M Na2SO4 and NaCl.
Conclusion: The properties of the P. pulmonarius MnP certainly make this enzyme a good agent for textile dye
effluent treatment.
