Characterization of a Solvent-tolerant Manganese Peroxidase from Pleurotus pulmonarius and its Application in Dye Decolorization

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, 87020-900, Maringa,Brazil

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.

Cite this article as:

da Silva Polacchine Bruna, Gomes Correa Carvalho Rubia, Kato Gabriel Camila, de Souza Farani Daniela, Bracht Adelar and Peralta Marina Rosane*, Characterization of a Solvent-tolerant Manganese Peroxidase from Pleurotus pulmonarius and its Application in Dye Decolorization, Current Biotechnology 2017; 6 (4) . https://dx.doi.org/10.2174/2211550105666160224004258