Characterization of a Solvent-Tolerant Manganese Peroxidase (MnP) from G anoderma Lucidum and Its Application in Fruit Juice Clarification

Abstract

Manganese peroxidase (MnP) is necessary in fruit juice clarification for the degradation of phenolic compounds. In the present study, MnP was produced using basal medium supplemented with tamarind shell (1% w/v), ethanol (2% v/v) and gallic acid (1 mM) to a maximum activity of 65 U/mL. A 43.0 kDa MnP was purified by ammonium sulfate fractionation, Sephadex G-100 and DEAE-cellulose column chromatography with 6.5-fold and 13% yield. The optimal activity of the purified MnP was achieved at pH 5.5 and temperature of 45C with 2,6-dimethoxyphenol as substrate. The inhibitors sodium azide, cyanide and EDTA inhibited the MnP activity up to 100, 93 and 84%, respectively. MnP showed high activity and stability in the presence of different metal ions, surfactants and organic solvents. Clarification of different fruit juices with MnP showed its potential application in the food and beverage industry. Practical Applications Manganese peroxidase (MnP) is extensively used in various applications, such as pulp delignification, dye decoloration, biotransformation, biosensor applications and fruit juice clarification. Ganoderma lucidum-derived purified MnP is a solvent-tolerant metalloenzyme that showed its potential for industrial application in clarification of various fruit juices. The stability of MnP in the presence of various divalent cations, surfactants and solvents suggests that it could be used in industrial effluent treatments as well as the food and beverage industry.