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.