Investigation of biocatalytic properties of soybean seed hull peroxidase

Soybean seed hull peroxidase (SBP) is an inexpensive oxidoreductive enzyme and could potentially be used to oxidise/polymerise various organic pollutants present in the industrial and petrochemical wastes. SBP is able to retain its catalytic properties under wide ranges of pH and at elevated temperatures. In this study, a systematic evaluation of the biocatalytic properties of SBP was carried out. The optimal pH for SBP activity is pH 6.0 and significant activity was observed between 2.2 and 8.0. SBP also showed three times higher activity at an elevated temperature of 80°C and at pH 6.0 when compared to the activity at room temperature. The pH and temperature of the reaction mixture were found to significantly influence the SBP activity. SBP is fairly active in organic solvents. The enzyme exhibited highest activity in the presence of 16.67% (w/v) ethanol followed by acetone, methanol and acetonitrile. The enzyme activity was reduced with an increase in concentration of the organic solvent. SBP also showed maximum activity at different concentrations of acetone using a phosphate buffer, pH 6.0 than with the other pH buffers. Benzene/acetone mixture seems to be another better solvent system for SBP where it showed about 65% of its activity at 16.67% (w/v) concentration.