Soybean seed hull peroxidase (SBP) is an inexpensive oxidoreductive enzyme
and could potentially be used to oxidise/polymerise various organic polluta
nts present in the industrial and petrochemical wastes. SEP is able to reta
in its catalytic properties under wide ranges of pH and at elevated tempera
tures. In this study, a systematic evaluation of the biocatalytic propertie
s of SEP was carried out. The optimal pH fur SEP activity is pH 6.0 and sig
nificant activity was observed between 2.2 and 8.0. SEP also showed three t
imes higher activity at an elevated temperature of 80 degreesC 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 SEP acti
vity. SEP is fairly active in organic solvents. The enzyme exhibited highes
t activity in the presence of 16.67% (w/v) ethanol followed by acetone, met
hanol and acetonitrile. The enzyme activity was reduced with an increase in
concentration of the organic solvent. SEP also showed maximum activity at
different concentrations of acetone using a phosphate buffer, pH 6.0 than w
ith the other pH buffers. Benzene/acetone mixture seems to be another bette
r solvent system for SEP where it showed about 65% of its activity at 16.67
% (w/v) concentration. (C) 2001 Elsevier Science B.V. All rights reserved.