Investigation of biocatalytic properties of soybean seed hull peroxidase

Citation
Zh. Geng et al., Investigation of biocatalytic properties of soybean seed hull peroxidase, CATAL TODAY, 64(3-4), 2001, pp. 233-238
Citations number
11
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
CATALYSIS TODAY
ISSN journal
09205861 → ACNP
Volume
64
Issue
3-4
Year of publication
2001
Pages
233 - 238
Database
ISI
SICI code
0920-5861(20010120)64:3-4<233:IOBPOS>2.0.ZU;2-U
Abstract
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.