Extraction and biochemical characterization of a peroxidase from soybean (Glycine max) seed coats

فاقد چكيده

Plants food wastes have been given much less attention or even disregarded. In some instances, however, oxidative enzymes from residual plant tissues have been shown to effectively degrade recalcitrant pollutants. Soybean seed coat 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 temperatures. In this study, a systematic evaluation of the biocatalytic properties of SBP was carried out. The enzyme exhibited highest activity and stability at pH 6.0 and retained over 75% of the maximum activity for 12 hours. SBP also showed 2.5 times higher activity at a temperature of 65°C when compared to the activity at room temperature. The SBP was found to be heat-stable with 95% of the enzymatic activity remaining after heat treatment at 75°C and for 30min. 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 20% (v/v) acetone. The enzyme activity was reduced with an increase in concentration of the organic solvent.