شماره ركورد كنفرانس :
5048
عنوان مقاله :
Extraction and biochemical characterization of a peroxidase from soybean (Glycine max) seed coats
Author/Authors :
Farnoush ،Ghaemmaghami Petroleum and Chemical engineering department - Sharif University of Technology, Tehran, Iran , Sepideh ،Motamed Petroleum and Chemical engineering department - Sharif University of Technology, Tehran, Iran , Iran ،Alemzadeh Petroleum and Chemical engineering department - Sharif University of Technology, Tehran, Iran
كليدواژه :
catalytic properties , enzyme activity , organic solvents , oxidoreductive , soybean seed coat peroxidase
عنوان كنفرانس :
ششمين كنگره بين المللي مهندسي شيمي
چكيده لاتين :
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.