Abstract
Peroxidase, extracted from soybean seeds was isolated by ammonium sulfate precipitation technique and purified
by ion exchange and gel filtration chromatography. The crude enzyme having 17.29 U/mL activity and 1.586 U/mg
specific activity was subjected to ammonium sulfate precipitation technique for partial purification and the resulted
activity and specific activity were 12.85 U/mL and 5.68 U/mg respectively. After ion exchange chromatography
through DEAE-cellulose, fraction No. 43 exhibited maximum activity of 18 U/mL and specific activity of 9.5 U/mg.
This fraction was then applied to sephadex G-75 column and after elution, the activity and specific activity was
enhanced to 16.04 U/mL and 14.948 U/mg respectively.
Key Words: Soybean seeds, peroxidase purification, ion exchange chromatography, gel filtration
