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Abstract

PURIFICATION AND CHARACTERIZATION OF PEROXIDASE EXTRACTED FROM WHEAT BRAN

Mahmoud Hamid*, Hameed Majeed and Akeel Hussein Al-Assie

Abstract

This study was aimed to purify peroxidase extracted from wheat branand studying its biochemical characteristics. Wheat grains sampleswere collected from wheat crop field, and milled then wheat bran wascollected by sieving using flour sieve. Peroxidase was extracted fromwheat bran by using different extraction buffer solutions, thenperoxidase was purified by three steps of purification includesprecipitation with ammonium sulfate in a saturation ratio of 70 %, ionexchange chromatography through DEAE-Cellulose, and gel filtrationchromatography throughout sephadex G-100. Results showed that thespecific activity of purified enzyme was 510 u/mg, with a yield of 18% and purification foldof 5.1. Results of characterization of the purified enzyme indicates that enzyme molecularweight was 52000 dalton by using Gel filtration technique and the optimum pH for enzymeactivity and stability was 7 , and the optimal temperature of the enzyme activity was 50°c and45°c respectively. The activation energy for conversion of substrate to product was 10.18Kcal / mol.

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