Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L)

Abstract

The diamine oxidase enzyme (DAO) can be isolated from mung bean sprouts (Vigna radiata L) through the process of extraction in phosphate buffer. Concentration and fractionation were performed by the addition of ammonium sulphate, (NH 4) 2 SO 4 saturation in stages and cold centrifuged at 10000 rpm. Enzyme activity of DAO crude and DAO fractionation results were tested using substrat histamin and measured with a spectrophotometer at a wavelength of 450 nm. This study revealed that the enzyme activity of the crude enzyme was1, 226 mU/mL, the fraction of 40-60% ammonium sulphate saturated had the highest activity which accounted for 3326 mU/mL and after gel filtration, the results for both activity and specific activity were 116 mU/mL and 185 mU/mg protein.