Purification and characterization of polyphenol oxidase enzyme from Iğdır apricot (Prunus armeniaca L.)

Abstract

In this study, polyphenol oxidase enzyme obtained from Iğdır apricot was purified with method of affinity chromatography. The apricot cultivar “şalak” was provided from Iğdır region. To purify polyphenol oxidase enzyme, obtained from Iğdır apricot, phosphate buffer at 7.3 pH was used and the homogenate was prepared. The homogenate was applied to activate sepharose 4B-tyrosine-paminobenzoic acid affinity column. For quantitative protein analyses, fractions obtained from column, and showing activity, was performed at 595 nm with coomassie blue method. In addition, optimum pH of enzyme, its optimum temperature, ionic strength effect and inhibition kinetics of some drugs and chemicals on enzyme were investigated. Optimum pH of enzyme and its optimum temperature were found to be 6 and 30oC, respectively. Furthermore, the study carried out on the ionic strength revealed that the highest activity was observed in concentration of 0.16 M (NH4)2SO4.