Investigations of the inhibition kinetics of some drugs and chemicals on enzyme of polyphenol oxidase purified from Apricot’s (Salak)

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Polyphenol oxidase (PPO) was purified from Igdir apricot, with a 367 fold purification of PPO by affinity chromatography being achieved. Amount of the protein was determined according to Bradford method. Vmax and Km values were found by means of Lineweaver- Burk graphs. Asetly salisilic acid, paracetamol, ascorbic acid (vitamin C), sodium sulphate, copper sulphate, glucose, sodium nitrite, sodium chlorure, glisine, sodium azide, 2-merkaptoethanol, tyrosine, citric acid, etilendiamin tetra acetic acid (EDTA) ve p-amino benzoic acid were used as inhibitor. Inhibition constants Ki of each inhibitor were found from Lineweaver-Burk graphs. It was found that the p-aminobenzoik acid function showed the highest inhibitory effect.

Polyphenol oxidase; characterization; purification; inhibitor; kinetics