Manuscript accepted on : December 24, 2007
Published online on: 03-02-2016
Cilem Cimen, Halit Demir, Aycan GUr and Senol Kubilay
Science and Arts Faculty, Department of Chemistry, Yuzuncu Yil University, Van - 650 80 (Turkey)
ABSTRACT: 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.
KEYWORDS: Polyphenol oxidase; characterization; purification; inhibitor; kinetics
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| Copy the following to cite this article: Cimen C, Demir H, GUr A, Kubilay S. Investigations of the inhibition kinetics of some drugs and chemicals on enzyme of polyphenol oxidase purified from Apricot’s (Salak). Biosci Biotechnol Res Asia 2007;4(2) |
| Copy the following to cite this URL: Cimen C, Demir H, GUr A, Kubilay S. Investigations of the inhibition kinetics of some drugs and chemicals on enzyme of polyphenol oxidase purified from Apricot’s (Salak). Biosci Biotechnol Res Asia 2007;4(2). Available from: https://www.biotech-asia.org/?p=6074 |
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