Abstract

Dilip B. Patil

The inhibition of apple polyphenol oxidase catalyzed oxidation of catechol by sodium halides has been carried out on the basis of kinetic measurement of catechol oxidation. The concentration of catechol was varied in the range of 0.8 x 10-3 M to 2.0 x 10-3 M and that of inhibitors was maintained 8.0 x 10-4 M. The apparent Michaelis constant, kmapp and dissociation constant of enzyme-inhibitor complex, ki were determined at pH 7.00 and temperature 27.0 °C. All the halides shows competitive type of inhibition.

Apple polyphenol oxidase; oxidation of catechol; alkali salt inhibitors

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