Abstract

Dilip B. Patil

The inhibition of polyphenol oxidase catalyzed oxidation of catechol by sodium thiosulphate, sodium dithionite and sodium metabisulphite has been carried out on the basis of kinetic measurement of catechol oxidation. The concentration of catechol was varied in the range of 1.10 x 10-3 M to 2.75 x 10-3 M and that of inhibitors was maintained 8.50 x 10-6 M. The apparent Michaelis constants Kmapp and dissociation constants of enzyme-inhibitor complex, Ki were determined at pH 7.00 and temperature 27°C. These three organic compound shows competitive type of inhibition.

Catechol; polyphenol oxidase; inorganic inhibitors

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