CHARACTERIZATION OF LATENT POLYPHENOL OXIDASE IN TABLE BEET - EFFECT OF SODIUM DODECYL-SULFATE

Polyphenol oxidase (EC 1.14.18.1) from table beet leaves was extracted in both soluble and membrane-bound forms. In both cases the enzyme ob tained was in its latent state. Polyphenol oxidase was kinetically cha racterised using 4-tert-butylcatechol as a substrate in both the laten t and activated enzyme forms. The latent form was activated by sodium dodecyl sulphate (SDS) so that characterisation was carried out in the presence and absence of SDS. The kinetic parameters for both soluble and membrane-bound forms at different pH values were calculated.