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 obtained was in its latent state. Polyphenol oxidase was kinetically characterised using 4-tert-butylcatechol as a substrate in both the latent 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.
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Escribano et al. (1997) studied this question.
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