The effects of β-cyclodextrin (β-CD) on polyphenol oxidation
catalyzed by apple polyphenol oxidase
(PPO), endive PPO, or mushroom tyrosinase have been compared.
β-CD forms a complex with
phenolic substrates of PPO by inclusion. Assuming a 1:1
β-CD/phenol stoichiometry, and assuming
that PPO is inactive on the complex β-CD/phenol,
K
D values were similar when determined
kinetically
by inhibition of apple PPO or endive PPO. However, the
experimental velocities found during
inhibition of mushroom tyrosinase by β-CD were higher than the values
predicted by this model.
In this latter case, it was assumed that mushroom tyrosinase is
able to act on the complex β-CD/phenol. A new model based on this assumption allows experimental
and calculated velocities to be
fit in presence of β-CD.
Keywords: Enzymatic browning; polyphenol oxidase; apple; endive; mushroom;
inhibition;
cyclodextrin
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