Abstract

ABSTRACT Polyphenol oxidase (PPO) was extracted from white grapes (var. Victoria, South Africa) and partially purified by ammonium sulfate precipitation. Detailed kinetic studies on thermal and high‐pressure inactivation of grape PPO were preformed in McIlvaine buffer (pH = 4.0), in reconstituted grape must and in grape must. Thermal inactivation of PPO in McIlvaine buffer followed a first‐order model while in reconstituted grape must and grape must a biphasic inactivation behavior has been observed. Under all conditions investigated, a first‐order kinetic model could describe the pressure inactivation data. It was found that PPO is more thermostable and pressure‐stable in must than in reconstituted grape must and McIlvaine buffer at the same pH = 4.0.

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