Comparison of biochemical properties and thermal inactivation of membrane-bound polyphenol oxidase from three apple cultivars (Malus domestica Borkh)

A comparative study of the properties of membrane‐bound polyphenol oxidase (mPPO) from three apple cultivars, namely Red Fuji (FJ), Granny Smith (GS) and Golden Delicious (GD), was carried out for the first time. Data indicate that mPPOs from three cultivars exhibit significantly different properties. GS mPPO had the strongest affinity to catechol, but FJ mPPO had the highest maximum velocity. Red Fuji (FJ) mPPO had the significantly higher activity than those of GD and GS mPPOs. Red Fuji (FJ) mPPO had the highest activity at pH 8.00, while GD and GS mPPOs at 4.50 and 7.50–8.00, respectively. Red Fuji (FJ) mPPO was more stable than GD and GS mPPOs over the pH range of 5.0–8.5. The optimal temperature for GS mPPO was within 70–75 °C, which is higher than those for mPPOs from FJ and GD. Thermal inactivation of the three mPPOs followed a first‐order kinetic model with different inactivation kinetic parameters.