Control of polyphenol oxidase in whole potatoes by low temperature blanching

摘要

Russet Burbank potatoes can be blanched up to 60 min at 50 degreesC without any loss in firmness and without appearance of browning on their peels, eyes or infected areas. Low temperature blanching (LTB) for 45 min did not cause a significant reduction in crude polyphenol oxidase (PPO) activity (12%). However, when heating time was extended to 60 min, the activity and specific activity of the enzyme were reduced by 27-45% and 22-43% respectively. The remaining enzyme extracted from heated potatoes was partially purified 3.3-3.75-fold by 0-95% ammonium sulphate precipitation and dialysis, and its kinetic parameters were determined. The comparison of the kinetic parameters of PPO in control (K-m=10.3 mM and V-max/K-m=0.15) and in 60 min heated potatoes (K-m=13 mM and V-max/K-m=0.054) indicated the reduced affinity of the remaining enzyme to its substrate. Thus, LTB at 50 degreesC for 60 min not only inactivated part of the PPO activity but also reduced the kinetic capacity of remaining enzyme. Extending heating time to 75 min caused the appearance of slight browning on the peels and eyes of potatoes and reduced their firmness. The observed browning was due to the sharp drop in the K-m that caused the activation of the PPO. Heating at 50 degreesC did not affect lipoxygenase activity, but the K-m of the enzyme dropped from 0.4 to 0.15 mM and the enzyme became kinetically more reactive at low substrate concentrations. Covalently bound pectin methylesterase considerably activated (38%) by heating and this caused the drop of pH in potato tissues.