Abstract
Peroxidase (POD) associated with the browning of fresh-cut fruits and vegetableswas extracted from purple skin eggplant(Solanum melongena L.) and characterised using reliable spectrophotometric methods. Maximal POD activity was found at 35 °C and pH 6.0 with guaiacol as the substrate. The enzyme was stable at his optimal temperature (35 °C) and hisat pH stability was in the range of 5.6 - 6.6.Peroxidase retained its full activity in the presence of ion K+, Cu2+, Na+, Pb2+ and Ba2+ but were inhibited strongly by the ion Fe2+ and Mg2+ and the reducing agents as sodium thiosulfateand ascorbic acid. Effect of heattreatment on eggplant peroxidase showed that D-values decreased with increasing temperature, indicating faster peroxidase inactivation at higher temperatures.At 60 °C, the D-values ranged from 20.42 to 54.24 min. Hence, heat treatment at 60 °C for 30 min reduced browning of eggplant fruit.These data can be used to predict prevention of browning in the purple skin eggplantby thermal inactivation and the use of chimical agents onthe enzyme.
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