ISOLATION AND CHARACTERIZATION OF BROMELAIN ENZYME FROM PINEAPPLE AND ITS UTILIZATION AS ANTI-BROWNING AGENT

Abstract

Bromelain is a complex mixture of proteases and non-proteases components found in pineapple (Ananas cosmosus). The objective of this study was to find out a suitable extraction and purification process. Then characterize the pulp and stem bromelain enzyme and compare the effectiveness of those enzyme as anti-browning agent with commercial anti-browning agents. Both the stem and pulp extracted with sodium citrate buffer had higher protein content 1.178 and 0.332 mg/ml, respectively. Enzyme activity of stem bromelain was higher in extracted with sodium citrate buffer (0.0031 U/ml) and enzyme activity of pulp bromelain was higher in distilled water extraction (0.0085 U/ml). Bromelain with ethanol precipitation had higher protein content and enzyme activity than ammonium sulfate. The results showed that ammonium sulfate precipitation was achieved higher purification fold (1.76) and activity yield 27.53%. Bromelain showed a maximum activity at pH 8.5 and at 50°C temperature for 30 min. Stem bromelain with 1% concentration had better anti-browning activity than ascorbic acid and citric acid. There was no significant difference between ammonium sulfate and ethanol precipitation in terms of purification fold and yield. Although ethanol had achieved a lower purification fold but it had higher protein content and enzyme activity and it seems to be more suitable for bromelain recovery, based on process time, low ionic strength and low cost.