Abstract

This study was carried out to characterize a crude extract from pineapple peel after precipitation by three methods with the aim of obtaining an enzymatic extract from agro-industrial waste. The characterization of these extracts involved the determination of both protein content and specific protease activities. The effects of pH and temperature on specific protease activity and on the stability of the extracts were also evaluated. The optimal values of specific activity for the crude extract (CE) were pH 6.0 (5.76 U mg−1 protein) and 7.0 (5.71 U mg−1 protein) and a temperature of 70 °C (16 U mg−1 protein). The average values for the relative specific activity were 17.4% (pH 3.0 to 9.0) and 42.7% (at 30, 50, and 70 °C). The ethanolic extract had the highest specific activity (10.7 U mg−1 protein) in comparison to the best results obtained for the isoelectric precipitation (7.7 U mg−1 protein) and the ammonium sulfate precipitation (4.7 U mg−1 protein). Moreover, the ethanolic extract was more stable than the CE, retaining 60.9% and 53.7% of the initial specific activity during the evaluation of the stability at different pH and temperature values, respectively. The optimal values of pH and temperature were almost the same for the crude and the ethanolic extracts. In addition, the ethanolic extract was more stable than the CE in the experimental conditions tested in this work.

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