The present study is aimed at isolating and purifying the bromelain enzyme extracted from the cores of the fruit of the pineapple plant (Ananas comusus). The process of purification of the crude enzyme extract included, in sequence, fractionation through ammonium sulfate precipitation, dialysis, and ion-exchange chromatography. Fractionation of the crude enzyme extract with ammonium sulfate resulted in an increase of the specific activity. The fraction with the highest specific activity was that obtained by precipitation with 50-80 % ammonium sulfate. For this fraction, the specific activity was 8.683 U/mg and the degree of purity of the enzyme was 160 times greater than that of the crude enzyme extract. Further purification by column chromatography using diethylaminoethyl cellulose (DEAE-C) as ion-exchange medium produced six fractions (out of 92) characterized by peaks in proteolytic activity. In particular, the highest proteolytic activity (10.530 U/mg) was displayed by the fifth such fraction. The platelet aggregation inhibitory activity of the DEAE-C-purified bromelian extract was assayed through the Born's method that uses platelet-rich plasma and asetosal as positive control. The aggregation percent of this bromelain extract was measured to be 49.70% and its inhibition percent 46.89 %.
|Journal||Journal of Physics: Conference Series|
|Publication status||Published - 29 Jan 2020|
|Event||Basic and Applied Sciences Interdisciplinary Conference 2017, BASIC 2017 - , Indonesia|
Duration: 18 Aug 2017 → 19 Aug 2017
- Ananas comosus
- pineapple core
- specific activity