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Extraction and purification of bromelain from pineapple peelings (Ananas comosus

By: Abay-Abay, Ellah Jane C

Publisher: Cebi City ; CIT-U ; 2013DDC classification: T Ab18 2013 Summary: The extraction and purification of Bromelain from pineapple (AnanasComosus) peelings are performed. Specifically, the amount and activity of the extracted bromelain from the peelings of the Smooth Cayenne Philippine pineapple cultivar is determined. Bromelain is separated and purified using Polyethylene Glycol (PEG)-Potassium Phosphate Aqueous Two-Phase System at different pH values 5, 6, 7, & 8 and at different w/w PEG-salt concentrations of 18%-14% and 20%-16%. It is assayed for its enzymatic activity via Casein Digestion Unit (CDU) and Bradford method for the protein quantification of the pure extract. It is found that optimum protein concentration is obtained at pH 7.0 and 20% PEG-16% salt ATP system at about 0.66121878µg/ml. CDU results for the proteolytic activity is maximum at 0.345169151 micromoles of L-Tyrosine equivalent released for pH 7.0 18%-14% ATPs concentration. The protein partition (Kp) of 0.862822796 to 0.904185013, enzymatic partition (Ke) of 0.209390765 to 2.654809839, purification factor (PF) of 0.231579557 to 3.076888848, selectivity(S) of 0.231579557 to 3.076888848, and the yield(Y) of 68.68% to 75.52% are obtained.

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Item type	Current location	Home library	Call number	Status	Date due	Barcode	Item holds
RESERVED BOOKS	COLLEGE LIBRARY	COLLEGE LIBRARY	T Ab18 2013 (Browse shelf)	Available		T1781

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The extraction and purification of Bromelain from pineapple (AnanasComosus) peelings are performed. Specifically, the amount and activity of the extracted bromelain from the peelings of the Smooth Cayenne Philippine pineapple cultivar is determined. Bromelain is separated and purified using Polyethylene Glycol (PEG)-Potassium Phosphate Aqueous Two-Phase System at different pH values 5, 6, 7, & 8 and at different w/w PEG-salt concentrations of 18%-14% and 20%-16%. It is assayed for its enzymatic activity via Casein Digestion Unit (CDU) and Bradford method for the protein quantification of the pure extract. It is found that optimum protein concentration is obtained at pH 7.0 and 20% PEG-16% salt ATP system at about 0.66121878µg/ml. CDU results for the proteolytic activity is maximum at 0.345169151 micromoles of L-Tyrosine equivalent released for pH 7.0 18%-14% ATPs concentration. The protein partition (Kp) of 0.862822796 to 0.904185013, enzymatic partition (Ke) of 0.209390765 to 2.654809839, purification factor (PF) of 0.231579557 to 3.076888848, selectivity(S) of 0.231579557 to 3.076888848, and the yield(Y) of 68.68% to 75.52% are obtained.

000-099

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