TY - JOUR
T1 - Stability Test of Partially Purified Bromelain from Pineapple (Ananas comosus (L.) Merr) Core Extract in Artificial Stomach Fluid
AU - Setiasih, S.
AU - Adimas, A. Ch D.
AU - Dzikria, V.
AU - Hudiyono, S.
N1 - Publisher Copyright:
© Published under licence by IOP Publishing Ltd.
PY - 2018/2/7
Y1 - 2018/2/7
N2 - This study aimed to isolate and purify bromelain from pineapple core (Ananascomosus (L.) Merr) accompanied by a stability test of its enzyme activity in artificial gastric juice. Purification steps start with fractionation by a precipitation method were carried out stepwise using several concentration of ammonium sulfate salt, followed by dialysis prosess and ion exchange chromatography on DEAE-cellulose column. Each step of purification produced an increasing specific activity in enzyme fraction, starting with crude extract, respectively: 0.276 U/mg; 14.591 U/mg; and 16.05 U/mg. Bromelain fraction with the highest level of purity was obtained in 50-80% ammonium sulphate fraction after dialyzed in the amount of 58.15 times compared to the crude extract. Further purification of the enzyme by DEAE-cellulose column produced bromelain which had a purity level 160-fold compared to crude enzyme. The result of bromelain stability test in artificial stomach juice by milk clotting units assay bromelain fraction have proteolytic activity in clotting milk substrate. Exposing bromelain fraction in artificial stomach juice which gave the highest core bromelain proteolytic activity was achieved at estimated volume of 0.4-0.5 mL. Exposure in a period of reaction time to artificial stomach juice that contained pepsin showed relatively stable proteolytic activity in the first 4 hours.
AB - This study aimed to isolate and purify bromelain from pineapple core (Ananascomosus (L.) Merr) accompanied by a stability test of its enzyme activity in artificial gastric juice. Purification steps start with fractionation by a precipitation method were carried out stepwise using several concentration of ammonium sulfate salt, followed by dialysis prosess and ion exchange chromatography on DEAE-cellulose column. Each step of purification produced an increasing specific activity in enzyme fraction, starting with crude extract, respectively: 0.276 U/mg; 14.591 U/mg; and 16.05 U/mg. Bromelain fraction with the highest level of purity was obtained in 50-80% ammonium sulphate fraction after dialyzed in the amount of 58.15 times compared to the crude extract. Further purification of the enzyme by DEAE-cellulose column produced bromelain which had a purity level 160-fold compared to crude enzyme. The result of bromelain stability test in artificial stomach juice by milk clotting units assay bromelain fraction have proteolytic activity in clotting milk substrate. Exposing bromelain fraction in artificial stomach juice which gave the highest core bromelain proteolytic activity was achieved at estimated volume of 0.4-0.5 mL. Exposure in a period of reaction time to artificial stomach juice that contained pepsin showed relatively stable proteolytic activity in the first 4 hours.
UR - http://www.scopus.com/inward/record.url?scp=85046253001&partnerID=8YFLogxK
U2 - 10.1088/1757-899X/299/1/012016
DO - 10.1088/1757-899X/299/1/012016
M3 - Conference article
AN - SCOPUS:85046253001
SN - 1757-8981
VL - 299
JO - IOP Conference Series: Materials Science and Engineering
JF - IOP Conference Series: Materials Science and Engineering
IS - 1
M1 - 012016
T2 - 1st International Conference on Chemistry and Material Science, IC2MS 2017
Y2 - 4 November 2017 through 5 November 2017
ER -