Purification of bromelain enzyme from MD2 hybrid pineapple core by ultrafiltration and its antioxidative potential

• Published in: Science, Engineering and Health Studies
• Main Author: Tarmizi N.H.; Kamarudin N.S.; Johari A.S.; Zulkepli N.A.; Mokhtar N.; Ya’kub M.K.
• Format: Article
• Language: English
• Published: Silpakorn University 2023
• Online Access: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85192869826&partnerID=40&md5=52f99d426d5fb7379867affb668f9f06

Bromelain, a protease enzyme found in pineapple, is commonly recognized for its therapeutic applications. This study aimed to investigate the antioxidant activity of bromelain from MD2 pineapple core using the ultrafiltration method and assess bromelain antioxidant activities in correlation with its purity. A partially purified bromelain (PPB) was obtained using ammonium sulfate (50%), followed by centrifugal ultrafiltration as a purifying step for ultrafiltrate bromelain (UFB). The antioxidant activities of bromelain were evaluated by 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging assay and ferric ions reducing antioxidant power methods. Using the protein content of crude extract as a reference, the purification fold of PPB was 0.20-fold, while UFB was 3.25-fold. PPB and UFB showed DPPH scavenging activities with IC50 values of 67.60±9.55 µg/mL and 42.11±2.55 µg/mL, respectively. At a concentration of 1000 µg/mL, the reducing power of PPB and UFB was 30.89%±2.03% and 35.09%±1.59%, respectively, which were lower than that of ascorbic acid. The result shows an increase in bromelain antioxidant activities after the ultracentrifugation, concluding that ultrafiltration effectively preserves antioxidant potentials in bromelain. Bromelain is a medium antioxidant with medium potential as a free radical scavenger but has poor reducing power. © 2023 Silpakorn University. All rights reserved.