Antioxidant and α-Glucosidase Inhibitor Peptides from Pindang Fish Boiling Water | ||||
| Egyptian Journal of Aquatic Biology and Fisheries | ||||
| Article 28, Volume 29, Issue 3, May and June 2025, Page 433-451 PDF (517.88 K) | ||||
| DOI: 10.21608/ejabf.2025.427244 | ||||
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| Author | ||||
| Dali et al. | ||||
| Abstract | ||||
| Liquid pindang fish, the by-product water used during pindang boiling and typically discarded after processing, was investigated for its bioactive potential following peptide fractionation. The study aimed to evaluate the antioxidant and α-glucosidase inhibitory activities of peptide fractions obtained through ultrafiltration using membranes with molecular weight cut-offs (MWCO) of 3 kDa and 10 kDa. The total protein/peptide content was analyzed, and three bioactivity assays were employed: 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging, ferric reducing antioxidant power (FRAP), and α-glucosidase inhibition. Fractionation results demonstrated that peptides <3 kDa exhibited the highest antioxidant and α-glucosidase inhibitory activities, followed by the 3–10 kDa and >10 kDa fractions. Among the samples, the D15 <3 kDa fraction (peptides obtained after 15 minutes of hydrolysis with a semi-purified enzyme) showed the highest DPPH radical scavenging activity, with a value of 1.83 ± 0.01 mg AAE/mg protein, which was 2.49 times higher than the unfractionated sample. For FRAP activity, the C15 3 kDa fraction (15-minute hydrolysis using crude enzyme) exhibited the strongest reducing power, measured at 33.54 ± 2.75 mg TEAC/mg protein, which was 7.47 times greater than the unfractionated sample. Overall, the C15 <3 kDa peptide fraction demonstrated strong reducing power and α-glucosidase inhibition, while the D15 <3 kDa fraction was most effective in neutralizing DPPH radicals. These findings highlight the potential of liquid pindang fish waste as a valuable source of bioactive peptides with antioxidant and antidiabetic properties. | ||||
| Keywords | ||||
| Antioxidant peptide; Fractionation; α-glucosidase inhibition; Fisheries byproducts; Molecular size | ||||
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