| Issue |
BIO Web Conf.
Volume 221, 2026
7th EMBRIO International Symposium: “Ocean for the Future: Integrating Marine Biodiversity, Sustainability, and Resilience” (EIS 2025)
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|---|---|---|
| Article Number | 02002 | |
| Number of page(s) | 14 | |
| Section | Technology and Innovation | |
| DOI | https://doi.org/10.1051/bioconf/202622102002 | |
| Published online | 12 February 2026 | |
Effect of ultrafiltration on the antioxidant activity of alcalase-hydrolyzed catfish (Clarias gariepinus) protein
Department of Aquatic Product Technology, Faculty of Fisheries and Marine Sciences, IPB University, Jl Agatis Kampus IPB Dramaga, Bogor, West Java 16680, Indonesia
* Corresponding author: This email address is being protected from spambots. You need JavaScript enabled to view it.
Abstract
Catfish (Clarias sp.) is one of Indonesia's leading aquaculture commodities with potential utilization as a source of functional protein. Protein hydrolysis using alcalase enzyme can generate bioactive peptides with antioxidant activity. These antioxidant properties are typically more prominent in low-molecular-weight peptides, thus requiring separation via ultrafiltration. This study aimed to evaluate the effect of ultrafiltration on the antioxidant activity of catfish protein hydrolysate. Hydrolysis was carried out using alcalase at concentrations of 1%, 2%, and 3%, followed by fractionation using a 3 kDa molecular weight cut-off (MWCO) ultrafiltration membrane. Antioxidant activity was assessed using the DPPH and ABTS assays. The highest degree of hydrolysis (62,42%) was obtained at 3% enzyme concentration. The <3 kDa fraction exhibited the highest antioxidant activity, with IC50 values of 41,20 ppm (DPPH) and 2,80 (ABTS), both categorized as very strong antioxidants. These findings indicate that ultrafiltration is an effective method for enriching short peptides with high antioxidant potential.
© The Authors, published by EDP Sciences, 2026
This is an Open Access article distributed under the terms of the Creative Commons Attribution License 4.0, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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