| 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 | 02003 | |
| Number of page(s) | 15 | |
| Section | Technology and Innovation | |
| DOI | https://doi.org/10.1051/bioconf/202622102003 | |
| Published online | 12 February 2026 | |
Antioxidant activity of catfish (Pangasius sp.) protein hydrolyzed by alcalase enzyme
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
Protein hydrolysis using alcalase enzyme yields a high degree of hydrolysis, generating bioactive peptides with potential applications as nutraceuticals and functional food ingredients. Striped catfish (Pangasius sp.), characterized by its high protein and moderate fat content, represents a promising source of antioxidant peptides. This study aimed to evaluate the antioxidant activity of striped catfish protein hydrolysates produced by alcalase hydrolysis and subsequently fractionated using ultrafiltration. Hydrolysis was conducted with alcalase at concentrations of 1%, 2%, and 3%, followed by ultrafiltration through a 3 kDa MWCO membrane. Antioxidant activity was assessed using DPPH and ABTS assays. The highest degree of hydrolysis (43.37%) was observed at 3% enzyme concentration. The <3 kDa fraction exhibited strong antioxidant activity with IC50 values of 21.97 ppm (DPPH) and 3.28 ppm (ABTS). These findings demonstrate that ultrafiltration effectively produces smaller peptides with enhanced antioxidant activity.
© 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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