Issue |
E3S Web Conf.
Volume 585, 2024
5th International Conference on Environmental Design and Health (ICED2024)
|
|
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Article Number | 06002 | |
Number of page(s) | 5 | |
Section | Health | |
DOI | https://doi.org/10.1051/e3sconf/202458506002 | |
Published online | 07 November 2024 |
Enzymatic treatments of collagen from barramundi (Lates Calcarifer) skin for production of bioactive peptides hydrolysates
1 Faculty of Chemical and Energy Engineering, Universiti Teknologi Malaysia, 81310 Johor Bahru, Johor, Malaysia.
2 Faculty of Food Science and Nutrition, Universiti Malaysia Sabah, UMS Road, 88400 Kota Kinabalu, Sabah, Malaysia.
3 Universitas Ciputra Surabaya, CBD Boulevard, Citraland Sambikerep, Surabaya 60129, Indonesia
4 Department of Chemical and Environmental Engineering, Malaysia-Japan International Institute of Technology, Universiti Teknologi Malaysia, 54100 Kuala Lumpur, Malaysia.
5 Innovation Centre in Agritechnology for Advanced Bioprocessing, Universiti Teknologi Malaysia, Pagoh Campus, 84600 Pagoh, Johor, Malaysia.
* Corresponding author: dnorulfairuz@utm.my
The utilization of barramundi skin, a by-product of the fish processing industry, as a prospective source of alternative collagen has been explored. To further broaden the prospect of barramundi collagen, its hydrolysate form (CH) was investigated using different enzymatic hydrolysis (alcalase and papain) at various concentration (1%, 2% and 3%). Degree of hydrolysis (DH) of the resulting hydrolysates were determined. The CH were then subjected to physico- chemical characterization including assessment of protein content, FTIR spectra, morphology, solubility and antioxidant properties. Among these, alcalase at a concentration of 1% exhibited notable efficacy, yielding a hydrolysate with DH of 56.5 %, 61.44% ABTS radical scavenging activity and 85% solubility across the pH range studied. Furthermore, both alcalase and papain- derived collagen hydrolysates demonstrated the capacity to disrupt the triple helix structure of crude collagen as observed through FTIR spectroscopy and scanning electron microscopy analysis. These results place collagen obtained from barramundi skin as a potential biotechnological alternative to produce highly potential bioactive peptide-containing hydrolysates.
© The Authors, published by EDP Sciences, 2024
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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