DOI : https://doi.org/10.18517/ijaseit.14.4.19647

Comparison of Physicochemical Properties of Barracuda (Sphyraena barracuda Edwards, 1771) Skin Collagen Hydrolyzed Using Two Different Pepsin Sources

Leshanthiy A/P K Santhi Rasegaran (1), Abdul Aziz Jaziri (2), Ahmad Hazim Abdul Aziz (3), Rossita Shapawi (4), Ruzaidi Azli Mohd Mokhtar (5), Wan Norhana Md. Noordin (6), Nurul Huda (7), Rahmi Nurdiani (8)
(1) Faculty of Food Science and Nutrition, Universiti Malaysia Sabah, Jalan UMS, Kota Kinabalu, 88400, Sabah, Malaysia
(2) Faculty of Food Science and Nutrition, Universiti Malaysia Sabah, Jalan UMS, Kota Kinabalu, 88400, Sabah, Malaysia
(3) Faculty of Food Science and Nutrition, Universiti Malaysia Sabah, Jalan UMS, Kota Kinabalu, 88400, Sabah, Malaysia
(4) Higher Institution Centre of Excellence (HICoE), Borneo Marine Research Institute, Universiti Malaysia Sabah, Jalan UMS 88400, Kota Kinabalu, Sabah, Malaysia
(5) Biotechnology Research Institute, Universiti Malaysia Sabah, Jalan UMS, Kota Kinabalu 88400, Sabah, Malaysia
(6) Fisheries Research Institute, Batu Maung, 11960, Penang, Malaysia
(7) Faculty of Sustainable Agriculture, Universiti Malaysia Sabah. Sandakan 90509, Sabah, Malaysia
(8) Department of Fish Product Technology, Faculty of Fisheries and Marine Science, Universitas Brawijaya, Malang 65415, East Java, Indonesia
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How to cite (IJASEIT) :
Rasegaran , Leshanthiy A/P K Santhi, et al. “Comparison of Physicochemical Properties of Barracuda (Sphyraena Barracuda Edwards, 1771) Skin Collagen Hydrolyzed Using Two Different Pepsin Sources”. International Journal on Advanced Science, Engineering and Information Technology, vol. 14, no. 4, Aug. 2024, pp. 1305-11, doi:10.18517/ijaseit.14.4.19647.
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This research focused on the comparison of extractability and physicochemical properties of barracuda (Sphyraena barracuda Edwards, 1771) skin collagens prepared using pepsins from bovine (PSC-B) and porcine (PSC-P). The PSC-P sample had a significantly higher (p<0.05) collagen extractability (31.16%) compared to the BCPB (19.48%). Based on the Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) profiles, all hydrolyzed collagens were identified as a type I collagen with two different alpha chains (α1 and α2).  The Infrared spectra showed that the collagen's triple-helical structure was maintained in the PSC-B and PSC-P samples, as mostly reported from other literatures. In terms of the thermal stability, the Tmax value of BCP-B (43.63°C) was greater than that of BCP-P (Tmax = 37.49°C), and their values were comparable to other literatures related on marine fish skin collagens. Overall, the by-product skin of barracuda (S. barracuda Edwards, 1771) can be utilized for alternative collagen products.

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