| Autor: |
Rasegaran, Leshanthiy A/P K Santhi, Jaziri, Abdul Aziz, Abdul Aziz, Ahmad Hazim, Shapawi, Rossita, Mohd Mokhtar, Ruzaidi Azli, Noordin, Wan Norhana Md., Nurdiani, Rahmi, Huda, Nurul |
| Předmět: |
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| Zdroj: |
International Journal on Advanced Science, Engineering & Information Technology; 2024, Vol. 14 Issue 4, p1305-1311, 7p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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