Comparison of collagen characteristic from the skin and swim bladder of Gulf corvina (Cynoscion othonopterus)

Preparation and Characterization of Thermally Stable Collagens from the Scales of Lizardfish (Synodus macrops)

“…It has also been reported in the literature that the hydrolysis of telopeptide by pepsin might increase the free amino group, and this may have led to the higher wavenumber of PSC [40,42]. Moreover, the results of the CD spectrum obtained from the ASC and PSC was similar to the CD spectrum of gulf corvina collagen (positive absorption peaks at 221 nm and negative absorption peaks at 198 nm) [10], Perinereis nuntia cuticle collagen (positive absorption peaks at 221 nm and negative absorption peaks at 199 nm) [28], and Nile tilapia skin collagen (positive absorption peaks at 221 nm and negative absorption peaks at 197 nm) [16]. In addition, the XRD spectrum analysis showed that the distance between the molecular chains and the distance between their skeletons of the ASC and PSC were similar to the Pacific cod skin collagen [22] and the cuticle of the Perinereis nuntia collagen [28].…”

“…CD is a simple and effective technique to identify whether the triple helical structure is intact [22]. The CD spectrum of native collagen with a triple-helix structure shows a positive peak at 221 nm (maximum positive cotton effect), a negative peak at 198 nm (maximum negative cotton effect), and a crossover point (zero rotation) at approximately 213 nm [10,22]. As shown in Figure 2c, the CD spectrum of lizardfish scales ASC and PSC exhibited weak positive absorption peaks at 221 nm and 220 nm, respectively, and negative absorption peaks were observed at 198 nm and 197 nm, respectively, both with a crossover point at 213 nm.…”

“…Marine collagen has lower gelling and melting temperatures than mammalian collagen, but marine collagen is cheaper to extract and easier to prepare than mammalian collagen [8,9]. Marine collagen, such as that from sponges, jellyfish, squids, octopuses, cuttlefish, and fish skin, bone, and scales, comes from both marine vertebrates and invertebrates [9,10]. There is great demand for marine collagen, and this is now the main source of collagen globally.…”

“…There is great demand for marine collagen, and this is now the main source of collagen globally. Sourour Addad et al (2011) obtained collagen from Jellyfish [11], Tziveleka et al (2017) isolated the collagen from marine sponges Axinella cannabina and Suberites carnosus [12] and skin and Cruz-López et al (2018) extracted collagen from gulf corvina skin and swim bladder [10]. As reported in the literature, the marine collagen market is expected to reach USD 983.84 million by 2025, with a compound annual growth rate of 7.4% [13].…”

Changes in the Molecular Characteristics of Bovine and Marine Collagen in the Presence of Proteolytic Enzymes as a Stage Used in Scaffold Formation

“…It is known, for example, that scaffolds based on collagen and acrylates possess improved mechanical properties and cytocompatibility [20][21][22][23][24][25]. It should also be taken into account that collagen is a thermally unstable polymer; at temperatures above 30-40 • C, its denaturation with the formation of gelatin begins [26][27][28][29]. Comparative data on the properties of hybrid materials based on collagen and gelatin proves the perspective of their use in combination or replacement of collagen with gelatin in scaffold-based technologies [30][31][32].…”