Comparative study on acid‐soluble and pepsin‐soluble collagens from skin and swim bladder of grass carp (Ctenopharyngodon idella)

Abstract

Collagens were successfully extracted from the skin and swim bladder of grass carp. These fish by-products could serve as an alternative source of collagens for a wide variety of applications in the food and nutraceutical industries.

Acid and enzymatic extraction of collagen from Atlantic cod (Gadus Morhua) swim bladders envisaging health-related applications

“…Figure 1 displays the illustrative results, with the profiles of the several collagen extracts exhibiting the characteristic bands of type I collagen which is considered the gold standard in biomedical industries and tissue engineering approaches. The SDS-PAGE bands profiles of the swim bladder collagens (ASCsb and PSCsb) were quite similar to the equivalent collagens obtained from the skin of the same fish, as shown in Figure 1, demonstrating the feasibility of using swim bladders for the isolation of collagen, as reported for other fish species [12,22,23]. Moreover, the similarity of those profiles with the one exhibited by type I collagen obtained from bovine skin, namely the presence of two distinct a-chains (a1 and a2), with molecular weight of about 150 kDa, with a1 much more intense than a2 (theoretically, the double), as well as dimers -b chainat about 250 kDa, is compatible with a classification of swim bladder collagens as type I [6,13].…”

“…Kaewdang et al (2014) reported that ASC and PSC (acid soluble collagen and pepsin soluble collagen) from yellowfin tuna swim bladders were extracted with a yield of 1.07% and 12.10%, respectively. The differences in yields can be attributed to the different collagen structures in marine fish and the varying crosslinking of collagen fibrils in different by-products [12].…”

“…Nevertheless, based on the electrophoretic patterns of collagens extracted from cod swim bladders, there are differences between ASCsb and PSCsb, suggesting that the crosslinks of collagens were more abundant in ASCsb than in PSCsb. It may be due that some b and c (trimer) components were cleaved after digestion with pepsin [12].…”

“…Collagen is the main protein of connective tissue and the most abundant in vertebrate and invertebrate organisms [6,[10][11][12]. It represents about 30% of total proteins, having a fundamentally structural role in connective tissue as skins, tendons, ligaments and bones, being the most prevalent component of the extracellular matrix (ECM) [13].…”

“…Collagens of marine origin have gained more attention and importance because of their high extraction yield and availability, no risk of pathogen infection compared to land-based animals (cows, pigs, poultry, etc.) collagen, minor regulatory and ethical issues and no religious barriers [12,14,15]. Marine collagen from fish, sponges and jellyfish is increasingly used in various biomedical, cosmetics and pharmaceuticals applications [6,16,17].…”