Physicochemical properties and film-forming ability of fish skin collagen extracted from different freshwater species

Amino acid profile of collagen fractions extracted from by-products ofOphistonema libertateandScomber japonicus

“…Tamilmozhi, Veeruraj, and Arumugam (2013) reported 4.3% higher values of Hyp (of the total AAs) for PSC in sail fish skin than M-PSC. As previously stated, the AA profile as well as the physical and chemical properties of collagen could depend on factors such as species and their living environment (Tang et al, 2015). In addition, the results of this study also suggest that pepsin-soluble collagen from small pelagic species such as pacific thread herring and chub mackerel are rich in non-essential AAs.…”

“…High concentrations of collagen have been detected in scales and bones of marine and freshwater fish (Nagai, Araki, & Susuki, 2002;Nagai, Izumi, & Ishii, 2004;Tang et al, 2015;Veeruraj, Arumugam, Ajithkumar, & Balasubramanian, 2015;Zhou et al, 2015). The collagen has been used by the food, medical, cosmetic, and inclusively clothing industries (Alfaro, Balbinot, Weber, Tonial, & Machado-Lunkes, 2015;Regenstein & Zhou, 2007;Zhou et al, 2015).…”

Physicochemical characteristics and fibril-forming properties of collagen from paddlefish (Polyodon spathula) and globefish (Fugu flavidus) skin byproducts

“…This result was in accordance with previous reports for collagen from bester sturgeon skin (Zhang et al, 2014b), suggesting that ions might bind to the regions with excess charge density and accelerate protein monomers register longitudinally to form fibrils. However, the fibril-forming rate and degree of collagen from salmon skin and jellyfish were suppressed by the addition of NaCl (Yunoki et al, 2004;Hoyer et al, 2014), indicating fibrillogenesis is highly sensitive to collagen sources, the experimental conditions and the disparity in structural information which encoded in primary sequences (Tang et al, 2015).…”

“…Fibrillar rearrangement of collagens is the foundation behind the mechanical properties of almost all load-bearing tissues (Exposito et al, 2010). Due to the high fibril-forming ability, biocompatibility and low immunogenicity, collagens have been considered as excellent natural biopolymers which are developed as sausage casings or packaging films of meat products in food industry, and tissue scaffolds or wound dressings in pharmaceutical fields (Cozza et al, 2016;Tang et al, 2015). Traditionally, industrial production of collagens is mainly from terrestrial animals such as bovine, porcine skins and tendons.…”

Optimización de la Extracción del Colágeno Soluble en Ácido de Subproductos de Tilapia Roja (Oreochromis spp) mediante un Diseño de Superficie de Respuesta

“…1 ml de la solución se mezcló con una relación igual de sulfato cúprico 0.01N, hidróxido de sodio 2,5 M, peróxido de hidrogeno al 6% y 0,1 ml de sulfto ferroso 0.05 M. luego de agitar vigorosamente la muestra hasta que desaparecieran las burbujas de gas, se adiciono 4,0 ml de ácido sulfúrico 3N y 2 ml de la solución de p-dimetilaminobenzaldehido al 5%. Se calentó durante 16 min a 70 ºC con un posterior choque térmico en un baño de hielo, se midio la absorbancia en un espectrofotómetros UV/VIS Genesys 10s marca Thermo a 540nm (Tang et al, 2015). La curva de calibración se realizó usando seis soluciones estándar de trans-4-Hydroxy-L-proline ≥99% marca Sigma.…”