Abstract
Gelatin extraction process from Kumakuma (Brachyplathystoma filamentosum) skin was optimized using a calcium hydroxide solution. The gelatin obtained was characterized through scanning electron microscopy and analyses of yield, gel strength, color, viscosity, amino acid profile, melting point, foaming capacity, and emulsifying capacity. The optimized conditions were defined over ten days of pre-treatment at 50°C. This condition resulted in desirability of 0.965 and yield and gel strength values of 20.24% and 221 g, respectively. Glycine was the main amino acid both in the fish skin (11.68%) and in the gelatin obtained (23.39%). Gelatin had extendable and consistent gel characteristics and its microstructure showed even threads with small gaps throughout, which is favorable for the food industry. Key words: Residue, fish, pre-treatment, gelatin, gel strength.
Highlights
Gelatin is a valuable protein derived from animal byproducts obtained through partial hydrolysis of collagen originated from cartilages, bones, tendons and skins of cold-water, and warm-water fish (Sakr, 1997)
No study has been carried out with the Amazon species Kumakuma (Brachyplathystoma filamentosum), a large-size fish that can reach over 1.5 m in the overall length and weigh 100 kg, which is widely used in the filleting industry (Gonçalves et al, 2003)
The results indicate that variations in viscosity may be related to the different freshwater fish species and to the extraction method
Summary
Gelatin is a valuable protein derived from animal byproducts obtained through partial hydrolysis of collagen originated from cartilages, bones, tendons and skins of cold-water (cod, king weakfish, salmon, among others), and warm-water fish (tuna, catfish, tilapia, among others) (Sakr, 1997). Depending on the method employed in the pre-treatment, two types of gelatin with different characteristics can be produced. Type-A gelatin (isoelectric point at pH 6 to 9) is produced by acid treatment of the collagen, while type-B gelatin Point at pH 5) is produced by alkaline treatment (Stainsby, 1987). Gelatin is a protein derived from the partial hydrolysis of collagen and is made up of approximately 19 amino acids (Osborne et al, 1990). Collagen’s thermal stability is related to its imino acid content (proline and hydroxyproline). The higher this content, the greater the stability of the bonds among proteins. The controlled cooling of collagen (below its melting point) causes the recovery of the helicoidal structure (Wong, 1994)
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