Colágeno de tilápia: uma alternativa para agregar valor aos subprodutos da indústria de pescados

• Ano de defesa: 2019
• Autor(a) principal: Fontoura, Andrine Menna da
• Tipo de documento: Dissertação
• Tipo de acesso: Acesso aberto
• Idioma: por
• Instituição de defesa: Universidade Federal de Santa Maria; Brasil; Ciência e Tecnologia dos Alimentos; UFSM; Programa de Pós-Graduação em Ciência e Tecnologia dos Alimentos; Centro de Ciências Rurais
• Palavras-chave em Português: Colágeno; Pescado; FTIR; SDS-PAGE; Pepsina; Propriedades; Collagen; Fish; Pepsin; Properties; CNPQ::CIENCIAS AGRARIAS::CIENCIA E TECNOLOGIA DE ALIMENTOS
• Link de acesso: http://repositorio.ufsm.br/handle/1/16650

Tilapia processing residues can reach up to 70% of the raw material, due to the high protein content. Obtaining collagen is a promising alternative to add value to these wastes. The methods of obtaining collagen are based on chemical and / or enzymatic hydrolysis. In this context, the objective of this study was to obtain collagen from tilapia residues (carcass, carcass residue and skin) through chemical-enzymatic hydrolysis. The collagens obtained from the processing residues of the tilapia were extracted with pepsin and obtained a good yield (%) the triple helical structure was preserved, which can be confirmed by electrophoresis analysis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR). The collagens were mainly composed of type I collagen. As for functionality, the collagens showed high solubility in acid pH and low solubility at high pH, the emulsifying activity index was superior to conventional gelatins. Pretreatment with and without hydrogen peroxide showed no significant difference (p <0.05) in the centesimal composition and collagen functionality. The time of chemical-enzymatic extraction with pepsin had a positive effect on the yield of collagen without affecting its integrity. It can be concluded that the residues generated by the processing of the industry have proven to be a technologically viable source for the extraction of collagen and the collagens of these residues have shown to be promising as an alternative to the traditional collagens with great potential of industrial application.