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J Sci Food Agric ; 96(11): 3795-800, 2016 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-26676993

RESUMEN

BACKGROUND: Fish skin has become a new source of collagen. It is usually extracted at low temperature. Increasing the extraction temperature can increase the collagen yield. However, high temperature might cause degradation of the triple helical structure of collagen, which is related to its functional biomaterial. This work thus aimed to investigate the effect of extraction temperature on the extraction efficiency and characteristics of acid-soluble collagen (ASC), particularly its triple helical structure. RESULTS: ASC was extracted at 5 ± 1, 15 ± 1 and 25 ± 1 °C for 0-24 h with 0.3 or 0.5 mol L(-1) acetic acid. The results showed that extraction with 0.5 mol L(-1) acetic acid gave a higher extraction efficiency than that in 0.3 mol L(-1) acetic acid (P < 0.5). Extraction at 25 ± 1 °C for 5 h with 0.5 mol L(-1) acetic acid gave a higher extraction efficiency (73.73 ± 1.28%), which is higher than that of 5 ± 1 °C by about 1.7-fold. All ASC obtained were identified as type I collagen and showed similar physicochemical properties. CONCLUSION: The results showed that extraction temperature strongly affected extraction efficiency. Extraction at 25 °C did not affect the triple helical structure, which was confirmed by the results of Fourier transform infrared, circular dichroism spectrum and collagen self-assembly. © 2015 Society of Chemical Industry.


Asunto(s)
Cíclidos , Colágeno Tipo I/química , Proteínas de Peces/química , Residuos Industriales/análisis , Piel/química , Ácido Acético/química , Animales , Dicroismo Circular , Frío , Colágeno Tipo I/economía , Colágeno Tipo I/aislamiento & purificación , Electroforesis en Gel de Poliacrilamida , Proteínas de Peces/economía , Proteínas de Peces/aislamiento & purificación , Industria de Procesamiento de Alimentos/economía , Hidroxiprolina/análisis , Indicadores y Reactivos/química , Residuos Industriales/economía , Cinética , Microscopía Electrónica de Rastreo , Desnaturalización Proteica , Pliegue de Proteína , Estabilidad Proteica , Estructura Secundaria de Proteína , Solubilidad , Espectroscopía Infrarroja por Transformada de Fourier , Tailandia
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