An alternative source of type I collagen based on by-product with higher thermal stability

• Published in: Food hydrocolloids 2017-02, Vol.63, p.372-382
• Main Authors: Yousefi, M., Ariffin, F., Huda, N.
• Format: Article
• Language: English
• Subjects: Acid soluble collagen (ASC); Pepsin soluble collagen (PSC); Quails' feet (Coturnix japonica); Thermal stability
• ISSN: 0268-005X; 1873-7137
• DOI: 10.1016/j.foodhyd.2016.09.029

Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were isolated from quails' feet and characterized. The electrophoretic patterns indicated that the collagens are composed of α1, α2, β and γ-chains, corresponding to the properties of collagen type I. One major characteristic of the obtained collagens is that they were found to have high thermal stability. The denaturation temperature (Td) and maximum transition temperature (Tmax) of ASC (39.6 and 110.7 °C) and PSC (38.33 and 109 °C) assessed using the differential scanning calorimetry and rheometer. These results could be attributed to the high imino acid content of ASC and PSC (248.72 and 224.17 residues/1000 residues) and degree of pro-hydroxylation (45.91% and 45.44%), respectively. Both ASC and PSC can assemble into collagen fibrils. The D-periodicities of fibrils assembled from PSC (70.6) were slightly smaller than those of fibrils assembled from ASC (72.9). Summarizing the experimental results suggested that the extracted collagens from quails’ feet with high thermal stability could be considered an alternative to mammalian-derived collagen in biomaterials, functional foods, pharmaceuticals and cosmetics. [Display omitted] •Acid and pepsin soluble collagens were isolated from quail feet.•The quail feet collagen can be considered as an alternative source of type I collagen.•ASC and PSC possess higher imino acid content than calf-skin and pig-skin collagens.•Both ASC and PSC exhibit higher thermal stability.•The collagen may find applications in functional foods and pharmaceuticals.