Physicochemical properties of collagen extracted from quail feet (Coturnix Japonica)

In this study acid soluble collagen (ASC) from Quail Feet (Coturnix Japonica) was isolated and physicochemical properties of collagen were evaluated. In many countries, quails are reared for eggsand meat production. Obviously, quail feet are one of the major by-products of quail meat processing.Therefore, the purpose of this study was to investigate the possibility of increasing the use value of these by-products by isolation of collagen. Acid solubilized collagen (ASC) was extracted from thequail feet using acetic acid for 72 h, followed by precipitation with 0.9 M NaCl. ASC with the yield of4.55 % (wet weight basis) was obtained from quail feet. Its physicochemical properties, such as protein pattern, amino acid composition, denaturation temperature and FTIR spectra werecharacterized. ASC from quail feet sources contained glycine as the major amino acid. In addition,extracted collagen contained high amount of proline and hydroxyproline. Fourier transform infrared (FTIR) spectra revealed that, ASC was in triple helix. Therefore, the isolated collagen from quail feet could serve as an alternative source of collagen for further application in food, cosmetics and nutraceutical industries

کلیدواژه ها:

Quail feet (Coturnix japonica) ، Acid solubilized collagen (ASC) ، FTIR ، denaturation temperature (Td)