PURIFICATION AND BIOCHEMICAL PROPERTIES OF TYPE I COLLAGEN FROM QUAIL FEET (COTURNIX JAPONICA)

摘要

Lactic acid soluble collagen (LASC) from Japanese quail feet was isolated and comparatively characterized. The quails are reared in Malaysia for eggs and meat production. Quail feet are one of the major by-products of quail meat processing. The purpose of this study was to extract the collagen from this by-product and analysis of biochemical properties. LASC was extracted from the quail feet using lactic acid for 72 h and followed by precipitation with 0.9 M NaCI. Amino acid analysis indicated that the major amino acid was glycine and it contained arelatively higher content of proline and hydroxyproline, compared with marine based collagen. Hence, LASC had higher thermal stability than marine based collagen. Fourier transform infrared (FTIR) spectra revealed that, LASC was in the form of a triple helix. Therefore, the isolated collagen from quail feet can potentially be used as an alternative source of collagen in various applications.