Abstract
The collagens (COL2, COL4, and COL5) were extracted from chrome-tanned leather shavings via three distinctive routes of acid method. The dechroming degree of COL2 extracted with the easiest operation was the highest (95.6% ± 1.2%) and the yield exceeded 90%; however, the total amount of acid was the most and the cost was the highest. In the second route, although the three-step dechroming process brought cumbersome operation, the dechroming degree and yield of COL4 were 90.5% ± 0.8% and 92.2% ± 0.6%, respectively, and the acid amount was less than that in the first route. For COL5, the dechroming degree and yield was the lowest; nevertheless, this route had the advantages of lowest cost and simpler operation. Electrophoretic patterns showed that all the collagens contained α1, α2, and β chains without low molecular weight components and were close to those of type I collagen. Compared with native collagen extracted from fresh calf skin, the regenerated collagens also maintained unique triple helix conformation determined via ultraviolet, infrared spectra and X-ray diffraction, confirmed by the similar values of AIII/A1455 and Δν. Additionally, the collagens existed in the form of fibrils with D-period pattern of ~ 67nm. Furthermore, the denaturation temperatures of COL2, COL4, and COL5 were 71.2, 79.1, and 85.4°C, respectively, which were relevant to the tighter arrangement of fibrils with the increased chromium content.
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