Abstract
Because many suitable properties, collagen type I is used in medical and cosmetical applications, for this, the collagen extraction from biological tissues as the first source for obtaining this protein is important. We used skin and tail tendon from bovine, and rat tail tendon to obtain collagen type I. Acetic acid was employed to dissolve the collagen from biological tissues, once obtained was characterized using Sodium Dodecyl Sulfate Polyacrilamide Gel Electrophoresis (SDS-PAGE) technique, DSC and SEM. It was found that indeed the collagen type I was obtained. The thermal analysis showed that the denaturation temperature (Td) was 70 °C for all cases and that the folding of the protein at this temperature is irreversible, involving in all cases two steps: an unfolding of the native protein (N) and an irreversible alteration of the unfolded protein (U) to yield a final state (F) that is unable to fold back to the native state. The protein morphology was studied using SEM, it was found that morphology protein is fibrillar. The results suggested that the obtaining process is very efficient because the collagen concentration obtained was very high.
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