Physicochemical Properties of Collagen Isolated from Calf Limed Splits

Abstract

Samples of collagen extracted from calf limed splits by three different methods (acetic acid, pepsin, and alkali treatments) were characterized with respect to their thermal stability, subunit composition, and morphology of fibril network. Differential scanning calorimetry showed that the denaturation temperature of pepsin-treated collagen was very similar to that of commercial type I collagen but much higher than those of acetic acid-treated collagen and alkali-treated collagen. Analysis by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and Western blotting revealed that the subunit composition in collagen solution samples appeared to be major type I collagen and minor type III collagen. Scanning electron microscopy showed that acetic acid-treated collagen had a porous fibrillar network structure, while pepsin-treated collagen and alkali-treated collagen had membranous networks resembling that of commercial type I collagen.