Melting Behavior of Gels Prepared from Isolated Subunits of Collagen

Acid‐soluble collagen (ASC) was prepared from fresh pigskin corium, and denatured under mild conditions to obtain a mixture of parent gelatins. The mixture was precipitated with ammonium sulfate and preliminarily fractionated into four fractions by step‐wise redissolution in ammonium sulfate solutions of decreasing concentration. From these fractions, substantially pure α1, α2, β 11 , and β 12 peptide chains could be obtained by CM‐cellulose ion‐exchange chromatography. Differential scanning calorimetry (DSC) of the melting process of these peptide gels demonstrated that the thermal stability of α2‐gel was very much lower than that of α1‐gel.