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Melting Behavior of Gels Prepared from Isolated Subunits of Collagen
Author(s) -
TAKAHASHI KOJI,
SHIRAI KUNIO,
WADA KEIZO
Publication year - 1988
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1988.tb07881.x
Subject(s) - differential scanning calorimetry , chemistry , ammonium sulfate , chromatography , thermal stability , cellulose , corium , peptide , ion exchange , ion chromatography , sulfate , ammonium , nuclear chemistry , ion , organic chemistry , biochemistry , heat transfer , thermodynamics , physics
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.