Physicochemical Properties of Succinylated Calfskin Pepsin-Solubilized Collagen

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  • ZHANG Zhongkai
    The Key Laboratory of Leather Chemistry and Engineering of the Ministry of Education, Sichuan University
  • LIU Wentao
    The Key Laboratory of Leather Chemistry and Engineering of the Ministry of Education, Sichuan University
  • LI Dong
    The Key Laboratory of Leather Chemistry and Engineering of the Ministry of Education, Sichuan University
  • LI Guoying
    The Key Laboratory of Leather Chemistry and Engineering of the Ministry of Education, Sichuan University

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Some physicochemical properties of calfskin pepsin-solubilized collagen (PSC) and succinylated PSC (SPSC) were compared. The amino acid profile remained significantly unchanged. Sodium dodecylsulphate-polyacrylamide gel electrophoresis showed that subunits of SPSC migrated less than those of PSC. The denaturation temperatures of PSC and SPSC were 38.4 °C and 34.7 °C respectively. Succinylation slightly altered the triple-helical conformation of collagen, as determined by circular dichroism.

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