Characterization of acylated pepsin-solubilized collagen with better surface activity.

A new kind of acylated collagen with water solubility and better surface activity was prepared via reaction of pepsin-solubilized calf skin collagen with lauroyl chloride and succinic anhydride in this paper. The equilibrium surface tension and the isoelectric point were 55.92 mN/m and 4.93 respectively, suggesting that acylated collagen had surface activity as well as water solubility. Meanwhile, the results of Fourier transform infrared spectroscopy analyses and electrophoresis patterns demonstrated that the triple helix conformation of collagen was not destroyed, but the subunits of acylated collagen shifted to higher molecular weight than those of native collagen. Scanning electron microscope and differential scanning calorimeter measurements revealed that lyophilized acylated collagen exhibited relatively well-distributed pore structure and its denaturation temperature was about 9.0 °C higher than that of native collagen. Additionally, the increase of the diameter of the fibrils was observed by atomic force microscopy. Acylated collagen with water solubility and better surface activity might broaden the application of collagen-based materials to cosmetics, drug delivery and pharmacotherapy.