Improvement of the material property of shark type I collagen by composing with pig type I collagen |
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| Authors: | Nomura Y Toki S Ishii Y Shirai K |
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| Institution: | Applied Protein Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Tokyo 183-8509, Japan. ny318@cc.tuat.ac.jp |
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| Abstract: | Fibril reconstruction process, that is, the nucleation and growth of mixed type I collagen fibril of shark and pig, progressed faster than that of the individual collagen species of shark or pig. The reconstructed mixed collagen fibril had a greater resistance to return to the solution or to melt into gelatin in comparison with the counterpart consisting solely of shark collagen. The denaturation temperature of the mixed collagen gel was about 10 degrees C higher than that of shark, and about 5 degrees C lower than that of pig. By scanning electron microscopy, the diameter of mixed collagen fibril showed an intermediate range between shark and pig collagen fibril. The breaking strength of the mixed collagen gel was tougher than that of pig, but weaker than that of shark. Other physicochemical properties of the mixed type I collagen gel were observed to be at intermediate positions between those of shark and pig type I collagen gels. |
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