Research on Proteolytic Cleavage of Bovine Type I Collagen

• Main Authors: Kai-Yueh Shin, 石凱元
• Other Authors: Shyh-Yu Shaw
• Format: Others
• Language: zh-TW
• Published: 2003
• Online Access: http://ndltd.ncl.edu.tw/handle/66009133533010115919

碩士 === 國立成功大學 === 化學系碩博士班 === 91 === Collagen is the most abundance biopolymer in connective tissue. Its special triple helical structure and biopolymer property has made it widely used in biopharmaceutical, tissue engineering, cosmetics and food industries. In this research, we used pepsin to cleave bovine type I collagen and studied pepsin-cleaved collagen fragments. Under low temperature condition (4℃), pepsin only cleaved off only a small fragment from collagen and yield a 93 kDa collagen fragment as determined by MALDI mass spectrometry. Under higher temperature condition (40℃), the collagen was cleaved into many small fragment. The cleavage of collagen by pepsin not only improves its water solubility but also improves its biological activity. The result of mouse osteoblast cell proliferation assay showed that pepsin-cleavage collagen is approximately two fold better than the uncleavaed collagen.