交聯反應修飾豬的第一型膠原蛋白之定性測試

Characterization of cross-linking modified porcine type I collagen

蔡至恭(Jhih-Gong Tsai)

指導教授 ： 黃志宏 ； 孫熙文

國立臺北科技大學/工程學院/生物科技研究所/碩士(2008年)

https://doi.org/10.6841/NTUT.2008.00407

摘要

隨著使用方式的不同或選用不同的物種，萃取出來的膠原蛋白的物理
、化學與生物性質都有可能因此產生變化。因此，不同方式取得的膠原蛋白材料需要進行各種性質測試，避免性質變化產生不可預期的影響。因為材料本身分子彼此聯繫不足，分別使用紫外光照射與添加綠槴子素的交聯方法，強化分子的四級結構。經過測試後，估計由豬皮萃取得到的第一型膠原蛋白經過交聯後結構與機械強度的變化。結果顯示以物理的方法交聯後材料的機械強度提昇，以化學的方法交聯則增加對酵素的抵抗能力。這些結果能夠作為在未來使用膠原蛋白材料並應用時的參考。

關鍵字

膠原蛋白 ； 交聯

並列摘要

The chemical, physical and biological properties of the collagen materials may vary depending on the preparative processes and source of species. Thus, the characteristics of a collagen material must be thoroughly examined, as the changes in its intrinsic properties could lead to an unexpected functional consequence. In order to overcome this fundamental structural weakness, I employed UV and Genipin cross-linking methodologies to alter the quaternary structure of porcine type I collagen. In this thesis, I report a comprehensive assessment on the structural integrity and mechanical strength performance of the cross-linking modified porcine type I collagen extracted from porcine hides. My results demonstrate that physical cross-linking improves the mechanical strength while chemical cross-linking improves the resistivity of enzymatic degradation of the modified collagen. These findings undoubtedly provide useful information on the application of collagen-based products.

並列關鍵字

collagen ； cross-linking

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