現代醫材的研究與製程中已經有過許多以生物材料作為主要成份的嘗試與探討，而膠原蛋白也是其中之一，它可以由生物組織萃取而得，並且具有高吸水能力(high water absorption capacity)、生物相容性(biocompatibility)、生物降解性(bio-degradability)以及低免疫原性(low immunogenicity)等優點，也有機械強度低與熱穩定性差之缺點，此次研究以魚鱗膠原蛋白作為反應起始物，藉由最佳交聯反應條件，優化海洋膠原蛋白性質。實驗過程可分為三個部分，第一部分為較台灣鯛魚鱗膠原蛋白與鯉魚魚鱗膠原蛋白之性質，並根據兩種膠原蛋白以交聯作用所製作出的薄膜性質差異，選擇出最佳的交聯反應起始物；第二部分為探討交聯反應的官能基作用與分子間立體障礙，再以實驗結果找出最佳的交聯反應順序；第三部分則是根據前兩部分的實驗結果，選定反應起始物的魚鱗膠原蛋白種類、交聯反應順序，並進行反應藥劑的比例探討，最終得出交聯反應的最佳條件。此次研究的最佳反應起始物為台灣鯛魚鱗膠原蛋白，最佳交聯順序為膠原蛋白-核醣-殼聚醣，最佳反應時間為24小時，最佳藥劑比例為0.6 g台灣鯛魚鱗膠原蛋白+2 mL的0.1%核醣+2 mL的1%殼聚醣，上述最佳反應條件所製成的薄膜膨潤比為4.42、熱變性溫度為94.57 ˚С，薄膜的表面結構光滑且孔洞少，以紅外光譜(FT-IR)分析數據可見大約於1600~1650 cm-1的膠原蛋白C=O官能基訊號位置向波數小的方向偏移的幅度較大、訊號強度削弱的幅度也較大，並且特徵峰保有雙峰的峰型，此表示交聯反應中成功與膠原蛋白的C=O官能基產生之氫鍵數目較多，並且產物分子間的排列較規則，因此薄膜交聯程度較高，且表面結構光滑、少孔洞。我們在研究的過程中也探討了兩種交聯劑與膠原蛋白反應的順序對於產物性質的影響，當膠原蛋白與殼聚醣兩種巨型分子相互靠近接合時，會有立體位向的考量，並導致氫鍵鍵結數目較少與產物分子間排列較不規則，若加以分子體積較小的核醣參與反應，且以加料次序控制交聯反應的順序，能有效改善巨型分子交聯問題，並製成交聯程度較高的薄膜。

The experiment process can be divided into three parts.
The first part is to analyze and compare the difference in protein properties between tilapia scale collagen and Carp scale collagen, and the two kinds of collagens are used to make collagen films respectively. According to the experimental results, the best fish scale collagen was selected as the starting material for the cross-linking film forming experiment. The second part is to discuss the mechanism of the cross-linking reaction, and to know the best cross-linking sequence based on experimental data. The third part discusses the ratio of reactants on the basis of the experimental results of the first two parts. After experiments, we found that the best reaction conditions were 0.6 g of tilapia scale collagen, followed by 0.1% ribose and 1% chitosan, reacted at room temperature for 24 hours, and finally the film was formed by freeze-drying technology. The film made under the best reaction conditions has a swelling ratio of 4.42 and a thermal denaturation temperature of 94.57 ˚С. The surface structure of the film is smooth and there are few holes. Analyze the film by FT-IR spectroscopy, it was found that the C=O group signal of collagen at about 1600~1650 cm-1 shifted to a small wavenumber direction, the signal intensity was weakened, and the signal was bimodal. These mean that there were more hydrogen bonds successfully generated with the C=O functional group of collagen in the cross-linking reaction and the arrangement of the molecules was more regular, so the degree of cross-linking of the film was higher, and the surface structure was smooth and there were few holes.We have explored the reaction sequence of the two cross-linking agents and collagen. When the two giant molecules of collagen and chitosan are close to each other, there will be steric obstacles, which will lead to less hydrogen bond generation and less regularity. If smaller molecule of ribose is added to react and the sequence of the cross-linking reaction is controlled, the problem of cross-linking of giant molecules can be effectively improved, and a film with a higher degree of cross-linking can be made.

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