Extraction Of Common Mammalian Source Collagen And Its Performance Characterization
Keywords
Collagen, Different Sources, Extraction, Biomaterials
Abstract
In order to evaluate the physical and chemical properties and biological properties of collagen from different mammalian sources, enzymatic extraction was used to extract collagen from common mammals such as pigs, rats and cattle, and the amino acid composition, physical and chemical properties and biocompatibility of the extracted collagen were analyzed. Make an evaluation. The results show that the amino acid composition and content of collagen from different sources are different; FT-IR spectrum shows that the three extracted collagens maintain their triple helix structure well; TG results show that the three types of collagen have relatively similar thermal behavior, among which pig Pig skin collagen (PS-col) has higher stability against thermal degradation; SEM photos show that rat tail collagen film (RT-col) has a slightly rough surface structure, while the surface of pig skin collagen film is relatively smooth. , the bovine tendon collagen membrane (BT-col) is moderate; AFM observed that the three types of collagen all present a collagen fiber bundle-like structure, but there are differences in the formation of collagen fibers from different sources of collagen; the mechanical property test shows that the bovine Achilles tendon collagen membrane Tendon collagen can better resist external forces and has good material flexibility. Pig skin collagen has the largest Young’s modulus and is less prone to deformation than the other two. The mechanical properties of rat tail collagen are between the two. In vitro cell experiment results show that all three collagens have good biocompatibility. Provide more reference for optimizing collagen-based biomaterials to meet different needs.
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Original research was done by Wu Minghui, Liu Yang, Liu Xia, Zhang Zhongxun, Mao Yuanze, Deng Linhong
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