Cross-linking and film-forming properties of transglutaminase-modified collagen fibers tailored by denaturation temperature
Cross-linking and film-forming properties of transglutaminase-modified collagen fibers tailored by denaturation temperature
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通过变性温度调节转谷氨酰胺酶修饰的胶原纤维的交联和成膜特性
DOI：
10.1016/j.foodchem.2018.07.223
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发表时间：
2019-01-15
期刊：
影响因子：
8.8
通讯作者：
Wu, Zinan
中科院分区：
文献类型：
--
作者：
Cheng, Shan;Wang, Wenhang;Wu, Zinan
谷氨酰胺转氨酶（TGase）催化链内和链间谷氨酰胺和赖氨酸肽残基之间的交联已被用于修饰蛋白质的结构。然而，其对类蛋白如胶原蛋白的酶促性能仍未完全阐明。在此，我们研究了在不同温度下预热的膜的交联效率，并估计其物理化学性质。电泳结果表明，提取的胶原蛋白具有典型的三股螺旋结构，但随着温度的升高，其含量减少甚至消失。因此，X射线衍射（XRD）表明，三重螺旋的量减少，对应于薄膜的热稳定性和机械性能的下降。TGase交联降低了所有膜的厚度，而机械性能和热稳定性有显著的改善，特别是在45 ℃和65 ℃下。在变性温度和TGase交联的适当平衡下，胶原蛋白的定制成膜特性可以为生物可降解和可食用包装应用提供工程胶原材料的潜力。
Transglutaminase (TGase) catalyzing crosslinking between intra- and inter-chain glutamine and lysine peptide residues has been used for modifying protein's structure. However, its enzymatic performance on albuminoids such as collagen was still not completely illustrated. Herein, we investigated the crosslinking efficiency of films preheated at different temperatures and estimated its physicochemical properties. The electrophoresis results showed that the extracted collagen had typical triple helix structure but reduced and even disappeared as temperature increased. Accordingly, X-ray diffraction (XRD) indicated that the amount of triple helices decreased, corresponding to the decreases in thermal stability and mechanical properties of films. TGase cross linking decreased the thickness of all films, while mechanical properties and thermal stability had a significant improvement especially at 45 degrees C and 65 degrees C. With the proper equilibrium of denature temperature and TGase crosslinking, the tailored film-forming properties of collagen can offer a potential to engineer collagenic material for biodegradable and edible packaging applications.