The rheological and structural properties of fish collagen cross-linked by N-hydroxysuccinimide activated adipic acid

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• 作者：Min Zhang^a ; ^b ; Jiheng Li^a ; Cuicui Ding^a ; Wentao Liu^a ; Guoying Li^a ; ^{liguoyings@163.com}
• 关键词：Fish skin ; Collagen ; Cross-link ; Rheological properties ; Network
• 刊名：Food Hydrocolloids
• 出版年：2013
• 出版时间：March, 2013
• 年：2013
• 卷：30
• 期：2
• 页码：504-511
• 全文大小：890 K

文摘

Fish skin collagen, with a concentration (6?mg/ml) higher than its critical aggregation concentration (¡«0.5?mg/ml), was cross-linked using N-hydroxysuccinimide activated adipic acid (NHS-AA). Dynamic rheological measurement indicated that the storage modulus, loss modulus, complex viscosity and dynamic denaturation temperature increased while the loss tangent decreased with increasing the?degree of cross-linking (DC). In addition, collagens with different DC exhibited a significant difference in their activation energies. It was found that collagens with DC in three intervals (DC?<?¡«25 % , ¡«25 % ?<?DC?<?¡«50 % and DC?>?¡«50 % , respectively) possessed remarkably different rheological behaviors each other. That is, collagens with DC?<?¡«25 % exhibited a liquid-like behavior, while collagens with DC?>?¡«25 % tended to exhibit a solid-like behavior, and especially a sudden loss of flow was observed for collagen with DC?>?¡«50 % . Similar trends were observed from the features in differential scanning calorimetry (DSC) thermograms of collagen. That is, denaturation temperature (T_d) was slightly increased and the endothermic peak became broader as DC?<?¡«25 % , T_d was increased gradually as DC was further increased, while a sudden increase in T_d was observed and the endothermic peak became sharp for collagen with DC?>?¡«50 % . The three-step changes in the rheological behaviors and DSC thermograms of collagens might be due to the unique aggregation behavior of collagen in solution.