DSC investigation of bovine hide collagen at varying degrees of crosslinking and humidities.
DSC investigation of bovine hide collagen at varying degrees of crosslinking and humidities.
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DOI：
10.1016/j.ijbiomac.2017.04.124
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发表时间：
2017-10
影响因子：
8.2
通讯作者：
Michaela Schroepfer;M. Meyer
中科院分区：
文献类型：
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作者：
Michaela Schroepfer;M. Meyer
采用差示扫描量热法（DSC）对不同水化程度下的牛皮胶原蛋白（non - clc; non-CrossLinkedCollagen）进行了分析，并与与戊二醛（CLC-GA）和铬（III）离子（CLC-Cr）交联的牛皮胶原蛋白样品进行了比较。交联和干燥可以提高变性温度。划分了不同的区域，反映了水对变性温度影响的变化。此外，在中等水化程度下，与完全水化状态相比，非交联胶原的焓增加。这反映了25%水合作用范围内水的胶状作用。即使在非常低的交联水平下，牛皮胶原的交联也会使完全水合状态下的焓降低25%。这可以通过交联剂对胶原分子水合网络的强烈影响来解释，假设焓主要是氢键的结果。在极低含水量时，CLC-Cr的DSC峰完全消失。这可以解释为氢硫代铬酸盐（III）配合物和胶原之间对水的竞争。
Bovine hide collagen (nonCLC; non-CrossLinkedCollagen) was analysed by differential scanning calorimetry (DSC) at different hydration degrees and compared with hide collagen samples crosslinked with glutaraldehyde (CLC-GA) and chromium(III) ions (CLC-Cr), respectively. Crosslinking and drying were confirmed to increase the denaturation temperature. Different regions were assigned, that reflect the variation of the influence of water on the denaturation temperature. Furthermore, at moderate hydration degrees, the enthalpies of non-crosslinked collagen increase compared to the fully hydrated state. This reflects a glue-like action of water in the range of 25% hydration. Crosslinking of bovine hide collagen decreases the enthalpy by 25% in the fully hydrated state, even at very low levels of crosslinking This can be explained by intensive effects of the crosslinking agent on the hydration network of the collagen molecules, assuming that the enthalpies are principally a result of hydrogen bonding. At very low water contents DSC peaks of CLC-Cr completely disappear. This could be explained by competition between hydroxosulfochromate(III) complexes and collagen for water.