Influence on the physicochemical properties of fish collagen gels using self-assembly and simultaneous cross-linking with the N-hydroxysuccinimide adipic acid derivative
Influence on the physicochemical properties of fish collagen gels using self-assembly and simultaneous cross-linking with the N-hydroxysuccinimide adipic acid derivative
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N-羟基琥珀酰亚胺己二酸衍生物自组装和同时交联对鱼胶原蛋白凝胶理化性质的影响
DOI：
10.3109/03008207.2015.1020941
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发表时间：
2015-02
影响因子：
2.9
通讯作者：
Guoying Li
中科院分区：
文献类型：
--
作者：
Lirui Shen;Zhenhua Tian;Wentao Liu;Guoying Li
摘要以南方鲇皮为原料，通过胶原分子自组装和N-羟基琥珀酰亚胺己二酸衍生物（NHS-AA）交联制备胶原凝胶。将NHS-AA的剂量转换为[NHS-AA]/[NH 2]比率（0.025-1.6，通过NHS-AA的[活性酯基]和胶原蛋白的赖氨酸和羟赖氨酸残基的[ε-NH 2]计算）。当比例< 0.05时，胶原分子通过自组装形成胶原凝胶，导致胶原凝胶的乳白色外观和部分胶原纤维的特征性D周期性，胶原凝胶（[NHS-AA]/[NH 2] = 0.05）显示出变性温度的小幅增加（Td，42.8 °C）、剩余重量（12.59%）、比水含量（SWC 233.7）和弹性模量（G′ 128.4 Pa）与未交联胶原凝胶（分别为39.1 °C，9.12%，222.4和85.4 Pa）进行比较。当比值> 0.05时，D周期消失，外观由乳白色逐渐变为透明，表明NHS-AA对胶原分子自组装的抑制作用更加明显。结果表明，[NHS-AA]/[NH 2] = 0.2的胶原凝胶具有最低的Td（35.8 °C）、剩余重量（7.96%）、SWC（130.9）和G′（31.9 Pa）。当配比为1.6时，胶原分子自组装受到明显抑制，胶原凝胶主要通过共价交联键形成，胶原凝胶外观透明，Td（47.0 °C）、剩余重量（45.92%）和G′（420.7 Pa）最大。这些结果表明，使用不同剂量的NHS-AA可以制备具有不同性质的胶原凝胶。
Abstract Collagen gels from Southern catfish (Silurus meridionalis Chen) skins were prepared via the self-assembly of collagen molecules and simultaneous cross-linking with the N-hydroxysuccinimide adipic acid derivative (NHS-AA). The doses of NHS-AA were converted to [NHS-AA]/[NH2] ratios (0.025–1.6, calculated by the [active ester group] of NHS-AA and [ε-NH2] of lysine and hydroxylysine residues of collagen). When the ratio < 0.05, collagen gels were formed by collagen molecule self-assembly, resulting in the opalescent appearance of collagen gels and the characteristic D-periodicity of partial collagen fibrils, the collagen gel ([NHS-AA]/[NH2] = 0.05) displayed a small increase in denaturation temperature (Td, 42.8 °C), remaining weight (12.59%), specific water content (SWC 233.7) and elastic modulus (G′ 128.4 Pa) compared with uncross-linked collagen gel (39.1 °C, 9.12%, 222.4 and 85.4 Pa, respectively). As the ratio > 0.05, disappearance of D-periodicity and a gradual change in appearance from opalescent to transparent suggested that the inhibition of NHS-AA in the self-assembly of collagen molecules was more obvious. As a result, the collagen gel ([NHS-AA]/[NH2] = 0.2) had the lowest Td (35.8 °C), remaining weight (7.96%), SWC (130.9) and G′ (31.9 Pa). When the ratio was 1.6, the collagen molecule self-assembly was markedly suppressed and the formation of collagen gel was predominantly via the covalent cross-linking bonds which led to the transparent appearance, and the maximum values of Td (47.0 °C), remaining weight (45.92%) and G′ (420.7 Pa) of collagen gel. These results indicated that collagen gels with different properties can be prepared using different NHS-AA doses.
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影响因子：
5.8
作者：
M. Gašperlin;L. Tušar;M. Tušar;J. Kristl;J. Šmid-Korbar
通讯作者：
M. Gašperlin;L. Tušar;M. Tušar;J. Kristl;J. Šmid-Korbar
影响因子：
2.8
作者：
Shunji Yunoki;Nobuhiro Nagai;Takeshi Suzuki;M. Munekata
通讯作者：
Shunji Yunoki;Nobuhiro Nagai;Takeshi Suzuki;M. Munekata
DOI：
10.1016/j.colsurfb.2011.10.002
发表时间：
2012-02
期刊：
Colloids and surfaces. B, Biointerfaces
影响因子：
--
作者：
R. Usha;K. J. Sreeram;A. Rajaram
通讯作者：
R. Usha;K. J. Sreeram;A. Rajaram
影响因子：
5.8
作者：
Dupont-Gillain, CC;Jacquemart, I;Rouxhet, PG
通讯作者：
Rouxhet, PG
影响因子：
6.1
作者：
Nomura, Y;Toki, S;Shirai, K
通讯作者：
Shirai, K