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Properties of alkali-solubilized collagen solution crosslinked by N-hydroxysuccinimide activated adipic acid

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Abstract

The effect of N-hydroxysuccinimide activated adipic acid (NHS-AA) on the properties of alkali-solubilized collagen solutions was examined. The residual amino group content in crosslinked collagen, determined by trinitrobenzensulfonic acid (TNBS) assay, was decreased with increasing NHS-AA concentration. The results from differential scanning calorimeter (DSC) indicated that the maximum denaturation temperature (T d) of crosslinked collagen solution was about 4.2°C higher than that of un-crosslinked collagen solution (36.6°C). Moreover, the values of storage modulus (G′), loss modulus (G″) and complex viscosity (η*), obtained by means of dynamic frequency sweeps, were increased as NHS-AA concentration added up to 1.5 mM, and then decreased slightly when further increased NHS-AA concentration. Besides, for collagen solution crosslinked with 1.5 mM NHS-AA, dynamic denaturation temperature (T dd) was about 1.1°C lower than T d (40.8°C), and the Arrhenius-type time-temperature superposition (TTS) principle was applied to yield the activation energy to be 474.4 kJmol−1.

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Authors and Affiliations

  1. National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu, 610065, PR China

    Yihui Chen, Min Zhang, Wentao Liu & Guoying Li

  2. College of Chemistry and Chemical Engineering, Chongqing University of Science and Technology, Chongqing, 401331, PR China

    Yihui Chen

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  1. Yihui Chen
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  2. Min Zhang
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  3. Wentao Liu
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  4. Guoying Li
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Correspondence to Guoying Li.

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Chen, Y., Zhang, M., Liu, W. et al. Properties of alkali-solubilized collagen solution crosslinked by N-hydroxysuccinimide activated adipic acid. Korea-Aust. Rheol. J. 23, 41–48 (2011). https://doi.org/10.1007/s13367-011-0006-6

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  • DOI: https://doi.org/10.1007/s13367-011-0006-6

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