Partial Characterization of Fish Skin Collagen Cross-Linked by N-Hydroxysuccinimide Activated Adipic Acid |
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| Authors: | Min Zhang |
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| Institution: | 1. The Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University , Chengdu , 610065 , PR China;2. College of Materials Engineering, Fujian Agriculture and Forestry University , Fuzhou , 350002 , PR China |
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| Abstract: | Fish skin collagen solutions (0.3%, w/v) were treated using N-hydroxysuccinimide activated adipic acid (NHS-AA) as a cross-linking agent. Partial important physicochemical properties such as the molecular weight, the morphologies, the interaction between molecules, and especially the thermal stability of the cross-linked collagens were examined by various methods. Results from sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) indicated the formation of cross-links, and thus the molecular weight of collagen was increased. Atomic force microscopy (AFM) suggested that the fiber diameter of cross-linked collagens was larger than that of collagen control. Scanning electron microscopy (SEM) showed that the number of pores from collagen sponges was reduced, accompanied by the rise in their pore sizes. According to Fourier transform infrared spectroscopy (FTIR) spectra, the value of amide III/amide I increased as a small amount of NHS-AA was used. Then it decreased and remained at a relatively constant level as NHS-AA was further added, which might indicate the altered interaction between collagen molecules due to cross-linking. Most important is the improved thermal stability of the cross-linked collagens as determined by differential scanning calorimetry (DSC). The reason for this improvement was further exposed by two-dimensional (2D) FTIR with temperature as perturbation. |
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| Keywords: | fish skin collagen cross-linking agent characterization two-dimensional Fourier transform infrared spectroscopy (2D-FTIR) |
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