Effect Of Cross-Linking On Dynamic Rheological Properties And Thermal Stability Of Collagen Solutions
Keywords
Collagen, N-Hydroxysuccinimide Reactive Adipate, Cross-Linking, Rheological Properties, Thermal Stability
Abstract
Abstract: In order to improve the viscoelastic properties and thermal stability of collagen solution, as well as improve the ability of collagen to resist enzymatic hydrolysis, this article uses a new cross-linking agent, N-hydroxysuccinimide adipate (NHS-AA) , cross-linking modification of collagen solution. The dynamic rheometer measurement results show that at f=0.02 Hz and 25¡ãC, the elastic modulus (G’), viscous modulus (G”) and complex viscosity (¦Ç*) of the collagen solution are respectively higher than those before cross-linking. of 0.03 Pa, 0.11 Pa and 0.76 Pa.s increased to 22.83 Pa, 3.36 Pa and 143.90 Pa.s. Differential scanning calorimetry (DSC) measurement results showed that the thermal denaturation temperature of the cross-linked collagen solution reached 42.5¡ãC, which was 2.1¡ãC higher than that of the uncross-linked collagen solution (40.4¡ãC). For sponges made from cross-linked collagen solutions, electrophoresis (SDS-PAGE) studies have shown that the ability of collagen sponges to resist enzymatic degradation is significantly enhanced.
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Original research was done by Chen Yihui
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