Influence on the physicochemical properties of fish collagen gels using self-assembly and simultaneous cross-linking with the N-hydroxysuccinimide adipic acid derivative.

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.