Effect of fish collagen modification on its thermal and rheological properties

Abstract This report describes the effects of different methods of silver carp collagen crosslinking on its properties, particularly their thermal, mechanical viscoelastic and biological behavior. Enzymatic analyses and determination of the degree of crosslinking showed the stabilizing effect of both dehydrothermal (DHT) and 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC)/N-hydroxysuccinimide (NHS) treatments on fish collagen. The results of the thermal (DSC) measurements demonstrated that collagen crosslinked by EDC/NHS ensured a high thermal stability compared with collagen crosslinked dehydrothermally. The denaturation temperature ( T d ) of unmodified collagen samples increased from 77 to 80 °C and 88 °C for DHT- and EDC/NHS-treated collagen, respectively. The influence of DHT or EDC/NHS crosslinking on the viscoelastic behavior of fish collagen was elaborated by a shift of the tan δ max peak toward higher temperatures resulting in higher thermostability of the modified collagen samples.