LAUSR

Transglutaminase (TGase) catalyzing crosslinking between intra- and inter-chain glutamine and lysine peptide residues has been used for modifying protein's structure. However, its enzymatic performance on albuminoids such as collagen was still not completely illustrated. Herein, we investigated the crosslinking efficiency of films preheated at different temperatures and estimated its physicochemical properties. The electrophoresis results showed that the extracted collagen had typical triple helix structure but reduced and even disappeared as temperature increased. Accordingly, X-ray diffraction (XRD) indicated that the amount of triple helices decreased, corresponding to the decreases in thermal stability and mechanical properties of films. TGase crosslinking decreased the thickness of all films, while mechanical properties and thermal stability had a significant improvement especially at 45 °C and 65 °C. With the proper equilibrium of denature temperature and TGase crosslinking, the tailored film-forming properties of collagen can offer a potential to engineer collagenic material for biodegradable and edible packaging applications.