Transglutaminase crosslinking promotes physical and oxidative stability of filled hydrogel particles based on biopolymer phase separation.

In the present study, the effect of transglutaminase (TGase) concentration on the physical and oxidative stabilities of filled hydrogel particles created by biopolymer phase separation was investigated. The results showed that filled hydrogels had relatively smaller particle sizes, higher absolute zeta-potentials, higher interfacial layer thicknesses and lightness values with the increasing of TGase concentration (P < 0.05), as evidenced by the apparent viscosity and viscoelasticity behavior. However, the relatively higher TGase concentration promoted the protein aggregation, which weakens the protection of the surface protein layer, having the negatively impacted the physical stability of filled hydrogels. Microstructural images which obtained via cryo-scanning electron microscopy also verified the above results. In particular, it is noted that filled hydrogels displayed the lowest degrees of lipid and protein oxidation during 10 days of storage (P < 0.05) at TGase concentration of 10 U/g. Prevention against oxidation was attributed mainly to TGase crosslinking of protein molecules on the surface of droplets, which likely provided a denser interface around lipid droplets. Our results indicated that TGase was a favourable agent to crosslink protein on the surface of lipid and improve the physical and oxidative stability of filled hydrogel particles.