Casein-hempseed protein complex via cross-link catalyzed by transglutaminase for improving structural, rheological, emulsifying and gelation properties

In present study, microbial transglutaminase (MTGase) was applied to strengthen the interaction between casein and hempseed protein (HPI) through crosslinking. The structural and functional characteristics of this heteropolymers were investigated. Both homologous and heterologous crosslinking were achieved by adding MTGase in casein-HPI system, and thus enhanced zeta potential, surface hydrophobicity, viscosity, emulsifying and gelation properties of the complex. However, HPI hindered the crosslinking due to unbalanced Lys/Gln ratios. Emulsifying and gelling properties were significantly correlated with the secondary structures. When MTGase activity was < 30 U/g or treatment time was < 2 h, the α-helix content decreased by 9% while the β-sheet content increased by 12%, respectively, with MTGase activity and treatment time increase. The structural alterations resulted in the better emulsifying activity, gel networks and water holding capacity of the complex. This work represents a novel interaction mode between casein and HPI via MTGase to elevate functional properties of complex.