Properties of co-gel between Tenebrio Molitor larvae protein and myofibrillar protein induced by transglutaminase.

[Display omitted] • The co-gel properties between TMLP and MP were enhanced by TGase. • TGase changed the secondary and tertiary structures of co-gel. • TGase promoted the formation of more compact microstructures. • A 60 U/g TGase concentration was appropriate for improving the co-gel. This study explored the effect of adding transglutaminase (TGase) to a co-gel of Tenebrio Molitor larvae protein (TMLP) and myofibrillar protein (MP). Different concentrations of TGase (0–90 U/g) were added to the co-gel. The results showed that 60 U/g TGase treatment significantly improved the gel strength and water holding capacity (WHC) by 26.51 g and 9.2 %, respectively. TGase promoted the rheological properties and accelerated the three-dimensional network structure of the co-gel. Moreover, TGase significantly increased (P < 0.05) the tyrosine residues, tryptophan residues content and hydrophobic interactions of the aliphatic groups. The chemical forces between the protein molecules changed. TGase promoted the transition of α-helix to β-sheet and free water to immobilized water, thereby improving the WHC of co-gel. The principal component analysis reflected the links among indicators. This study illustrated that TGase might be an effective strategy to improve the co-gel of TMLP and MP and emulsified meat products with insects. [ABSTRACT FROM AUTHOR]