Collaborative stabilizing effect of trehalose and myofibrillar protein on high internal phase emulsions: Improved freeze-thaw stability and 3D printability

Food Chem. 2024 Dec 19:469:142564. doi: 10.1016/j.foodchem.2024.142564. Online ahead of print.

Abstract

This study investigated the improvement of adding trehalose (Tre) on freeze-thaw (F-T) stability and 3D printability of myofibrillar protein (MP)-based high internal phase emulsions (HIPEs), also the underlying mechanism. Appropriate Tre addition formed thicker shell-like structure around MP by hydrogen bonds, and induced protein unfolding to ameliorate amphiphilicity. Additionally, Tre promoted the MP diffusion to interface to reduce interfacial tension. After interface saturation, Tre inducing MP rearrangement contributed more to form compact interface layer. Larger interface coverage increased hydrophobic interactions between droplets, constructing stronger MP-Tre-HIPEs gel network, inhibiting more free water to form ice crystals, confirmed by reduced destabilization index and freezing point. Such gel network enhanced their own viscoelasticity and thixotropic recovery, exhibiting superior printing accuracy. Conversely, excessive Tre aggregates (15 %-20 %) competed with MP for interfacial adsorption and filled between interfacial layer of adjacent droplets, weakening gel network. These findings expanded MP-HIPEs high-value application in frozen-foods and 3D printing.

Keywords: 3D printing; Freeze-thaw stability; High internal phase emulsions; Interfacial adsorption; Myofibrillar protein; Trehalose.