Insight on the emulsifying mechanisms of low-salt type emulsions stabilized by Maillard conjugates: Myofibrillar protein peptide-dextrin with different degrees of hydrolysis.

In this study, we investigated the emulsifying properties and stabilisation mechanisms of low-salt type emulsions stabilised by MP-base conjugates prepared via the Maillard reaction between DX and MP peptides (MPP). Mild hydrolysis by Alcalase promoted a well-controlled Maillard reaction in dry conditions. Combining hydrolysis and Maillard reaction caused the dissociation and unfolding of highly aggregated MP structures; the ordered secondary structure was lost and the hydrophobic residue was exposed. The MPP-DX conjugates greatly improved the emulsifying ability and stability in the low-salt system; the resulting emulsion exhibited a small droplet size and homogeneous microstructure with desirable storage stability. Further, the glycation products were found to effectively suppress gravity-induced creaming. The MPP-DX glycoconjugate developed with 5% DG, exhibiting strongest flocculation and creaming stability, was determined as the optimal emulsifying agent for low-salt type emulsions. These findings provide a theoretical basis for developing low-salt meat products and/or emulsion-based foods.