Abstract
Improving the functionality of commercial plant proteins is essential for food application. Here an alternative strategy is provided to modify the structure of pea protein by microbial transglutaminase-induced cross-linking with whey protein for enhancing emulsifying and encapsulation properties. The protein structures and the physicochemical stability of β-carotene-loaded emulsions were investigated subject to protein ratio and cross-linking. Formation of disulphide and isopeptide bonds between heteroproteins according to cross-linking changed protein structures by exposing the hydrophobic sites of proteins with stiffer network. The cross-linked pea/whey protein complexes at protein ratio of 2:1 formed a stable emulsion with a droplet size of 0.10 µm, showing no phase separation for 30 days of storage and high encapsulation efficiency of 92%. These findings provided a novel strategy to design plant/dairy protein networks to protect lipophilic bioactive compounds by replacing half or more dairy protein with plant protein, leading to gradual change towards plant-based diets.
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