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Enzymatic cross-linking of pea and whey proteins to enhance emulsifying and encapsulation properties

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. Th...

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Bibliographic Details
Published in:Food and bioproducts processing 2023-05, Vol.139, p.204-215
Main Authors: Kim, Woojeong, Wang, Yong, Ye, Qianyu, Yao, Yin, Selomulya, Cordelia
Format: Article
Language:English
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Summary: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. [Display omitted] •Enzymatic cross-linking between pea and whey proteins formed rigid protein network.•Emulsion stability was enhanced by cross-linking with submicron droplets.•Highly stable emulsions were formed by cross-linked pea/whey protein at 2:1 ratio.•Protein cross-linking enhanced encapsulation and protection of β-carotene.
ISSN:0960-3085
DOI:10.1016/j.fbp.2023.03.011