Preparation of whole-egg analogs using RuBisCo protein-mung bean protein-glucomannan-ankaflavin conjugates: Formation mechanism and property characterization.

Authors

Ibrahim Khalifa, Remah Sobhy, Zhou Qin, Sajid Maqsood, Xiaobo Zou

Published in

Food chemistry. Volume 525. Issue Pt 1. Pages 150306. Jul 04, 2026. Epub Jul 04, 2026.

Abstract

We fabricated whole-egg analogs (WE) by combining bottom-up-designed yolk (EY) and white (EW) components and benchmarked their performance against real eggs (RE). Molecular docking and 80-ns molecular dynamic simulations revealed binding energies of -5.1, -4.58, and - 3.55 kcal/mol for EY-ankaflavin, EY-glucomannan, and EY-EW conjugates, respectively, with RMSD values around 1.78-1.86 Å, confirming complex stability via noncovalent forces. WE exhibited 1.3-fold higher shear viscosity and more pronounced shear-thinning than RE, a 5 °C lower gelation temperature, and a final gel strength 25% lower. DSC profiles showed two endothermic peaks at ∼65 and ∼ 78 °C, mirroring RE. Texture analysis demonstrated a 40% increase in hardness and a 20% boost in resilience, with springiness and chewiness matching RE. The in vitro digestion assays indicated a 32% increase in lipid hydrolysis, a 28% rise in protein hydrolysis, and 78% vitamin D bio-accessibility in WE, underscoring its nutritional and functional parity with real eggs.

PMID:
42447593
Bibliographic data and abstract were imported from PubMed on 15 Jul 2026.

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