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

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.