Protein-protein noncovalent ligand binding enables structural improvements in 3D-printed fish analogs by molecular synergy of soy, mung, and potato proteins

In this study, 3D-printed fish analogs were fabricated using soybean (SPI), mung bean (MBP), and potato proteins (PP) by employing a bottom-up design of single (FA-1), binary (FA-2/3), and ternary (FA-4) protein-protein-lutein interactions. The fabricated fish analogs were characterized by their rheological, textural, thermal, and morphological features. The molecular docking and multispectral findings were used to understand the possible synergistic interaction among proteins, and the results disclosed that SPI-MBP-PP showed more noncovalent forces, which later reflected in efficient binding with lutein to form the suitable edible inks via H-bonds, electrostatic, and hydrophobic forces. FA-4 showed optimized water mobility while maintaining shape fidelity necessary for consistent 3D-printed fabrication of fish analogs. Meanwhile, fish analog formulations for 3D printing showed varying rheological and textural properties, while FA-4 offered superior structural integrity and binding properties for stable printing. FA-4 exhibited superior thermal stability (XRD & DSC patterns), correlating with better 3D-printing performance through improved flow behavior and shape retention. Taken together, the 3D-printed fish-analogs formulated herein may be appropriate for consumers pursuing healthy and sustainable plant-based substitutes. • Ternary SPI-MBP-PP synergy via H-bonding/hydrophobic forces boosted edible ink stability. • FA-4 optimizes water mobility and shape fidelity for consistent 3D-printed fish analogs. • Superior structural integrity in FA-4 enabled stable 3D printing via enhanced binding. • FA-4 thermal stability (XRD/DSC) correlated with improved flow behavior and shape retention. • Plant-based fish analogs offer sustainable alternatives with optimized texture and printability.