Abstract
Understanding how cooking method alters muscle protein structure is critical for optimizing meat texture and quality. This study employed Molecular Dynamics (MD) simulations to elucidate the mechanistic differences between sous-vide (at 27 °C (rt), 60 °C, 65 °C, and 70 °C) and boiling (100 °C) treatments on actomyosin structural stability. Increasing temperature promote α-helix loss and β-sheet formation in all systems. High-temperature sous-vide conditions (65 °C and 70 °C) result in progressive helicity reduction, while β-sheet content remains comparable to the native state. This suggests controlled, gradual protein unfolding without extensive disordered β-sheet aggregation. In contrast, boiling (100 °C) produces a smaller reduction in α-helical content due to hydrophobic collapse that traps localised domains, but induces a marked increase in β-sheet formation. The reduced myosin-actin contacts found in boiling condition also reflect the filament dissociation. Sous-vide provides more actin-myosin contacts indicating the preserved structural integrity of actomyosin complex. These findings demonstrate that sous-vide and boiling follow distinct denaturation pathways: sous-vide promotes gradual intramolecular unfolding, whereas boiling favours rapid β-sheet-driven aggregation and structural disruption. This study provides molecular-level understanding to support optimization of cooking strategies for improved meat quality.