Abstract
This study elucidates the molecular mechanism underlying the enhanced flavor formation in Hunan bacon processed under temperature cycling (4 °C - 55 °C) with liquid smoke. Focusing on the interaction between myofibrillar proteins (MPs) and the key smoke flavor compound 2,3-butanedione, we employed multi-technique approaches including HS-SPME-GC-MS, spectroscopy, and molecular dynamics simulation. Results showed that temperature cycling induced a partially unfolded yet dynamic MP structure, characterized by increased surface hydrophobicity and accessible binding sites, which significantly enhanced the binding capacity and stability for 2,3-butanedione. Thermodynamic analysis revealed the interaction was enthalpy-driven under cycling conditions, facilitating efficient flavor retention. These findings provide a protein-flavor interaction perspective to explain the accelerated ripening and superior sensory quality of bacon processed by cyclic temperature treatment, offering insights for optimizing smoked meat production.