Multidimensional mechanism of pulsed electric field synergized L-arginine upon goose meat tenderization: Based on molecular dynamics simulation and protein interaction network

Although pulsed electric field (PEF) and L-arginine alone can improve meat tenderness, their synergistic molecular mechanism remains unclear. This study first explored the tenderization mechanism of combined PEF and L-arginine (LP) in goose meat. Results showed that LP reduced goose meat shear force by 51.30%, with effects significantly superior to either treatment alone. Hematoxylin-eosin staining revealed that LP enlarged intermuscular spaces. Infrared spectroscopy indicated that LP induced a conformational shift from α-helix to β-sheet in myofibrillar proteins (MPs). Fluorescence spectroscopy showed a significantly increased fluorescence intensity, confirming structural unfolding of MPs. Enzyme activity assays showed that LP elevated calpain activity by 64.33%. SDS-PAGE further confirmed the accelerated degradation of troponin-T. Molecular dynamics simulations revealed that PEF primarily drives the restructuring of the enzyme-substrate binding interface, while L-arginine stabilizes the process by maintaining the hydrogen bond network. This study provides a theoretical basis for developing efficient and controllable meat tenderization technologies.