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Phospholipid-myosin non-covalent binding in emulsified meat systems: Interfacial behavior and conformational changes
Jing Liu1, Mingming Huang1, Yanwei Mao1
1College of Food Science and Engineering, Shandong Agricultural University, Tai'an 271018, PR China.
Abstract:
This study examines non-covalent interactions between phospholipids and myosin in emulsified meat by varying myosin and lecithin ratios (M-L1:0 to M-L1:2). Lecithin competitively displaces myosin at oil-water interfaces, reducing droplet size from 8.2 to 1.6 μm and modulating zeta potential. Interfacial myosin adsorption decreases from 43.58% to 24.08% at lower lecithin ratios (≤M-L1:1). Conformationally, low lecithin ratios (≤M-L1:1) induce β-sheet enrichment, enhancing rigidity, while higher ratios (≥M-L1:1) revert myosin to a disordered state. Binding of lecithin can increase myosin surface hydrophobicity (P < 0.05), validated through fluorescence quenching and characteristic hydrogen-bonding at 3661 cm-1, which correlates with improved thermal and storage stability. Molecular dynamics confirm that phosphatidylcholine embeds spontaneously in myosin's hydrophobic groove (ΔG = -55.36 kcal/mol), with hydrophobic interactions dominating, synergized by hydrogen bonds and electrostatic forces. These mechanisms establish a theoretical framework for emulsified meat systems.
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