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Myofibrillar protein marination model: a calculation and its mechanism
Zexu Wang1, Fang Yang1, Qixing Jiang1
1State Key Laboratory of Food Science and Resources, School of Food Science and Technology, Jiangnan University, Wuxi, China.
Background:
The classic diffusion equation and that for osmotic pressure use ion solution, but cannot be applied in a complex food system. The diffusion coefficient (De) is a physical quantity that describes the rate at which a substance diffuses in another medium and is commonly used in diffusion equations. Osmotic pressure (π) refers to the pressure generated when solute molecules in a solution diffuse through a semipermeable membrane toward the solvent side. Myofibrillar protein (MP), a main component in salted meat, was investigated in this study.
Results:
The results showed that, De values in ion solution were always higher (4.00-5.69 × 10-10 m2 s-1) than those in MP (1.33-1.81 × 10-11 m2 s-1), but the declining rate was slower at a salt concentration of 40-80 g kg-1 and quicker at 80-160 g kg-1. πMP (2.84 MPa) was higher than πion (2.68 MPa) only at low contents of salt. When the salt concentration exceeded 40 g kg-1, πMP was lower than πion; πMP increased from 2.84 to 10.08 MPa and πion increased from 2.68 to 10.40 MPa.
Conclusion:
Under low contents of salt, solubility increased and α-helix decreased, resulting in partial unfolding of the protein and enhanced binding to and absorption of water. This made the viscosity decrease, thus reducing the declining rate of De and decreasing πMP. At high contents of salt, aggregation increased viscosity, and thus increased the declining rate of De and πMP. This would provide a theoretical foundation for the amendment of the classic equations of De and πMP. © 2025 Society of Chemical Industry.
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