Abstract
The effect of high-pressure processing (200 MPa, 10 min) on the solubility of chicken breast myosin with 25% molar substitution of Na(+) by 3 anion types of potassium salts (KCl, K-lactate, and K-citrate) was investigated. The results showed that the lower hydrophobic group and reactive sulfhydryl group of nonpressurized myosin with the replacement of organic K-lactate or K-citrate possibly contributed to the aggregation of myosin molecules compared with the KCl group and thus decreased the solubility of both. In the presence of lactate or citrate, the high-pressure processing caused an increase in the surface hydrophobicity and reactive sulfhydryl group, indicating the unfolding of myosin molecule. Meanwhile, the increased hydration state and the decreased apparent viscosity suggested the disruption of protein-protein interactions and the strengthening of myosin-water interactions in pressurized myosin, ultimately resulting in increased solubility of the pressurized myosin with both organic potassium salts. The compensation of high-pressure processing is interesting for the efficient selection of the anion type in developing sodium-reduced industrial meat products.