Abstract
Myofibrillar proteins (MPs) have not been fully used for a long time due to its poor solubility in low ionic strength solutions. The study explored the effect of high pressure homogenization (HPH) cycles under two pressures on the solubility of MPs. The MPs solubility increased with HPH cycles (p < 0.05), the results of turbidity, appearance, droplet size indicated that the increase of solubility was due to MPs depolymerization, excessive HPH cycles (25k psi for 11 cycles) would lead to protein re-aggregation but does not affect solubility (p>0.05). SDS-PAGE suggested that myosin formed soluble polymers with different molecular weights through disulfide bonds during HPH cycles, the polymer consisted of myosin subunits of different molecular weights. Endogenous fluorescence spectra, intermolecular chemical forces, isoelectric point analysis and free amino acids (FAAs) indicated that the dissolution of polymers in low ionic strength media was dominated by polar environment and intermolecular steric hindrance, but not to FAAs.
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