Effects of sodium hexametaphosphate, sodium tripolyphosphate and sodium pyrophosphate on the ultrastructure of beef myofibrillar proteins investigated with atomic force microscopy

Myofibrillar protein isolated from beef muscles were treated with 3 phosphates (Sodium Hexametaphosphate, sodium tripolyphosphate, sodium pyrophosphate) with different concentrations of 0.3%, 0.6%, 0.9%, 1.2% respectively. Protein solubility, surface hydrophobicity and reactive sulfhydryl group was determined. Atomic force microscopy was used to observe the microscopic protein surface. SDS-PAGE was carried out to determine the proteolysis of myofibrillar protein. The solubility and surface hydrophobic bond of myofibrillar protein was highly increased and the diameter decreased by SHMP, TSPP, STPP. Reactive sulfhydryl groups increased after SHMP addition, but slightly decreased in STPP and TSPP treated MP. TSPP and STPP had the same effect on myofibrillar microstructure and was different from SHMP. Three phosphates all caused MP unfolding. The MP gel complexity was increased, and roughness was decreased after phosphates addition, indicating phosphates helped to construct a more ordered and smoother gel microcosmic surface.

Automated summary

The study investigated the effects of three phosphates (SHMP, TSPP, STPP) on myofibrillar protein from beef muscles, showing significant changes in protein solubility, surface hydrophobicity, and reactive sulfhydryl groups. Phosphate addition led to structural alterations in myofibrillar protein, increasing solubility and surface hydrophobicity while reducing diameter. The phosphates helped construct a more ordered and smoother gel microcosmic surface, resulting in increased gel complexity and decreased roughness.