Evaluation of gel and structural properties of pork myofibrillar protein gels using faba bean protein isolate at...

This study aimed to evaluate the gel and structural properties of pork myofibrillar protein gels (MPGs) using faba bean protein isolate (FBPI) at various salt concentrations.

MPGs were prepared with or without 1 % FBPI under three salt concentrations (0.15, 0.30, and 0.45 M), yielding six treatments. The gel strength, viscosity, and cooking yield were measured. In addition, microstructure, surface hydrophobicity, sulfhydryl group, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis were analyzed to examine the effects of FBPI and salt concentration on the gel and structural properties of MPGs.

MPGs containing 1.0% FBPI had a higher cooking yield, gel strength, protein surface hydrophobicity, and shear stress values than the control groups. The addition of FBPI resulted in more homogenous MPGs with a denser surface compared to the control groups. No interactions in functional properties between FBPI addition and salt concentration were observed, except for gel strength. MPGs at a 0.45 M salt concentration showed a higher cooking yield and hydrophobicity and fewer sulfhydryl groups than those at a 0.15 M salt concentration. The shear stress values at a 0.45 M salt concentration dramatically increased compared to those at 0.15 M and 0.30 M. Furthermore, higher salt concentrations (0.45 M salt) resulted in fewer cavities and a more compact three-dimensional structure.

Higher salt concentrations may improve the rheological properties of MPGs and influence the effects of FBPI on the viscosity and protein patterns. These findings suggested that controlling salt concentration and FBPI level could be an effective strategy to enhance the gelation and structural characteristics of meat protein systems.