The effects of salt concentration and pH upon water-binding, water-holding and protein extractability of turkey meat

The effects of salt concentration and pH upon protein extractability and water-binding by homogenates of turkey breast, thigh and drumstick meat, and also the effect of salt concentration and centrifugal force upon water-binding of raw meat and water-holding of cooked meat from breast and thigh were studied. Concentrations of sodium chloride above 0.3 M caused swelling of meat homogenates. With the pH value adjusted to 6.0 and with sodium chloride concentrations greater than 0.6 M, breast meat was able to swell more than leg meat. Water-binding increased with increasing pH value. Breast meat homogenates had more extractable protein than leg meat homogenates and protein extraction was increased by increasing both salt concentration and pH. Cooked breast meat retained more water than leg meat with or without salt. At low concentrations of salt, cooked breast meat retained more water than raw meats, but this was reversed at higher salt concentrations.     

Evaluation of mungbean protein isolates at various levels as a substrate for microbial transglutaminase and water binding agent in pork myofibrillar protein gels

The objective of this study was to investigate the effect of mungbean protein isolate (MPI) on the potential possibility of water binding agent and as a substrate for the microbial transglutaminase (MTGase) in myofibrillar protein. Cooking loss (CL,%), gel strength (GS, gf), sodium dodecyl sulphate‐polyacrylamide gel electrophoresis (SDS‐PAGE), differential scanning calorimetry (DSC) and scanning electron microscopy (SEM) were measured. The addition of MPI reduced CL, indicating that it has a water binding capacity during cooking. The major protein band (53 kDa) of MPI appeared when MPI was mixed with MP, but it disappeared when MTGase was incorporated. MPI treatment changed the endothermic peaks as compared with those of CTL. MTGase (1%) mediated pork MP increased CL and GS (P < 0.05), and reduced peak temperatures with vanishing of endothermic intensity at 1st and 3rd peaks, suggesting the structural changes of protein gelation. In microstructures, MTGase treatment showed a finely stranded structure in MP gels, while MPI showed a conglomerated surface in MTGase‐mediated MP gels. These results indicated that MPI appears to be a water binding agent during cooking and function as a substrate for MTGase in MP gelation.     

Dielectric properties of soybean protein isolate dispersions as a function of concentration, temperature and pH

Dielectric properties of commercial soy protein isolate (SPI) dispersions were measured over the frequency range of 200-2500 MHz by the open-ended coaxial probe method using a network analyzer as a function of concentration (5, 10 and 15 g/100 g water), temperature (20-90 °C) and pH (4.5, 6.6 and 10). Results indicated that the dielectric constant (ε′) decreased with temperature (except at 90 °C) and frequency while increased with concentration. The loss factor (ε″) increased with frequency and concentration; however, temperature showed mixed effect. Both ε′ and ε″ data were related to frequency using a polynomial model. The significant change in ε′ and ε″ at 90 °C was a result of protein denaturation which was identified by differential scanning calorimetry (DSC). Change in the association/dissociation behavior of SPI dispersions due to electrostatic attraction/repulsion among protein molecules on heating as a function of pH was assumed to be responsible for the significant increase in dielectric parameters. Penetration depth (D_p) was estimated under various conditions and it decreased with an increase in frequency, concentration, temperature and pH. The minimum D_p was found at alkaline pH at a temperature of 90 °C and frequency of 2450 MHz.