Using extrusion heat-denatured soy protein isolate (SPI) as a model, the mechanism for refunctionalizing heat-denatured soy protein by hydrothermal cooking (HTC) with alkali was studied. Heating causes soluble protein to form insoluble protein aggregates. Treating heat-denatured soy protein with alkali dispersion without HTC increased solubility and viscosity by dissolution of a portion of the protein aggregates and swelling of the large protein particles. This suspension was more stable to solid separation than that of the original untreated heat-denatured protein, but it was less stable than the protein suspensions that were refunctionalized by water dispersion with HTC or alkali dispersion with HTC. Water dispersion with HTC disrupted the large aggregates into smaller aggregates. The viscosity and total number of particles in the system also increased dramatically. The most significant effect was achieved with alkali dispersion (0.6 mmol NaOH/g) with HTC. The solubility increased from 4 to about 80% at neutral pH, and viscosity (at zero shear rate) increased by more than 1,000 times compared with extrusion heatdenatured SPI. Alkali dispersion (0.6 mmol NaOH/g) with HTC dissolved most of the protein particles, decreasing the particle number by a factor of almost 100. The suspensions of heat-denatured soy protein became much more stable after HTC as shown by particle settling velocities. The most effective treatment was alkali dispersion (0.6 mmol NaOH/g) with HTC, followed by water dispersion with HTC. The soy protein slurry refunctionalized by alkali dispersion (0.6 mmol NaOH/g) with HTC formed soft, translucent gels.Our previous work showed that hydrothermal cooking (HTC), especially when the protein was dispersed in alkali (0.2-0.8 mmol/g meal) prior to HTC, improved the functional properties, such as solids dispersibility, emulsification capacity, and foaming properties, of extruded-expelled (EE) soybean protein meals (1,2). The protein yield of soy protein isolate (SPI) after alkali dispersion with HTC (alkaline HTC) of EE soybean meal was improved by twofold (from 40 to 81%) compared with the original meal, whereas the protein yield after water dispersion with HTC (HTC without alkali) was 53%. We hypothesized that alkali dispersion with HTC increases the extractability of the protein and the stability of the resulting protein suspension (as SPI). The favorable increase in SPI properties could be due to increased protein solubility or dispersibility, decreased particle size of the denatured protein aggregates, increased viscosity, and/or reduced density differences between the dispersed and continuous phases. To eliminate interference from nonprotein components in EE meal, such as fiber and residual oil, we chose native SPI (with protein content >90%) as a model to study the mechanism of protein refunctionalization and improvement in SPI yield by alkali dispersion with HTC.
EXPERIMENTAL PROCEDURESMaterials. Native SPI (spray-dried without other intentional heat denaturation or additives) prepared at the Ce...