Heat-induced gel formation by soy proteins at neutral pH
article
Heat-induced gel formation by soy protein isolate at pH 7 is discussed. Different heating and cooling rates, heating times, and heating temperatures were used to elucidate the various processes that occur and to study the relative role of covalent and noncovalent protein interactions therein. Gel formation was followed by dynamic rheological measurements. Heat denaturation was a prerequisite for gel formation. The gelation temperature (84 °C) was just above the onset denaturation temperature of glycinin. The stiffness of the gels, measured as the elastic modulos, G′, increased with the proportion of denatured protein. An increase in G′ was also observed during prolonged heating at 90 °C. This increase is explained by the occurrence of rearrangements in the network structure and probably also by further incorporation of protein in the network. The increase in G′ upon cooling was thermoreversible indicating that disulfide bond formation and rearrangements do not occur upon cooling.
Topics
GelationProtein-protein interactionsRearrangementsRheologySoy protein isolateDisulfideGlobulinGlycininSoybean proteinChemistryCoolingDifferential scanning calorimetryDisulfide bondElasticityFlow kineticsGelGelationHeatHeatingMeasurementPHPhysical chemistryProtein denaturationProtein isolationProtein protein interactionRigidityTemperatureThermodynamicsYoung modulusCalorimetry, Differential ScanningChemistry, PhysicalDisulfidesElasticityGelsGlobulinsHeatHydrogen-Ion ConcentrationProtein DenaturationRheologySoybean ProteinsThermodynamics
TNO Identifier
72614
ISSN
00218561
Source
Journal of Agricultural and Food Chemistry, 50, pp. 1569-1573.
Pages
1569-1573
Files
To receive the publication files, please send an e-mail request to TNO Repository.