title: Heat-induced gel formation by soy proteins at neutral pH.
abstract: 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 degrees C) was just above the onset denaturation temperature of glycinin. The stiffness of the gels, measured as the elastic modulus, G', increased with the proportion of denatured protein. An increase in G' was also observed during prolonged heating at 90 degrees 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.
authors.affiliation: Centre for Protein Technology TNO-Nutrition and Wageningen University, Laboratory of Food Physics, P.O. Box 8129, 6700 EV Wageningen, The Netherlands.
authors.forename: Jacoba M S
authors.initials: JM
authors.lastname: Renkema
authors.forename: Ton
authors.initials: T
authors.lastname: van Vliet
mesh_terms: D002152:Calorimetry, Differential Scanning; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004220:Disulfides / Q000737:chemistry; D004548:Elasticity; D005782:Gels; D005916:Globulins / Q000737:chemistry; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D011489:Protein Denaturation; D012212:Rheology; D030262:Soybean Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D004220:Disulfides; D005782:Gels; D005916:Globulins; D030262:Soybean Proteins; C011474:glycinin