Whey protein soluble aggregates from heating with NaCl: physicochemical, interfacial, and foaming properties.
Whey protein isolate was heat-treated at 85 degrees C for 15 min at pH ranging from 6.0 to 7.0 in the presence of NaCl in order to generate the highest possible amount of soluble aggregates before insolubility occurred. These whey protein soluble aggregates were characterized for composition, hydrodynamic diameter, apparent molecular weight, zeta-potential, surface hydrophobicity index, activated thiol group content, and microstructure. The adsorption kinetics and rheological properties (E', etad) of these soluble aggregates were probed at the air/water interface. In addition, the gas permeability of a single bubble stabilized by the whey protein soluble aggregates was determined. Finally, the foaming and foam-stabilizing properties of these aggregates were measured. The amount of whey protein soluble aggregates after heat treatment was increased from 75% to 95% from pH 6.0 to pH 7.0 by addition of 5 mM to 120 mM NaCl, respectively. These soluble aggregates involved major whey protein fractions and exhibited a maximum of activated thiol group content at pH > 6.6. The hydrodynamic radius and the surface hydrophobicity index of the soluble aggregates increased from pH 6.0 to 7.0, but the molecular weight and zeta-potential decreased. This loss of apparent density was clearly confirmed by microscopy as the soluble aggregates shifted from a spherical/compact structure at pH 6.0 to a more fibrillar/elongated structure at pH 7.0. Surface adsorption was faster for soluble aggregates formed at pH 6.8 and 7.0 in the presence of 100 and 120 mM NaCl, respectively. However, interfacial elasticity and viscosity measured at 0.01 Hz were similar from pH 6.0 to 7.0. Single bubble gas permeability significantly decreased for aggregates generated at pH > 6.6. Furthermore, these aggregates exhibited the highest foamability and foam liquid stability. Air bubble size within the foam was the lowest at pH 7.0. The coarsening exponent, alpha, fell within predicted values of 1/3 and 1/2, except for very dry foams where it was 1/5.
Schmitt
Christophe
C
Department of Food Science, Nestlé Research Center, Vers-chez-les-Blanc, CH-1000 Lausanne 26, Switzerland. christophe.schmitt@rdls.nestle.com
Bovay
Claudine
C
Rouvet
Martine
M
Shojaei-Rami
Sabrina
S
Kolodziejczyk
Eric
E
D002627:Chemistry, Physical / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D008027:Light; D046529:Microscopy, Electron, Transmission; D008894:Milk Proteins / Q000737:chemistry*; D015233:Models, Statistical; D010316:Particle Size; D010539:Permeability; D011312:Pressure; D011485:Protein Binding; D011487:Protein Conformation; D012542:Scattering, Radiation; D012965:Sodium Chloride / Q000737:chemistry*; D012995:Solubility; D013499:Surface Properties; D000067816:Whey Proteins
D008894:Milk Proteins; D000067816:Whey Proteins; D012965:Sodium Chloride