The effects of high hydrostatic pressure and protein concentration on the denaturation and gelation of whey protein were investigated. Industrial whey protein isolate (WPI) and whey protein concentrate (WPC) solutions (pH 6.8) at various concentrations were pressurized for 10 min at 30 degrees C under 200-1000 MPa. With the WPI solution, the concentration for affecting the turbidity was 1% and was 6% for the viscosity at 400 MPa, while for inducing gelation, it was 10% at 600 MPa. With the WPC solution, the viscosity changed at a concentration >12%, and gel formation began at >18% at 400 MPa. The hardness and breaking stress of pressure-induced WPI gels increased with increasing concentration of WPI (12-18%) and hydrostatic pressure, the ratings for the 20% WPC gels being one-third those of the 20% WPI gels. The solubility of proteins from the pressure-induced WPI gels decreased with increasing pressure, while that of WPC gel induced at >600 MPa remained constant at approximately 50%. The microstructure of the WPI gels had a porous network form, whereas the WPC gels were irregular particulates. beta-Lactoglobulin, alpha-lactalbumin, and serum albumin preferentially participated in pressure-induced aggregation and gelation through S-S bonding.

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