Modifying the surface properties of whey protein using ultrafiltration

Changing the content of individual whey proteins by use of ultrafiltration was studied for enhancing the physico-functional properties of the modified whey protein concentrate (WPC). Whey was ultrafiltered using membranes with a molecular weight cut-off limit of 100 kDa to remove parts of the smaller proteins, alpha-lactalbumin (alpha-La) and caseinomacropeptide (CMP). The composition of the whey protein was determined using the SE-FPLC in connection with the Superose 12 column. Chromatographic profiles of the retentates indicated a steady decrease in CMP and alpha-La in progress of the ultrafiltration and also an increase in serum albumin and immunoglobulins depending on the volume reduction ratio. The permeate proteins are not lost, i.e., they can serve as a source for isolating CMP and alpha-La. Retentates enriched in Ig were found to support foaming and emulsifying properties.