Moisture-induced aggregation of whey proteins
Authors discuss factors (irreversible moisture-induced protein aggregation, hydrophilic interactions and advanced Maillard reactions) that cause loss of functionality and nutritional value of whey proteins.
Roles of charge interactions on astringency of whey proteins at low pH
This study compared the astringency of β-lactoglobulin (β-LG) at low pH with phosphate buffer controls having the same amount of phosphate and at similar pH. Results show that β-LG solutions are more astringent than phosphate buffers at similar pH and phosphate levels. Astringency is caused by acid and protein.
Effects of polyols on the stability of whey proteins in intermediate-moisture food model systems
This study determined how polyols influence the stability of whey proteins in intermediate-moisture food systems and cause bar hardening in protein-based nutrition bars. Results show that propylene glycol should not be used in whey-protein-based, high-protein, intermediate-moisture foods because it changes the protein conformation and stability. These changes result in protein aggregation that hardens the bar texture during storage.
Emulsifying properties of lactose-amines in oil-in-water emulsions
Lactose-amines were synthesized with hexadecyl-amide and lactose via the Maillard reaction, and their emulsion stabilization properties were investigated. Results show that lactose-amines synthesized with various heating conditions resulted in samples with emulsification activity.
Effect of composition on moisture sorption of delactosed permeate
Delactosed permeate (DLP) is an effluent generated after proteins and lactose are separated from cheese whey. DLP is difficult to commercialize because it has a high moisture content and is an unstable ingredient. This study identifies the primary constituents in DLP with the most influence on the characteristic sorption behavior of DLP, which is responsible for its stickiness and hygroscopicity.
Moisture-induced aggregation of whey proteins in a protein/buffer model system
This study evaluated the molecular mechanisms and controlling factors for moisture-induced whey protein aggregation in a model system. These aggregates rapidly formed during the first three days of storage at 35 C with a slower rate afterward. Intermolecular disulfide bonds were the main mechanism for protein aggregation.
Charged ultrafiltration membranes for whey protein fractionation
This study examined the use of positively charged membranes to increase the selectivity of ultrafiltration (UF) and allow the fractionation of proteins from cheese whey. By adding a positive charge to UF membranes, and adjusting the solution pH, it was possible to permeate proteins having little or no charge, such as glycomacropeptide, and retain proteins having a positive charge.