New Opportunities from the Isolation and Utilization of Whey Proteins

Abstract

Management of dairy whey has often involved implementation of the most economical disposal methods, including discharge into waterways and onto fields or simple processing into low value commodity powders. These methods have been, and continue to be, restricted by environmental regulations and the cyclical variations in price associated with commodity products. In any modern regimen for whey management, the focus must therefore be on maximizing the value of available whey solids through greater and more varied utilization of the whey components. The whey protein constituents offer tremendous opportunities. Although whey represents a rich source of proteins with diverse food properties for nutritional, biological, and functional applications, commercial exploitation of these proteins has not been widespread because of a restricted applications base, a lack of viable industrial technologies for protein fractionation, and inconsistency in product quality. These shortcomings are being addressed through the development of novel and commercially relevant whey processing technologies, the preparation of new whey protein fractions, and the exploitation of the properties of these fractions in food and in nontraditional applications. Examples include the following developments: 1) whey proteins as physiologically functional food ingredients, 2) alpha-lactalbumin and beta-lactoglobulin as nutritional and specialized physically functional food ingredients, and 3) minor protein components as specialized food ingredients and an important biotechnological reagents. Specific examples include the isolation and utilization of lactoferrin and the replacement of fetal bovine serum in tissue cell culture applications with a growth factor extract isolated from whey.

Antihypertensive Peptides from Food Proteins

“…As a result of changes in protein structure, the profile of peptides released may differ as digestive enzymes may be capable of digesting these regions of the protein that were previously inaccessible to the enzyme. This has been previously shown to be the case for whey protein [121][122]. Furthermore, ACE inhibitory peptides from whey protein isolates (WPI) pretreated at 65 °C were shown to have greater inhibitory activity than peptides from WPI pretreated at 95 °C.…”

Proteolysis in Milk During Experimental Escherichia coli Mastitis

“…Colony-forming unit increase was effective from PIH 3, and the plateau lasted until PIH 216. The bacteriostactic effect combined with the lag time could last between 3 and 6 h after E. coli inoculation, which corresponded to weak bacterial growth caused by some milk proteins with an inhibitory effect including lactoferrin, lysozyme, and some CN fragments resulting from proteolysis (Lahov and Regelson, 1996;Smithers et al, 1996).…”

Emerging trends in nutraceutical applications of whey protein and its derivatives

“…Whey protein is globular with main components as β-lactoglobulins (35-65 %) and α-lactalbulins (12-25 %). The minor ingredients include immunoglobulins (8 %), serum albumins (5 %) and lactoferrin (1 %) (Smithers et al 1996). Whey protein is a rich source of branched-chain amino acids (leucine, isoleucine, and valine), essential amino acids (cysteine) and peptides as well (Hulmi et al 2010).…”