Antibody binding and functional properties of whey protein hydrolysates obtained under high pressure

• Published in: Food hydrocolloids Vol. 23; no. 3; pp. 593 - 599
• Main Authors: Chicón, Rosa, Belloque, Josefina, Alonso, Elena, López-Fandiño, Rosina
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.05.2009; [New York, NY]: Elsevier Science; Elsevier
• Subjects: allergenicity; antigens; binding properties; Biological and medical sciences; dairy products; Emulsifying activity; emulsifying properties; Emulsions; Food additives; food allergies; Food industries; Foods; functional properties; Fundamental and applied biological sciences. Psychology; General aspects; Heat stability; High pressure; high pressure treatment; Hydrolysates; hydrophobicity; hypoallergenic foods; IgE-binding; IgG-binding; immunoglobulin E; immunoglobulin G; isoelectric point; lactalbumin; lactoglobulins; Milk and cheese industries. Ice creams; Pepsin; Peptides; protein binding; protein hydrolysates; Proteins; proteolysis; Whey; whey protein; Whey proteins; Heat stability; IgE-binding; Whey proteins; IgG-binding; Hydrolysates; High pressure; Emulsifying activity; Stability; Physical dressing; Milk protein; Hydrolysate; Quality; Whey protein
• ISSN: 0268-005X; 1873-7137
• DOI: 10.1016/j.foodhyd.2008.04.001

This paper examines the potential of high hydrostatic pressure to produce whey protein hydrolysates that combine low immunoglobulin (Ig)G- and IgE-binding with acceptable functional properties, with the aim to produce milk-based ingredients with reduced potential allergenicity that could be used in hypoallergenic foods. Treatment with pepsin and chymotrypsin under high pressure produced, in minutes, hydrolysates in which α-lactalbumin and β-lactoglobulin were totally proteolysed, giving rise to large and hydrophobic peptides. Such hydrolysates presented reduced antigenicity and human IgE-binding properties. The hydrolysates obtained with pepsin at 400 MPa showed improved heat stability, particularly at a pH, close to the isoelectric point of the whey proteins, and their emulsion activity indexes at pH 7.0 were superior to those of the untreated whey proteins. These results suggest that the peptides present retained low antigenicity together with sufficient capacity to form emulsions.