Influence of Milk Peptides in Determining the Functionality of Milk Proteins: A Review

Abstract

Milk is a rich source of functional ingredients. Unfortunately, milk is also rich in surface-active peptides that modulate the functionality of milk proteins. Fractionation, amino acid analysis and sequencing, and computerized hydropathy calculations showed that these peptides are highly amphipathic. These peptides exert their effects primarily by markedly decreasing surface or interfacial tension and by altering the colloidal properties of proteins. The hydrophobically driven association tendency of proteins, which plays a key role in interfacial stability, is diminished because of the masking of hydrophobic patches by the peptides. Destabilization of emulsions, to an extent, may also be due to desorption of proteins from the interface as a result of the greater surface activity of amphipathic peptides. Experiments are described in which controlled hydrolysis to generate trace amounts of peptides significantly altered the functionality of milk protein powders. Some theoretical bases of the observations are discussed.

A comparative study of the gelation properties of whey protein concentrate and whey protein isolate

“…Wang and Lucey [40] found that there was very little GMP (< 2%) in WPI made using an ion-exchange process compared with levels of up to 26% of the total protein content in WPI made by membrane filtration processes, respectively. The supplier of the whey protein products analyzed the WPC and WPI in relation to the annex IV of EU regulation (EG) 1725/79 (1999), which allows only a Haque [19] reported that hydrophobic peptides in milk or whey, which will be concentrated by ultrafiltration, may mask hydrophobic areas of proteins. Brandenburger et al [3] hypothesized that variations in WPC and WPI functionality might be due, in part, to differences in their low-molecular-weight components, i.e.…”

Wetting properties of food packaging

“…This indicates that milk could interact with the film. As already mentioned, milk is an emulsion rich in surface-active compounds known to decrease interfacial tension (Haque, 1993). The h ap values suggest that vibration enhanced the surface interaction with the milk surface's active components (e.g., amphipathic peptides, whey proteins, caseins and free fatty acids, Fennema, 1996;Kristensen, Jensen, Madsen, & Birdi, 1997;Williams, Jons, Paterson, & Pearce, 2005), improving wettability.…”

Modifications of structures and functions of caseins: a scientific and technological challenge

“…The relationship between enzymatic hydrolysis and structural change of casein is studied since several years (Lee et al 1987;Haque 1993;Panyam and Kilara 1996;Chobert et al 1998;Slattery and Fitzgerald 1998;Gastaldi et al 2003;Banach et al 2013;Wang et al 2013;Luo et al 2014). From a general point of view, proteolysis of caseins induces (1) decrease in their molecular weight, (2) increase in the number of ionized groups (NH 3 + and COO − ), and (3) conformational ND not determined change with exposure of hydrophobic groups.…”