Type

Journal Article

Authors

Alan L. Kelly
Kees G de Kruif
Patrick F Fox
Thom Huppertz

Subjects

Biochemistry

Topics
chemistry milk proteins pressure whey protein micelles caseins cattle animals protein conformation

High pressure-induced changes in bovine milk proteins: a review. (2005)

Abstract High pressure (HP)-induced changes in the proteins of bovine milk have become an area of considerable research interest in recent years; as a result, there is now a detailed understanding of the effects of HP on casein micelles and whey proteins. HP treatment at pressures >400 or >100 MPa denatures the two most abundant whey proteins, alpha-lactalbumin (alpha-la) and beta-lactoglobulin (beta-lg), respectively. The majority of denatured beta-lg in HP-treated milk associates with the casein micelles, although some denatured beta-lg remains in the serum phase or is attached to the milk fat globule membrane; HP-denatured alpha-la is also associated with the milk fat globules. Casein micelles are disrupted on treatment at pressures >200 MPa; the rate and extent of micellar disruption increases with pressure and is probably due to the increased solubility of calcium phosphate with increasing pressure. On prolonged treatment at 250-300 MPa, reassociation of micellar fragments occurs through hydrophobic bonding; this process does not occur at a pressure >300 MPa, leading to considerably smaller micelles in such milk. As a result of HP-induced changes, the size, number, hydration, composition and light-scattering properties of casein micelles in HP-treated milk differ considerably from those in untreated milk.
Collections Ireland -> University College Cork -> PubMed

Full list of authors on original publication

Alan L. Kelly, Kees G de Kruif, Patrick F Fox, Thom Huppertz

Experts in our system

1
Alan L. Kelly
Teagasc
Total Publications: 63