High pressure-induced changes in bovine milk proteins: A review

Huppertz, Thom, Fox, Patrick F., de Kruif, Kees G. and Kelly, Alan L. (2006) High pressure-induced changes in bovine milk proteins: A review. BBA: Proteins and Proteomics, 1764 3: 593-598. doi:10.1016/j.bbapap.2005.11.010

Author Huppertz, Thom
Fox, Patrick F.
de Kruif, Kees G.
Kelly, Alan L.
Title High pressure-induced changes in bovine milk proteins: A review
Journal name BBA: Proteins and Proteomics   Check publisher's open access policy
ISSN 1570-9639
Publication date 2006-03-01
Year available 2005
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1016/j.bbapap.2005.11.010
Volume 1764
Issue 3
Start page 593
End page 598
Total pages 6
Editor Reinhard Lange
Place of publication Amsterdam
Publisher Elsevier Science Bv
Language eng
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-1g), respectively The majority of denatured beta-1g in HP-treated milk associates with the casein micelles, although some denatured beta-1g remains in the serum phase or is attached to the milk fat globule membrane; HP-denatured a-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. (c) 2005 Elsevier B.V. All rights reserved.
Keyword α-lactalbumin
High pressure
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ
Additional Notes Available online 19 December 2005. Issue: Proteins Under High Pressure.

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collection: School of Agriculture and Food Sciences
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Created: Sat, 26 Jan 2008, 02:49:33 EST