Hostname: page-component-cd9895bd7-7cvxr Total loading time: 0 Render date: 2024-12-21T16:08:18.643Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of high hydrostatic pressure and whey proteins on the disruption of casein micelle isolates

Published online by Cambridge University Press:  26 October 2007

Federico M Harte ,
Subba Rao Gurram ,
Lloyd O Luedecke ,
Barry G Swanson  and
Gustavo V Barbosa-Cánovas
Federico M Harte
Affiliation:
Biological Systems Engineering Department, Washington State University, Pullman, WA 99164-6120USA
Subba Rao Gurram
Affiliation:
Biological Systems Engineering Department, Washington State University, Pullman, WA 99164-6120USA
Lloyd O Luedecke
Affiliation:
Department of Food Science and Human Nutrition, Washington State University, Pullman, WA 99164-6376USA
Barry G Swanson
Affiliation:
Department of Food Science and Human Nutrition, Washington State University, Pullman, WA 99164-6376USA
Gustavo V Barbosa-Cánovas*
Affiliation:
Biological Systems Engineering Department, Washington State University, Pullman, WA 99164-6120USA
*
*For correspondence; e-mail: barbosa@wsu.edu
Get access Rights & Permissions [Opens in a new window]

Abstract

High hydrostatic pressure disruption of casein micelle isolates was studied by analytical ultracentrifugation and transmission electron microscopy. Casein micelles were isolated from skim milk and subjected to combinations of thermal treatment (85°C, 20 min) and high hydrostatic pressure (up to 676 MPa) with and without whey protein added. High hydrostatic pressure promoted extensive disruption of the casein micelles in the 250 to 310 MPa pressure range. At pressures greater than 310 MPa no further disruption was observed. The addition of whey protein to casein micelle isolates protected the micelles from high hydrostatic pressure induced disruption only when the mix was thermally processed before pressure treatment. The more whey protein was added (up to 5 g/l) the more the protection against high hydrostatic pressure induced micelle disruption was observed in thermally treated samples subjected to 310 MPa.

Keywords

High hydrostatic pressurecaseinmicelleanalytical ultracentrifugation
Type
Research Article
Information
Journal of Dairy Research , Volume 74 , Issue 4 , November 2007 , pp. 452 - 458
Copyright
Copyright © Proprietors of Journal of Dairy Research 2007

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Anema, SG & Li, Y 2003a Effect of pH on the association of denatured whey proteins with casein micelles in heated reconstituted skim milk. Journal of Agricultural Food Chemistry 51 1640–1646CrossRefGoogle ScholarPubMed
Anema, SG & Li, Y 2003b Association of denatured whey proteins with casein micelles in heated reconstituted skim milk and its effect on casein micelle size. International Dairy Journal 70(1) 73–83Google ScholarPubMed
Anema, SG, Lowe, KE & Stockmann, R 2005 Particle size changes and casein solubilization in high pressure treated skim milk. Food Hydrocolloids 19 257–267CrossRefGoogle Scholar
Buchheim, W, Schrader, K, Morr, CV, Frede, E & Schutt, M 1996 Effects of high pressure on the protein, lipid and mineral phase of milk. In Heat treatments & alternative methods, pp. 202–213 (Ed Fox, PF). Brussels: International Dairy FederationGoogle Scholar
Dalgleish, DG 1998 Casein micelles as colloids: surface structures and stabilities. Journal of Dairy Science 81(11) 3013–3018CrossRefGoogle Scholar
Datta, N & Deeth, HC 1999 High pressure processing of milk and dairy products. The Australian Journal of Dairy Technology 54(1) 41–49Google Scholar
Drake, MA, Harrison, SL, Asplund, M, Barbosa-Cánovas, GV & Swanson, BG 1997 High-pressure treatment of milk and effects on microbiological and sensory quality of Cheddar cheese. Journal of Food Science 62(4) 843–860CrossRefGoogle Scholar
Fox, PF & McSweeney, PLH 1998 Dairy Chemistry and Biochemistry. New York: Chapman & HallGoogle Scholar
Gaucheron, F, Famelart, MH, Mariette, F, Raulot, K, Michel, F & Le Graet, Y 1997 Combined effects of temperature and high-pressure treatments on physicochemical characteristics of skim milk. Food Chemistry 59(3) 439–447CrossRefGoogle Scholar
Gebhardt, R, Doster, W & Kulozik, U 2005 Pressure-induced dissociation of casein micelles: size distribution and effect of temperature. Brazilian Journal of Medical and Biological Research 38 1209–1214CrossRefGoogle ScholarPubMed
Gulbrandsen, TD, Jansen, MB, Langsrud, T & Elisabeth, GV 2000 Size of native and heated casein micelles, content of protein and minerals in milk from Norwegian Red Cattle-effect of milk protein polymorphism and different feeding regimes. International Dairy Journal 10 313–323Google Scholar
Harte, F, Amonte, M, Luedecke, L, Swanson, BG & Barbosa-Cánovas, GV 2002a Yield stress and microstructure of set yogurt made from high hydrostatic pressure-treated full fat milk. Journal of Food Science 67(6) 2245–2250CrossRefGoogle Scholar
Harte, FM, Luedecke, LO, Swanson, BG & Barbosa-Cánovas, GV 2002b Disrupting effect of high hydrostatic pressure on casein micelle isolates. IFT Annual Meeting Technical Program Abstracts 130Google Scholar
Hoover, DG 2002 Microbial inactivation by high pressure. In Control of Foodborne Pathogens, pp. 419–449 (Eds Juneja, VK & Sofos, JN). New York: Marcel DekkerGoogle Scholar
Huppertz, T, Kelly, AL & Fox, PF 2002 Effects of high pressure on constituents and properties of milk. International Dairy Journal 12(7) 561–572CrossRefGoogle Scholar
Huppertz, T, Fox, PF & Kelly, AL 2003 High pressure induced changes in the creaming properties of bovine milk. Innovative Food Science and Emerging Technologies 4 349–359CrossRefGoogle Scholar
Huppertz, T, Fox, PF & Kelly, AL 2004a High pressure treatment of bovine milk: effects of casein micelles and whey proteins. Journal of Dairy Research 71 97–106CrossRefGoogle ScholarPubMed
Huppertz, T, Fox, PF & Kelly, AL 2004b Properties of casein micelles in high pressure-treated bovine milk. Food Chemistry 87 103–110CrossRefGoogle Scholar
Huppertz, T, Grosman, S, Fox, PF & Kelly, AL 2004c Heat and ethanol stabilities of high-pressure-treated bovine milk. International Dairy Journal 14 125–133CrossRefGoogle Scholar
Huppertz, T & Kruif, CG 2006 Disruption of casein micelles under high pressure: Influence of milk serum composition and casein micelle concentration. Journal of Agriculture and Food Chemistry 54 5903–5909CrossRefGoogle ScholarPubMed
Keenan, RD, Young, DJ, Tier, CM, Jones, AD & Underdown, J 2001 Mechanism of pressure-induced gelation of milk. Journal of Agricultural and Food Chemistry 49(7) 3394–3403CrossRefGoogle Scholar
Kelly, AL, Huppertz, T & Fox, PF 2002 Structural properties of casein micelles in high-pressure-treated milk. Technical Program Abstract 197IFT Annual MeetingGoogle Scholar
López-Fandiño, R, Carrascosa, AV & Olano, A 1996 The effects of high pressure on whey protein denaturation and cheese-making properties of raw milk. Journal of Dairy Science 79(6) 929–936CrossRefGoogle Scholar
Needs, EC, Capellas, M, Bland, AP, Manoj, P, Macdougal, D & Paul, G 2000a Comparison of heat and pressure treatments of skim milk, fortified with whey protein concentrate, for set yogurt preparation: effects on milk proteins and gel structure. Journal of Dairy Research 67(3) 329–348CrossRefGoogle ScholarPubMed
Needs, EC, Stenning, RA, Gill, AL, Ferragut, V & Rich, GT 2000b High-pressure treatment of milk: effects on casein micelle structure and on enzymic coagulation. Journal of Dairy Research 67(1) 31–42CrossRefGoogle ScholarPubMed
Panick, G, Malessa, R & Winter, R 1999 Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray. Biochemistry 38(20) 6512–6519CrossRefGoogle ScholarPubMed
Pierre, A, Michael, F & Le Graet, Y 1995 Variation in size of goat milk casein micelles related to casein genotype. Lait 75 489–502CrossRefGoogle Scholar
Regnault, S, Thiebaud, M, Dumay, E & Cheftel, JC 2004 Pressurization of raw skim milk of a dispersion of phosphocaseinate at 9°C or 20°C: effects on casein micelle size distribution. International Dairy Journal 14 55–68CrossRefGoogle Scholar
Schmidt, DG & Buchheim, W 1970 An electron-microscopy investigation of substructure of the casein micelles in cow's milk. Milchwissenschaft 25 596–600Google Scholar
Schrader, K & Buchheim, W 1998 High pressure effects on the colloidal calcium phosphate and the structural integrity of micellar casein in milk II. Kinetics of the casein micelle disintegration and protein interactions in milk. Kieler Milchwirtschaftliche Forschungsberichte 50 79–88Google Scholar
Scollard, PG, Beresford, TP, Needs, EC, Murphy, PM & Kelly, AL 2000 Plasmin activity, β-lactoglobulin denaturation and proteolysis in high pressure treated milk. International Dairy Journal 10 835–841CrossRefGoogle Scholar
Stothart, PH & Cebula, DJ 1982 Small-angle neutron scattering study of bovine casein micelles and sub-micelles. Journal of Molecular Biology 160(2) 391–395CrossRefGoogle ScholarPubMed
Trujillo, AJ, Capellas, M, Buffa, M, Royo, C, Gervilla, R, Felipe, X, Sendra, E, Saldo, J, Ferragut, V & Guamis, B 2000 Application of high pressure treatment for cheese production. Food Research Internationa 33(3–4) 311–316CrossRefGoogle Scholar
Van Holde, KE, Johnson, WC & Ho, PS 1998 Principles of Physical Biochemistry, pp. 195–198. New York: Prentice HallGoogle Scholar
Yang, J, Dunker, AK, Powers, JR, Clark, S & Swanson, BG 2001 β-Lactoglobulin molten globule induced by high pressure. Journal of Agricultural and Food Chemistry 49(7) 3236–3243CrossRefGoogle ScholarPubMed