Effect of dynamic high pressure on whey protein aggregation: A comparison with the effect of continuous short-time thermal treatments

Food Hydrocolloids

Volumn 22, Issue 6, 2008, Pages 1014-1032

  Grácia Juliá, Alvar ^a   René, Malika ^a   Cortés Muñoz, Marianela ^a   Picart, Laëtitia ^a   López Pedemonte, Tomás ^a   Chevalier, Dominique ^a   Dumay, Eliane ^a  

^a UMR IATE   (France)

Author keywords

Dynamic high pressure; Novel technologies; Photon correlation spectroscopy; Protein aggregation; Ultra high pressure homogenisation; Whey proteins

Indexed keywords

AGGLOMERATION; AGGREGATES; ATMOSPHERIC PRESSURE; ATOMIC FORCE MICROSCOPY; DYNAMICS; ELECTROPHORESIS; GELATION; HIGH PRESSURE EFFECTS; HYDROPHOBICITY; PHOTON CORRELATION SPECTROSCOPY; PHOTONS;

DYNAMIC HIGH PRESSURE; HIGH PRESSURE; HOMOGENIZERS; NOVEL TECHNOLOGY; PHOTON-CORRELATION SPECTROSCOPY; PRESSURE VALVES; PROTEIN AGGREGATION; ULTRA-HIGH-PRESSURE HOMOGENIZATION; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

PROTEINS;

EID: 40749088430     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2007.05.017     Document Type: Article

References (73)

1. Bouaouina H., Desrumaux A., Loisel C., and Legrand J. Functional properties of whey proteins as affected by dynamic high-pressure treatment. International Dairy Journal 16 (2006) 275-284
2. Boulet M., Britten M., and Lamarche F. Voluminosity of some food proteins in aqueous dispersions at various pH and ionic strengths. Food Hydrocolloids 12 (1998) 433-441
3. Brinez W.J., Roig-Sagues A.X., Herrero M.M.H., and Lopez B.G. Inactivation of Listeria innocua in milk and orange juice by ultrahigh-pressure homogenization. Journal of Food Protection 69 (2006) 86-92
4. Cairoli S., Iametti S., and Bonomi F. Reversible and irreversible modifications of β-lactoglobulin upon exposure to heat. Journal of Protein Chemistry 13 (1994) 347-354
5. Cheftel J.C., and Dumay E. Effects on high pressure on dairy proteins: A review. In: Hayashi R., and Balny C. (Eds). High-pressure bioscience and biotechnology (1996), Elsevier, Amsterdam 299-308
6. Croguennec T., Bouhallab S., Mollé D., O'Kennedy B.T., and Mehra R. Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin. Biochemical and Biophysical Research Communications 301 (2003) 465-471
7. Croguennec T., O'Kennedy B.T., and Mehra R. Heat-induced denaturation/aggregation of β-lactoglobulin A and B: Kinetics of the first intermediates formed. International Dairy Journal 14 (2004) 399-409
8. Dalgleish D.G., Senaratne V., and François S. Interactions between α-lactalbumin and β-lactoglobulin in the early stages of heat denaturation. Journal of Agricultural and Food Chemistry 45 (1997) 3459-3464
9. Datta N., Hayes M.G., Deeth H.C., and Kelly A.L. Significance of frictional heating for effects of high pressure homogenisation on milk. Journal of Dairy Research 72 (2005) 393-399
10. De la Fuente M.A., Hemar Y., Tamehana M., Munro P.A., and Singh H. Process-induced changes in whey proteins during the manufacture of whey protein concentrates. International Dairy Journal 12 (2002) 361-369
11. De la Fuente M.A., Singh H., and Hemar Y. Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins. Trends in Food Science and Technology 13 (2002) 262-274
12. De Wit J.N. Thermal stability and functionality of whey proteins. Journal of Dairy Science 73 (1990) 3602-3612
13. De Wit J.N. Nutritional and functional characteristics of whey proteins in food products. Journal of Dairy Science 81 (1998) 597-608
14. Diels A.M.J., Callewaert L., Wuytack E.Y., Masschalch B., and Michiels C.W. Inactivation of Escherichia coli by high-pressure homogenisation is influenced by fluid viscosity but not by water activity and product composition. International Journal of Food Microbiology 101 (2005) 281-291
15. Diels A.M.J., De Taeye J., and Michiels C.W. Sensitisation of Escherichia coli to anti-microbial pepetides and enzymes by high-pressure homogenisation. International Journal of Food Microbiology 105 (2005) 165-175
16. Dumay E., Kalichevsky M., and Cheftel J.C. Characteristics of pressure-induced gels of a β-lactoglobulin isolate at various times after pressure release. Food Science and Technology (LWT) 31 (1998) 10-19
17. Durand D., Gimel J.C., and Nicolai T. Aggregation, gelation and phase separation of heat denatured globular proteins. Physica A 304 (2002) 253-265
18. Finsy R., and De Jaeger N. Particle sizing by photon correlation spectroscopy. Part II: Average values. Particle and Particle Systems Characterization 8 (1991) 187-193
19. Floury J., Desrumaux A., Axelos M.A.V., and Legrand J. Degradation of methylcellulose during ultra-high pressure homogenisation. Food Hydrocolloids 16 (2002) 47-53
20. Floury J., Bellettre J., Legrand J., and Desrumaux A. Analysis of a new type of high pressure homogeniser. A study of the flow pattern. Chemical Engineering Science 59 (2004) 843-853
21. Floury J., Desrumaux A., and Lardières J. Effect of high-pressure homogenization on droplet size distributions and rheological properties of model oil-in-water emulsions. Innovative Food Science & Emerging Technologies 1 (2000) 127-134
22. Funtenberger S., Dumay E., and Cheftel J.C. Pressure-induced aggregation of β-lactoglobulin in pH 7.0 buffers. Food Science and Technology (LWT) 28 (1995) 410-418
23. Funtenberger S., Dumay E., and Cheftel J.C. High pressure promotes β-lactoglobulin aggregation through SH/S-S interchange reactions. Journal of Agricultural and Food Chemistry 45 (1997) 912-921
24. Galani D., and Apenten R.K.O. Heat-induced denaturation and aggregation of β-lactoglobulin: Kinetics of formation of hydrophobic and disulphide-linked aggregates. International Journal of Food Science and Technology 34 (1999) 467-476
25. Gimel J.C., Durand D., and Nicolai T. Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins. Molecules 27 (1994) 583-589
26. Hambling S.G., McAlpine A.S., and Sawyer L. β-lactoglobulin. In: Fox P.F. (Ed). Advanced dairy chemistry--1: Proteins (1992), Elsevier Science Publishers Ltd, London 141-190
27. Havea P., Singh H., and Creamer L.K. Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment. Journal of Dairy Research 68 (2001) 483-497
28. Hayes M.G., Fox P.F., and Kelly A.L. Potential applications of high pressure homogenisation in processing of liquid milk. Journal of Dairy Research 72 (2005) 25-33
29. Hayes M.G., and Kelly A.L. High pressure homogenization of raw whole milk. (a) Effects on fat globule size and other properties. Journal of Dairy Research 70 (2003) 297-305
30. Hinrichs J., and Rademacher B. Kinetics of combined thermal and pressure-induced whey protein denaturation in bovine skim milk. International Dairy Journal 15 (2005) 315-323
31. Hoffmann M.A.M., Roefs S.P.F.M., Verheul M., van Mil P.J.J.M., and de Kruif K.G. Aggregation of β-lactoglobulin studied by in situ light scattering. Journal of Dairy Research 63 (1996) 423-440
32. Hoffmann M.A.M., and van Mil P.J.J.M. Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulphide bonds. Journal of Agricultural and Food Chemistry 45 (1997) 2942-2948
33. Huffman L.M., and Harper W.J. Maximizing the value of milk through separation technologies. Journal of Dairy Science 82 (1999) 2238-2244
34. Huppertz T., Fox P.F., and Kelly A.L. High pressure-induced denaturation of α-lactalbumin and β-lactoglobulin in bovine milk and whey: A possible mechanism. Journal of Dairy Research 71 (2004) 489-495
35. Huppertz T., Kelly A.L., and Fox P.F. Effects of high pressure on constituents and properties of milk. International Dairy Journal 12 (2002) 561-572
36. Iametti S., De Gregori B., Vecchio G., and Bonomi F. Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. European Journal of Biochemistry 237 (1996) 106-112
37. Ikeda S., and Morris V.J. Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy. Biomacromolecules 3 (2002) 382-389
38. Kataoka M., Kuwajima K., Tokunaga F., and Goto Y. Structural characterization of the molten globule of α-lactalbumin by solution X-ray scattering. Protein Science 6 (1997) 422-430
39. Kazmierski M., and Corredig M. Characterization of soluble aggregates from whey protein isolate. Food Hydrocolloids 17 (2003) 685-692
40. Keck C.M., and Muller H.R. Drug nanocrystals of poorly soluble drugs produced by high pressure homogenisation. European Journal of Pharmaceutics and Biopharmaceutics 62 (2006) 3-16
41. Laligant A., Dumay E., Valencia C.C., Cuq J.L., and Cheftel J.C. Surface hydrophobicity and aggregation of β-lactoglobulin heated near neutral pH. Journal of Agricultural and Food Chemistry 39 (1991) 2147-2151
42. Le Bon C., Nicolai T., and Durand D. Growth and structure of aggregates of heat-denatured β-lactoglobulin. International Journal of Food Science and Technology 34 (1999) 451-465
43. Livney Y.D., Corredig M., and Dalgleish D.G. Influence of thermal processing on the properties of dairy colloids. Current Opinion in Colloid and Interface Science 8 (2003) 359-364
44. López-Fandiño R. High pressure-induced changes in milk proteins and possible applications in dairy technology. International Dairy Journal 16 (2006) 1119-1131
45. Manderson G.A., Hardman M.J., and Creamer L.K. Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A, B, and C. Journal of Agricultural and Food Chemistry 46 (1998) 5052-5061
46. McKenzie H.A. β-lactoglobulin. In: McKenzie H.A. (Ed). Milk proteins: Chemistry and molecular biology Vol. 2 (1971), Academic Press, New York 257-330
47. Moroni O., Jean J., Autret J., and Fliss I. Inactivation of lactococcal bacteriophages in liquid media using dynamic high pressure. International Dairy Journal 12 (2002) 907-913
48. Mulvihill D.M., and Donovan M. Whey proteins and their thermal denaturation-A review. Irish Journal of Food Science and Technology 11 (1987) 43-75
49. Oldfield D.J., Singh H., Taylor M.W., and Pearce K.N. Kinetics of denaturation and aggregation of whey proteins in skim milk heated in an ultra-high temperature (UHT) pilot plant. International Dairy Journal 8 (1998) 311-318
50. Oldfield D.J., Taylor M.W., and Singh H. Effects of preheating and other process parameters on whey protein reactions during skim milk powder manufacture. International Dairy Journal 15 (2005) 501-511
51. Panick G., Malessa R., and Winter R. Differences between the pressure- and temperature-induced denaturation and aggregation of β-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering. Biochemistry 38 (1999) 6512-6519
52. Paquin, P., Lacasse, J., Subirade, M., & Turgeon, S. (2003). Continuous process of dynamic high-pressure homogenization for the denaturation of proteins. US Patent 6,511,695 B1.
53. Patel H.A., Singh H., Havea P., Considine T., and Creamer L.K. Pressure-induced unfolding and aggregation of the proteins in whey protein concentrate solutions. Journal of Agricultural and Food Chemistry 53 (2005) 9590-9601
54. Pessen H., Purcell J.M., and Farrell H.M. Proton relaxation rates of water in dilute solutions of β-lactoglobulin. Determination of cross relaxation and correlation with structural changes by the use of two genetic variants of a self-associating globular protein. Biochimica et Biophysica Acta 828 (1985) 1-12
55. Picart L., Thiebaud M., René M., Guiraud J.P., Cheftel J.C., and Dumay E. Effects of high pressure homogenisation of raw bovine milk on alkaline phosphatase and microbial inactivation. A comparison with continuous short-time thermal treatments. Journal of Dairy Research 73 (2006) 454-463
56. Prabakaran S., and Damodaran S. Thermal unfolding of β-lactoglobulin: characterization of initial unfolding events responsible for heat-induced aggregation. Journal of Agricultural and Food Chemistry 45 (1997) 4303-4308
57. Qi X.L., Brownlow S., Holt C., and Sellers P. Thermal denaturation of β-lactoglobulin: Effect of protein concentration at pH 6.75 and 8.05. Biochimica et Biophysica Acta 1248 (1995) 43-49
58. Regnault S., Thiebaud M., Dumay E., and Cheftel J.C. Pressurisation of raw skim milk and of a dispersion of phosphocaseinate at 9 °C or 20 °C: Effects on casein miscelle distribution. International Dairy Journal 14 (2004) 55-68
59. Roefs P.F.M., and de Kruif K.G. A model for the denaturation and aggregation of β-lactoglobulin. European Journal of Biochemistry 226 (1994) 883-889
60. Sandra S., and Dalgleish D.G. Effects of ultra-high-pressure homogenization and heating on structural properties of casein micelles in reconstituted skim milk powder. International Dairy Journal 15 (2005) 1095-1104
61. Sawyer W.H. Heat induced denaturation of bovine β-lactoglobulins and relevance of disulfide aggregation. Journal of Dairy Science 51 (1968) 323-329
62. Sharma M., Haque Z.U., and Wilson W. Association tendency of β-lactoglo-bulin AB purified by gel permeation chromatography as determined by light scattering under quiescent conditions. Food Hydrocolloids 10 (1996) 323-328
63. Schokker E.P., Singh H., and Creamer L.K. Heat-induced aggregation of β-lactoglobulin A and B with α-lactalbumin. International Dairy Journal 10 (2000) 843-853
64. Schokker E.P., Singh H., Pinder D.N., Norris G.E., and Creamer L.K. Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH. International Dairy Journal 9 (1999) 791-800
65. Shimada K., and Cheftel J.C. Texture characteristics, protein solubility, and sulfhydryl group/disulfide bond contents of heat-induced gels of whey protein isolate. Journal of Agricultural and Food Chemistry 36 (1988) 1018-1025
66. Shimada K., and Cheftel J.C. Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate. Journal of Agricultural and Food Chemistry 37 (1989) 161-168
67. Stevenson M.J., and Chen X.D. Visualization of the flow patterns in a high-pressure homogenizing valve using a CFD package. Journal of Food Engineering 33 (1997) 151-167
68. Subirade M., Loupil F., Allain A.F., and Paquin P. Effect of dynamic high pressure on the secondary structure of β-lactoglobulin and on its conformational properties as determined by Fourier transform infrared spectroscopy. International Dairy Journal 8 (1998) 135-140
69. Tanaka N., and Kunugi S. Effect of pressure on the deuterium exchange reaction of α-lactalbumin and β-lactoglobulin. International Journal of Biological Macromolecules 18 (1996) 33-39
70. Thiebaud M., Dumay E., Picart L., Guiraud J.P., and Cheftel J.C. High pressure homogenisation of raw bovine milk. Effects on fat globule size distribution and microbial inactivation. International Dairy Journal 13 (2003) 427-439
71. Trujillo A.J., Capellas M., Saldo J., Gervilla R., and Guamis B. Applications of high-hydrostatic pressure on milk and dairy products: A review. Innovative Food Science and Emerging Technologies 3 (2002) 295-307
72. Vachon J.F., Kheadr E.E., Giasson J., Paquin P., and Fliss I. Inactivation of foodborne pathogens in milk using dynamic high pressure. Journal of Food Protection 65 (2002) 345-352
73. Verheul M., Roefs S.P.F.M., and de Kruif K.G. Kinetics of heat-induced aggregation of β-lactoglobulin. Journal of Agricultural and Food Chemistry 46 (1998) 896-903