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Regulation of milk protein solubility by a whey-derived proline-rich peptide product

Published online by Cambridge University Press:  23 April 2013

Sophie N. Selby-Pham ,
Kate Howell ,
Hema Jegasothy ,
Paul Sheean ,
Tanoj Singh ,
Cheryl Taylor  and
Louise E. Bennett
Sophie N. Selby-Pham
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia Department of Agriculture and Food Systems, Melbourne School of Land and Environment, University of Melbourne, Parkville, Victoria, 3051, Australia
Kate Howell
Affiliation:
Department of Agriculture and Food Systems, Melbourne School of Land and Environment, University of Melbourne, Parkville, Victoria, 3051, Australia
Hema Jegasothy
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia
Paul Sheean
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia
Tanoj Singh
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia
Cheryl Taylor
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia
Louise E. Bennett*
Affiliation:
CSIRO Animal, Food and Health Sciences, 671 Sneydes Road, Werribee, Victoria, 3030, Australia
*
*For correspondence; e-mail: [email protected]
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Abstract

The effects of a bovine whey peptide product enriched in proline (wPRP) on the solubility of milk proteins were tested under ambient conditions or following heat treatment at 75 and 100 °C, for 1 and 15 min, followed by post-incubation storage at either ambient temperature or 4 °C for up to 7 d. wPRP promoted solubilisation of milk proteins in a concentration-dependent manner without heat treatment and also after heat treatment at 75 and 100 °C, and the effect was enhanced after storage under either ambient or refrigerated storage conditions. Interactions of wPRP and milk proteins were monitored by particle size analysis and tryptic digestion and specifically linked with solubilisation of αS1 casein (αS1-Cn), which supported observed changes in milk protein solubility. The results suggested that wPRP preferably prevented or reversed physical versus covalent protein aggregation, with the relaxation of hydrophobic interactions at 4 °C providing an additive effect. This application of wPRP represents a novel approach to stabilisation of dairy proteins following thermal processing with industrial usefulness yet to be explored.

Keywords

Protein aggregationproline-rich peptidehydrophobic interaction
Type
Research Article
Information
Journal of Dairy Research , Volume 80 , Issue 3 , August 2013 , pp. 291 - 299
Copyright
Copyright © Proprietors of Journal of Dairy Research 2013 

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References

Anand, K & Ward, G 2005 Method of producting heat stable whey protein and products made there from. United States: US Patents Application No. US 2005/0163887 A1Google Scholar
Anema, SG 2008 The whey proteins in milk: thermal denaturation, physical interactions and effects on the functional properties of milk. In Milk Proteins: From Expression to Food, pp. 239–273 (Eds Thompson, A, Boland, M & Singh, H). Amsterdam, Boston: Academic Press-ElsevierGoogle Scholar
Anema, SG & Li, YM 2003 Association of denatured whey proteins with casein micelles in heated reconstituted skim milk and its effect on casein micelle size. Journal of Dairy Research 70 73–83CrossRefGoogle ScholarPubMed
Augustin, M-A & Clarke, PT 1990 Effects of added salts on the heat stability of recombined concentrated milk. Journal of Dairy Research 57 213–226Google Scholar
Baldwin, RL 1986 Temperature dependence of the hydrophobic interaction in protein folding. Proceedings of the National Academy of Sciences 83 8069–8072Google Scholar
Bennett, L, Williams, R, Ecroyd, H, Liu, YQ, Sudharmarajan, S & Carver, J 2009 Protective interactions of dairy peptides with fibril structures and relevance to Alzheimer's disease. Australian Journal of Dairy Technology 64 117–121Google Scholar
Bharadwaj, P, Head, R, Martins, R, Raussens, V, Sarroukh, R, Jegasothy, H, Waddington, L & Bennett, L 2012 Modulation of amyloid -b-1-42 structure and toxicity by proline-rich whey peptides. Food and FunctionGoogle Scholar
Boldogh, I, Aguilera-Aguirre, L, Bacsi, A, Choudhury, BK, Saavedra-Molina, A & Kruzel, M 2008 Colostrinin decreases hypersensitivity and allergic responses to common allergens. International Archives of Allergy and Immunology 146 298–306CrossRefGoogle ScholarPubMed
Chandrapala, J, Augustin, MA, McKinnon, I & Udabage, P 2010 Effects of pH, calcium-complexing agents and milk solids concentration on formation of soluble protein aggregates in heated reconstituted skim milk. International Dairy Journal 20 777–784CrossRefGoogle Scholar
Datta, N & Deeth, HC 2001 Age gelation of UHT milk‚ a review. Food and Bioproducts Processing 79 197–210CrossRefGoogle Scholar
de Rham, O & Chanton, S 1984 Role of ionic environment in insolubilization of whey protein during heat treatment of whey products. Journal of Dairy Science 67 939–949Google Scholar
Donato, L & Guyomarch, F 2009 Formation and properties of the whey protein/kappa-casein complexes in heated skim milk – A review. Dairy Science and Technology (EDP Sciences) 89 3–29Google Scholar
Foegeding, EA, Davis, JP, Doucet, D & McGuffey, MK 2002 Advances in modifying and understanding whey protein functionality. Trends in Food Science and Technology 13 151–159Google Scholar
Gao, H, Havea, P & Singh, H 2008 Whey product and process. USA: US Patents Application No. US 2008/0305235 A1Google Scholar
Guyomarc'h, F, Law, AJR & Dalgleish, DG 2003 Formation of soluble and micelle-bound protein aggregates in heated milk. Journal of Agricultural and Food Chemistry 51 4652–4660Google Scholar
Havn, SS, Ipsen, R, Nielsen, PM & Lilbaek, HM 2006 Improving the foaming properties and heat stability of whey protein concentrates by phospholipase treatment. Milchwissenschaft-Milk Science International 61 188–191Google Scholar
Janusz, M & Zablocka, A 2010 Colostral proline-rich polypeptides – immunoregulatory properties and prospects of therapeutic use in Alzheimers disease. Current Alzheimer Research 7 323–333CrossRefGoogle Scholar
Janusz, M, Staroscik, K, Zimecki, M, Wieczorek, Z & Lisowski, J 1981 Chemical and physical characterisation of a proline-rich polypeptide from sheep colostrum. Biochemical Journal 199 9–15CrossRefGoogle ScholarPubMed
Kanning, M, Casella, M & Olieman, C 1993 Milk and soy proteins analysis using capillary zone electrophoresis. Liquid Chromatography-Gas Chromatography International 6 701–704Google Scholar
Kay, BK, Williamson, MP & Sudol, M 2000 The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB Journal 14 231–241Google Scholar
Kulmyrzaev, A, Bryant, C & McClements, DJ 2000 Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins. Journal of Agricultural and Food Chemistry 48 1593–1597Google Scholar
Kumosinski, TF, Brown, EM & Farrell, HM 1993 Three – dimensional molecular modeling of bovine caseins: a refined, energy-minimized kappa-casein structure. Journal of Dairy Science 76 2507–2520CrossRefGoogle ScholarPubMed
Laleye, LC, Jobe, B & Wasesa, AAH 2008 Comparative study on heat stability and functionality of camel and bovine milk whey proteins. Journal of Dairy Science 91 4527–4534Google Scholar
Le, TT, El-Bakry, M, Neirynck, N, Bogus, M, Hoa, HD & Van der Meeren, P 2007 Hydrophilic lecithins protect milk proteins against heat-induced aggregation. Colloids and Surfaces B: Biointerfaces 60 167–173Google Scholar
Le, TT, Sabatino, P, Heyman, B, Kasinos, M, Dinh, HH, Dewettinck, K, Martins, J & Van der Meeren, P 2011 Improved heat stability by whey protein-surfactant interaction. Food Hydrocolloids 25 594–603Google Scholar
McCrae, CH 1999 Heat stability of milk emulsions: phospholipid-protein interactions. International Dairy Journal 9 227–231Google Scholar
McCrae, CH & Muir, DD 1992 Heat stability of recombined milk: influence of lecithins on the heat coagulation time-pH profile. Journal of Dairy Research 59 177–185Google Scholar
McMahon, DJ & Brown, RJ 1984 Composition, structure, and integrity of casein micelles: a review. Journal of Dairy Science 67 499–512Google Scholar
Morand, M, Guyomarc'h, F & Famelart, MH 2011 How to tailor heat-induced whey protein/kappa-casein complexes as a means to investigate the acid gelation of milk-a review. Dairy Science and Technology 91 97–126CrossRefGoogle Scholar
Muir, DD & Sweetsur, AWM 1977 Effect of urea on heat coagulation of caseinate complex in skim milk. Journal of Dairy Research 44 249–257CrossRefGoogle Scholar
Muir, DD & Sweetsur, AWM 1978 The effect of concentration on the heat stability of skim-milk. Journal of Dairy Research 45 37–45Google Scholar
O'Connell, JE & Fox, PF 1999a Effect of extracts of oak (Quercus petraea) bark, oak leaves, aloe vera (Curacao aloe), coconut shell and wine on the colloidal stability of milk and concentrated milk. Food Chemistry 66 93–96Google Scholar
O'Connell, JE & Fox, PF 1999b Effects of phenolic compounds on the heat stability of milk and concentrated milk. Journal of Dairy Research 66 399–407Google Scholar
O'Connell, JE & Fox, PF 2003 Heat stability of milk. In Encyclopedia of Dairy Sciences, pp. 1321–1326 (Eds Roginski, H, Fuquay, JW & Fox, PF). New York, Amsterdam: Academic PressGoogle Scholar
Parris, N 1993 Aggregation of whey proteins in heated sweet whey. Journal of Agricultural and Food Chemistry 41 460–464CrossRefGoogle Scholar
Parris, N, Hollar, CM, Hsieh, A & Cockley, KD 1997 Thermal stability of whey protein concentrate mixtures: aggregate formation. Journal of Dairy Science 80 19–28Google Scholar
Raikos, V 2010 Effect of heat treatment on milk protein functionality at emulsion interfaces. A review. Food Hydrocolloids 24 259–265CrossRefGoogle Scholar
Relkin, P & Mulvihill, DM 1996 Thermal unfolding of β-lactoglobulin, α-lactalbumin, and bovine serum albumin. A thermodynamic approach. Critical Reviews in Food Science and Nutrition 36 565–601Google Scholar
Schuster, D, Rajendran, A, Hui, SW, Nicotera, T, Srikrishnan, T & Kruzel, ML 2005 Protective effect of colostrinin on neuroblastoma cell survival is due to reduced aggregation of beta-amyloid. Neuropeptides 39 419–426Google Scholar
Singh, H 2004 Heat stability of milk. International Journal of Dairy Technology 57 111–119CrossRefGoogle Scholar
Thorn, DC, Meehan, S, Sunde, M, Rekas, A, Gras, SL, MacPhee, CE, Dobson, CM, Wilson, MR & Carver, JA 2005 Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alpha(s-) and beta-casein. Biochemistry 44 17027–17036Google Scholar
Thorn, DC, Ecroyd, H, Sunde, M, Poon, S & Carver, JA 2008 Amyloid fibril formation by bovine milk alpha(s2)-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha(s1)-casein. Biochemistry 47 3926–3936Google Scholar
Thorn, DC, Ecroyd, H & Carver, JA 2009 The two-faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity. Australian Journal of Dairy Technology 64 34–40Google Scholar
Williams, RPW, D'Ath, L & Augustin, MA 2005 Production of calcium-fortified milk powders using soluble calcium salts. Lait 85 369–381CrossRefGoogle Scholar
Williamson, MP 1994 The structure and function of proline-rich regions in proteins. Biochemical journal 297(Pt 2) 249Google Scholar
Xu, RJ 2001 Light scattering. In Particle Charcterisation: Light Scattering Methods, pp. 56–100Dordrecht, The Netherlands: Kluwer Academic PublishersGoogle Scholar
Ye, A 2008 Complexation between milk proteins and polysaccharides via electrostatic interaction: principles and applications‚ A review. International Journal of Food Science and Technology 43 406–415Google Scholar
Yong, YH & Forgeding, EA 2010 Caseins: utilizing molecular chaperone properties to control protein aggregation in foods. Journal of Agricultural and Food Chemistry 58 685–693Google Scholar
Yuksel, Z & Erdem, YK 2005 The influence of main milk components on the hydrophobic interactions of milk protein system in the course of heat treatment. Journal of Food Engineering 67 301–308Google Scholar
Zimecki, M 2008 A proline-rich polypeptide from ovine colostrum: colostrinin with immunomodulatory activity. In Bioactive Components of Milk, Vol. 606, pp. 241–250. Berlin: Springer-Verlag BerlinGoogle Scholar