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Effect of homogenisation in formation of thermally induced aggregates in a non- and low- fat milk model system with microparticulated whey proteins

Published online by Cambridge University Press:  19 May 2017

Isabel Celigueta Torres ,
Gema Nieto ,
Tommy Nylander ,
Adam Cohen Simonsen ,
Alexander Tolkach  and
Richard Ipsen
Isabel Celigueta Torres*
Affiliation:
Department of Food Science, Faculty of Life Sciences, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C
Gema Nieto
Affiliation:
Department of Food Science, Faculty of Life Sciences, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C
Tommy Nylander
Affiliation:
Lund University, Getingevägen 60, Box 124 SE-221 00, Lund, Sweden
Adam Cohen Simonsen
Affiliation:
Department of Physics and Chemistry, Center for Biomembrane Physics, University of Southern Denmark, Campusvej 55, DK-5230 Odense M
Alexander Tolkach
Affiliation:
Bayerische Milchindustrie eG, Klötzlmüllerstrasse 140, 84034 Landshut, Germany
Richard Ipsen
Affiliation:
Department of Food Science, Faculty of Life Sciences, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C
*
*For correspondence; e-mail: Isabel.CeliguetaTorres@rdyo.nestle.com
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Abstract

The objective of the research presented in this paper was to investigate how different characteristics of whey protein microparticles (MWP) added to milk as fat replacers influence intermolecular interactions occurring with other milk proteins during homogenisation and heating. These interactions are responsible for the formation of heat-induced aggregates that influence the texture and sensory characteristics of the final product. The formation of heat-induced complexes was studied in non- and low-fat milk model systems, where microparticulated whey protein (MWP) was used as fat replacer. Five MWP types with different particle characteristics were utilised and three heat treatments used: 85 °C for 15 min, 90 °C for 5 min and 95 °C for 2 min. Surface characteristics of the protein aggregates were expressed as the number of available thiol groups and the surface net charge. Intermolecular interactions involved in the formation of protein aggregates were studied by polyacrylamide gel electrophoresis and the final complexes visualised by darkfield microscopy. Homogenisation of non-fat milk systems led to partial adsorption of caseins onto microparticles, independently of the type of microparticle. On the contrary, homogenisation of low-fat milk resulted in preferential adsorption of caseins onto fat globules, rather than onto microparticles. Further heating of the milk, led to the formation of heat induced complexes with different sizes and characteristics depending on the type of MWP and the presence or not of fat. The results highlight the importance of controlling homogenisation and heat processing in yoghurt manufacture in order to induce desired changes in the surface reactivity of the microparticles and thereby promote effective protein interactions.

Keywords

Microparticulated whey proteinhomogenisationheatingaggregationprotein interactions
Type
Research Article
Information
Journal of Dairy Research , Volume 84 , Issue 2 , May 2017 , pp. 229 - 238
Copyright
Copyright © Proprietors of Journal of Dairy Research 2017 

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Footnotes

†

Current address: Nestlé Product Technology Centre, PO Box 204, Haxby Road, YO91 1XY York, UK.

References

Alexander, M & Dalgleish, DG 2005 Interactions between denatured milk serum proteins and casein micelles studied by diffusing wave spectroscopy. Langmuir 21 11380–11386 Google 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 73–83 Google Scholar
Anema, SG & McKenna, AB 1996 Reaction Kinetics of Thermal Denaturation of Whey Proteins in Heated Reconstituted Whole Milk. Journal of Agricultural and Food Chemistry 44 422–428 CrossRefGoogle Scholar
Czerwenka, C, Maier, I, Pittner, F & Lindner, W 2006 Investigation of the lactosylation of whey proteins by liquid chromatography-mass spectrometry. Journal of Agricultural and Food Chemistry 54 8874–8882 CrossRefGoogle ScholarPubMed
Dannenberg, F & Kessler, HG 1988 Reaction-Kinetics of the Denaturation of Whey Proteins in Milk. Journal of Food Science 53 258–263 Google Scholar
de Kruif, CG 1999 Casein micelle interactions. International Dairy Journal 9 183–188 Google Scholar
Famelart, MH, Tomazewski, J, Piot, M & Pezennec, S 2004 Comprehensive study of acid gelation of heated milk with model protein systems. International Dairy Journal 14 313–321 Google Scholar
Gaucheron, F 2005 The minerals of milk. Reproduction Nutrition and Development 45 473–483 Google 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 4652–4660 CrossRefGoogle ScholarPubMed
Holt, C, Davies, DT & Law, AJR 1986 Effects of colloidal calcium-phosphate content and free calcium-ion concentration in the milk serum on the dissociation of bovine casein micelles. Journal of Dairy Research 53 557–572 Google Scholar
IDF Standard 20B 1993 Determination of Nitrogen Content: Kjeldahl Method. International Dairy Federation, Brussels, Belgium Google Scholar
Jongberg, S, Lund, MN, Waterhouse, AL & Skibsted, LH 2011 4-methylcatechol inhibits protein oxidation in meat but not disulfide formation. Journal of Agricultural and Food Chemistry 59 10329–10335 Google Scholar
Kessler, HG 2002a Heat treatment, processes and effects-microorganisms and conditions of inactivation. In Food and Bio Process Engineering-Dairy Technology, pp. 130–216 (Ed. Kessler, A). Munich, Germany: Verlag A.Kessler Google Scholar
Kessler, HG 2002b Technology of cultured milk products-structure of gels-direct acidification-special milk products and use of hydrocolloids. In Food and Bio Process Engineering-Dairy Technology, 5th edition, pp. 459–492 (Ed. Kessler, A). Munich, Germany: Verlag Google Scholar
Losito, I, Carbonara, T, Monaci, L & Palmisano, F 2007 Evaluation of the thermal history of bovine milk from the lactosylation of whey proteins: an investigation by liquid chromatography-electrospray ionization mass spectrometry. Analytical and Bioanalytical Chemistry 389 2065–2074 Google Scholar
Lucey, JA 2004 Cultured dairy products: an overview of their gelation and texture properties. International Journal of Dairy Technology 57 77–84 CrossRefGoogle Scholar
Michalski, MC, Cariou, R, Michel, F & Garnier, C 2002a Native vs. damaged milk fat globules: membrane properties affect the viscoelasticity of milk gels. Journal of Dairy Science 85 2451–2461 CrossRefGoogle ScholarPubMed
Michalski, MC, Michel, F, Sainmont, D & Briard, V 2002b Apparent zeta-potential as a tool to assess mechanical damages to the milk fat globule membrane. Colloids and Surfaces B: Biointerfaces 23 23–30 Google Scholar
Mulsow, BB, Jacob, M & Henle, T 2009 Studies on the impact of glycation on the denaturation of whey proteins. European Food Research and Technology 228 643–649 Google Scholar
Oldfield, DJ, Taylor, MW & Singh, H 2005 Effect of preheating and other process parameters on whey protein reactions during skim milk powder manufacture. International Dairy Journal 15 501–511 Google Scholar
Relkin, P 1996 Thermal unfolding of beta-lactoglobulin, alpha-lactalbumin, and bovine serum albumin. A thermodynamic approach. Critical Reviews in Food Science and Nutrition 36 565–601 Google Scholar
Sandoval-Castilla, O, Lobato-Calleros, C, Aguirre-Mandujano, E & Vernon-Carter, EJ 2004 Microstructure and texture of yogurt as influenced by fat replacers. International Dairy Journal 14 151–159 Google Scholar
Schokker, EP, Singh, H, Pinder, DN & Creamer, LK 2000 Heat-induced aggregation of beta-lactoglobulin AB at pH 2·5 as influenced by ionic strength and protein concentration. International Dairy Journal 10 233–240 Google Scholar
Spiegel, T 1999 Whey protein aggregation under shear conditions – effects of lactose and heating temperature on aggregate size and structure. International Journal of Food Science and Technology 34 523–531 Google Scholar
Spiegel, T & Huss, M 2002 Whey protein aggregation under shear conditions – effects of pH-value and removal of calcium. International Journal of Food Science and Technology 37 559–568 CrossRefGoogle Scholar
Tolkach, A & Kulozik, U 2005 Fractionation of whey proteins and caseinomacropeptide by means of enzymatic crosslinking and membrane separation techniques. Journal of Food Engineering 67 13–20 Google Scholar
Tuinier, R & de Kruif, CG 2002 Stability of casein micelles in milk. Journal of Chemical Physics 117 1290–1295 Google Scholar
Vasbinder, AJ, Alting, AC & de Kruif, KG 2003 Quantification of heat-induced casein-whey protein interactions in milk and its relation to gelation kinetics. Colloids and Surfaces B-Biointerfaces 31 115–123 CrossRefGoogle Scholar
Vasbinder, AJ, van de Velde, FV & de Kruif, CG 2004 Gelation of casein-whey protein mixtures. Journal of Dairy Science 87 1167–1176 Google Scholar
Zuniga, RN, Tolkach, A, Kulozik, U & Aguilera, JM 2010 Kinetics of formation and physicochemical characterization of thermally-induced beta-lactoglobulin aggregates. Journal of Food Science 75 E261–E268 Google Scholar