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Characterization of lactoferrin oil-in-water emulsions and their stability in recombined milk

Published online by Cambridge University Press:  08 September 2010

Acero-Lopez A ,
Schell P ,
Corredig M  and
Alexander M
Acero-Lopez A
Affiliation:
Food Science Department, University of Guelph, Guelph, Ontario
Schell P
Affiliation:
Food Science Department, University of Guelph, Guelph, Ontario
Corredig M
Affiliation:
Food Science Department, University of Guelph, Guelph, Ontario
Alexander M*
Affiliation:
Food Science Department, University of Guelph, Guelph, Ontario
*
*For correspondence; e-mail: maalexan@uoguelph.ca
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Abstract

Emulsions were prepared with 20% soy oil and different concentrations of lactoferrin, and tested at pH values from 3 to 7·5. The stability of the emulsions decreased as the pH got closer to the isoelectric point of the protein. A concentration of 1% lactoferrin was determined to be sufficient to provide full coverage of the emulsion droplets. Lactoferrin-stabilized emulsions were then prepared in water at pH 6·6 and their behaviour when added to reconstituted milk was studied. It was observed that lactoferrin emulsions were stable when reconstituted in milk, but they showed aggregation when diluted in milk serum alone. The destabilization was caused by shielding of the charges on the surface of the oil droplets. Stabilization in milk occurred due to interactions at the interface with other soluble proteins. In fact, when β-lactoglobulin or sodium caseinate were added to the serum, stability of the emulsion droplets was restored, indicating that these proteins were able to adsorb at the interface and aid in the stabilization. Since ζ-potential measurements did not show significant overall charge on the emulsion droplets, this suggests that the stabilization forces are not only electrostatic in nature, but that there are other mechanisms at play.

Keywords

lactoferrinoil in water emulsionsrecombined milkcompetitive displacementdiffusing wave spectroscopy
Type
Research Article
Information
Journal of Dairy Research , Volume 77 , Issue 4 , November 2010 , pp. 445 - 451
Copyright
Copyright © Proprietors of Journal of Dairy Research 2010

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References

Andrews, AT, Taylor, MD & Owen, AJ 1985 Rapid analysis of bovine milk proteins by fast protein liquid chromatography. Journal of Chromatography A 348 177–185CrossRefGoogle ScholarPubMed
Baker, EN, Baker, HM & Kidd, RD 2002 Lactoferrin and transferrin: Functional variations on a common structural framework. Biochemistry & Cell Biology 80(1) 27–34CrossRefGoogle ScholarPubMed
Huang, S-W, Satue-Gracia, MT, Frankel, EN & German, JB 1999 Effect of Lactoferrin on Oxidative Stability of Corn Oil Emulsions and Liposomes. Journal of Agricultural and Food Chemistry 47(4) 1356–1361CrossRefGoogle ScholarPubMed
Lönnerdaal, B 2003 Advanced Dairy Chemistry. New York: Kluwer Academic/PlenumGoogle Scholar
Lönnerdaal, B & Iyer, S 1995 Lactoferrin: Molecular Structure and Biological Function. Annual Review of Nutrition 15(1) 93–110CrossRefGoogle Scholar
McClements, DJ 2005 Characterization of emulsion properties. In Food emulsions: principles, practices, and techniques, pp. 508–510. (Ed. Clydesdale, F.) Boca Raton: CRC Press 2nd EditionGoogle Scholar
Medina, I, Tombo, I, Satue-Gracia, MT, German, JB & Frankel, EN 2002 Effects of Natural Phenolic Compounds on the Antioxidant Activity of Lactoferrin in Liposomes and Oil-in-Water Emulsions. Journal of Agricultural and Food Chemistry 50(8) 2392–2399CrossRefGoogle ScholarPubMed
Sarkar, A, Goh, KKT & Singh, H 2009 Colloidal stability and interactions of milk-protein-stabilized emulsions in an artificial saliva. Food Hydrocolloids 23(5) 1270–1278CrossRefGoogle Scholar
Shimazaki, K-I, Kawaguchi, A, Sato, T, Ueda, Y, Tomimura, T & Shimamura, S 1993 Analysis of human and bovine milk lactoferrins by rotofor and chromatofocusing. International Journal of Biochemistry 25(11) 1653–1658CrossRefGoogle ScholarPubMed
Sørensen, M & Sørensen, SPL 1939 The proteins in whey. Compt. Rendus Laboratoire Carlsberg 23 55–99Google Scholar
Tomita, M, Wakabayashi, H, Yamauchi, K, Teraguchi, S & Hayasawa, H 2002 Bovine lactoferrin and lactoferricin derived from milk: production and applications. Biochemistry & Cell Biology 80(1) 109–112CrossRefGoogle ScholarPubMed
Wahlgren, MC, Arnebrant, T & Paulsson, MA 1993 The adsorption from solutions of [beta]-lactoglobulin mixed with lactoferrin or lysozyme onto silica and methylated silica surfaces. Journal of Colloid and Interface Science 158(1) 46–53CrossRefGoogle Scholar
Weitz, DA & Pine, DJ 1993 Dynamic light scattering: The method and some applications. Oxford, UK: Oxford University PressGoogle Scholar
Ye, A & Singh, H 2006 Adsorption behaviour of lactoferrin in oil-in-water emulsions as influenced by interactions with [beta]-lactoglobulin. Journal of Colloid and Interface Science 295(1) 249–254CrossRefGoogle ScholarPubMed
Ye, A & Singh, H 2007 Formation of multilayers at the interface of oil-in-water emulsion via interactions between lactoferrin and β-lactoglobulin. Food Biophysics 2 125–132CrossRefGoogle Scholar