Interactions between Milk Proteins and Micronutrients

Milk Proteins: from Expression to Food, Second Edition

Volumn , Issue , 2014, Pages 421-449

  Considine, Thérèse ^a   Flanagan, John ^b,c   Loveday, Simon M ^b  

^a FONTERRA RESEARCH CENTRE   (New Zealand)

^b MASSEY UNIVERSITY   (New Zealand)

^c Givaudan SA   (Switzerland)

Author keywords

biopolymers; casein; co solubility; coacervates; depletion flocculation; emulsion; fatty acid; food processing; interface; Maillard; micronutrient; microstructures; Milk proteins; mineral; phase separation; sugar; surfactant; thermodynamic incompatibility; vitamin; lactalbumin; lactoglobulin

Indexed keywords

EID: 84944198345     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-405171-3.00014-3     Document Type: Chapter

References (214)

1. S. Abbasi and E. Dickinson (2001) Influence of sugars on high-pressure induced gelation of skim milk dispersions. Food Hydrocolloids 15 315-319.
2. S. Abbasi and E. Dickinson (2002) Influence of high-pressure treatment on gelation of skim milk powder + low methoxyl pectin dispersions. High Pressure Res. 22 643-647.
3. M.H. Abd El-Salam and S. El-Shibiny (2012) Formation and potential uses of milk proteins as nano delivery vehicles for nutraceuticals: A review. Int. J. Dairy Technol. 65 13-21.
4. J. Adrian, R. Frangne and M. Rabache (1984) Effect of milk-proteins on retinol efficiency. Sci. Aliments 4 305-308.
5. D. Agudelo, M. Beauregard, G. Bérubé and H.A. Tajmir-Riahi (2012) Antibiotic doxorubicin and its derivative bind milk β-lactoglobulin. J. Photochem. Photobiol. B117 185-192.
6. B.F. Anderson, H.M. Baker, G.E. Norris, D.W. Rice and E.N. Baker (1989) Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution. J. Mol. Biol. 209 711-734.
7. L.O. Andersson, J. Brandt and S. Johansson (1971) The use of trinitrobenzenesulfonic acid in studies on the binding of fatty acid anions to bovine serum albumin. Arch. Biochem. Biophys. 146 428-440.
8. A. Anel, M. Calvo, J. Naval, M. Iturralde, M.A. Alava and A. Pineiro (1989) Interaction of rat α-fetoprotein and albumin with polyunsaturated and other fatty acids: Determination of apparent association constants. FEBS Lett. 250 22-24.
9. S.G. Anema (2010) Instability of pressure-treated reconstituted skim milk to acidification. Food Biophysics 5 321-329.
10. S.G. Anema (2012) Pressure-induced denaturation of β-lactoglobulin in skim milk: Effect of milk concentration. J. Agric. Food Chem. 60 6565-6570.
11. T. Arakawa and S.N. Timasheff (1982) Stabilization of protein structure by sugars. Biochemistry 21 6536-6544.
12. P. Aymard, D. Durand and T. Nicolai (1996) The effect of temperature and ionic strength on the dimerization of β-lactoglobulin. Int. J. Biol. Macromol. 19 213-221.
13. S. Baier and D.J. McClements (2001) Impact of preferential interactions on thermal stability and gelation of bovine serum albumin in aqueous sucrose solutions. J. Agric. Food Chem. 49 2600-2608.
14. S.K. Baier, E.A. Decker and D.J. McClements (2004) Impact of glycerol on thermostability and heat-induced gelation of bovine serum albumin. Food Hydrocolloids 18 91-100.
15. S.K. Baier and D.J. McClements (2003) Combined influence of NaCl and sucrose on heat-induced gelation of bovine serum albumin. J. Agric. Food Chem. 51 8107-8112.
16. G.F.M. Ball (1988) Fat-soluble vitamin assays in food analysis, a comprehensive review. London: Elsevier Applied Science
17. C. Barbana, M.D. Pérez, L. Sánchez, M. Dalgalarrondo, J.M. Chobert, T. Haertlé and M. Calvo (2006) Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy. Int. Dairy J. 16 18-25.
18. A. Barbiroli, F. Bonomi, P. Ferranti, D. Fessas, A. Nasi, P. Rasmussen and S. Iametti (2011) Bound fatty acids modulate the sensitivity of bovine β-lactoglobulin to chemical and physical denaturation. J. Agric. Food Chem. 59 5729-5737.
19. M. Bello, M.D.C. Portillo-Téllez and E. García-Hernández (2011) Energetics of ligand recognition and self-association of bovine β-lactoglobulin: Differences between variants A and B. Biochemistry 50 151-161.
20. A. Benzaria, M. Maresca, N. Taieb and E. Dumay (2013) Interaction of curcumin with phosphocasein micelles processed or not by dynamic high-pressure. Food Chem. 138 2327-2337.
21. W.R. Bezwoda and N. Mansoor (1986) Isolation and characterization of lactoferrin separated from human whey by adsorption chromatography using Cibacron Blue F3G-A linked affinity adsorbent. Clin. Chim. Acta 157 89-93.
22. J. Bhattacharyya and K.P. Das (2001) Interactions of chlorpromazine with milk proteins. Mol. Cell. Biochem. 221 11-15.
23. M.C. Bohin, J.P. Vincken, H.T.W.M. Van Der Hijden and H. Gruppen (2012) Efficacy of food proteins as carriers for flavonoids. J. Agric. Food Chem. 60 4136-4143.
24. P. Bourassa and H.A. Tajmir-Riahi (2012) Locating the binding sites of folic acid with milk α- and β-caseins. J. Phys. Chem. B 116 513-519.
25. J.I. Boye and I. Alli (2000) Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study. Food Res. Int. 33 673-682.
26. J.I. Boye, I. Alli and A.A. Ismail (1996) Interactions involved in the gelation of bovine serum albumin. J. Agric. Food Chem. 44 996-1004.
27. J.I. Boye, I. Alli and A.A. Ismail (1997) Use of differential scanning calorimetry and infrared spectroscopy in the study of thermal and structural stability of α-lactalbumin. J. Agric. Food Chem. 45 1116-1125.
28. J.I. Boye, A.A. Ismail and I. Alli (1996) Effects of physicochemical factors on the secondary structure of β-lactoglobulin. J. Dairy Res. 63 97-109.
29. C.R. Brinkmann, S. Thiel, M.K. Larsen, T.E. Petersen, J.C. Jensenius and C.W. Heegaard (2011) Preparation and comparison of cytotoxic complexes formed between oleic acid and either bovine or human α-lactalbumin. J. Dairy Sci. 94 2159-2170.
30. P. Busti, C.A. Gatti and N.J. Delorenzi (2006) Binding of alkylsulfonate ligands to bovine β-lactoglobulin: Effects on protein thermal unfolding. Food Res. Int. 39 503-509.
31. P. Busti, S. Scarpeci, C.A. Gatti and N.J. Delorenzi (2005) Binding of alkylsulfonate ligands to bovine β-lactoglobulin: Effects on protein denaturation by urea. Food Hydrocolloids 19 249-255.
32. K.M. Cawthern, M. Narayan, D. Chaudhuri, E.A. Permyakov and L.J. Berliner (1997) Interactions of α-lactalbumin with fatty acids and spin label analogs. J. Biol. Chem. 272 30812-30816.
33. M.S. Celej, S.A. Dassie, E. Freire, M.L. Bianconi and G.D. Fidelio (2005) Lingand-induced thermostability in proteins:Thermodynamic analysis of ANS-albumin interaction. Biochim. Biophys. Acta 1750 122-133.
34. W. Chanasattru, E.A. Decker and D.J. McClements (2007) Inhibition of droplet flocculation in globular-protein stabilized oil-in-water emulsions by polyols. Food Res. Int. 40 1161-1169.
35. W. Chanasattru, E.A. Decker and D.J. McClements (2007) Modulation of thermal stability and heat-induced gelation of β-lactoglobulin by high glycerol and sorbitol levels. Food Chem. 103 512-520.
36. W. Chanasattru, E.A. Decker and D.J. McClements (2007) Physicochemical basis for cosolvent modulation of β- lactoglobulin functionality: Interfacial tension study. Food Res. Int. 40 1098-1105.
37. W. Chanasattru, E.A. Decker and D.J. McClements (2008) Impact of cosolvents (polyols) on globular protein functionality: Ultrasonic velocity, density, surface tension and solubility study. Food Hydrocolloids 22 1475-1484.
38. M. Charles, B. Bernal and E. Guichard (1996) Interaction of β-lactoglobulin with flavour compounds. A.J. Taylor, D.S. Mottram (Eds) Flavour science: Recent developments Cambridge, UK: Royal Society of Chemistry 433-436.
39. Y.J. Cho, C.A. Batt and L. Sawyer (1994) Probing the retinol-binding site of bovine β-lactoglobulin. J. Biol. Chem. 269 11102-11107.
40. D.C. Clark, P.J. Wilde, D.R. Wilson and R. Wustneck (1992) The interaction of sucrose esters with β-lactoglobulin and β-casein from bovine-milk. Food Hydrocolloids 6 173-186.
41. T. Considine, H.A. Patel, S.G. Anema, H. Singh and L.K. Creamer (2007) Interactions of milk proteins during heat and high hydrostatic pressure treatments—a review. Innov. Food Sci. Emerging Technol. 8 1-23.
42. T. Considine, H.A. Patel, H. Singh and L.K. Creamer (2005) Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the heat-induced unfolding and aggregation of β-lactoglobulin B. J. Agric. Food Chem. 53 3197-3205.
43. T. Considine, H.A. Patel, H. Singh and L.K. Creamer (2007) Influence of binding conjugated linoleic acid and myristic acid on the heat- and high-pressure-induced unfolding and aggregation of β-lactoglobulin B. Food Chem. 102 1270-1280.
44. T. Considine, H. Singh, H.A. Patel and L.K. Creamer (2005) Influence of binding of sodium dodecyl sulfate, all-trans-retinol, and 8-anilino-1-naphthalenesulfonate on the high-pressure-induced unfolding and aggregation of β-lactoglobulin B. J. Agric. Food Chem. 53 8010-8018.
45. L. Creamer (1980) A study of the effect of sodium dodecyl sulfate on bovine β-casein self-association. Archives Biochemistry and Biophysics 199 172-178.
46. L.K. Creamer (1995) Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin. Biochemistry 34 7170-7176.
47. L.K. Creamer, S.M. Loveday and L. Sawyer (2011) Milk proteins | β-Lactoglobulin, Encyclopedia of Dairy Sciences. 2nd ed. Oxford: Elsevier
48. J.X. Dai-Dong, G. Novak and J. Hardy (1990) Stabilization of vitamin C by β-lactoglobulin during heat treatment. Sci. Aliments 10 393-401.
49. S. Damodaran and J.E. Kinsella (1980) Flavor protein interactions. Binding of carbonyls to bovine serum albumin—thermodynamic and conformational effects. J. Agric. Food Chem. 28 567-571.
50. S. Damodaran and J.E. Kinsella (1981) The effect of neutral salts on the stability of macromolecules – a new approach using a protein-ligand binding system. J. Biol. Chem. 256 3394-3398.
51. Das, S., Ellis, A., Mittal, V.A., Singh, H., Ye, A., 2013. Micronutrient fortification process and its uses, PCT Application No. PCT/NZ2013/000109.
52. A.F. Devi, R. Buckow, Y. Hemar and S. Kasapis (2013) Structuring dairy systems through high pressure processing. J. Food Eng. 114 106-122.
53. F. Diarrassouba, G. Remondetto, L. Liang, G. Garrait, E. Beyssac and M. Subirade (2013) Effects of gastrointestinal pH conditions on the stability of the β-lactoglobulin/vitamin D3 complex and on the solubility of vitamin D3. Food Res. Int. 52, 515-521
54. E. Dickinson (2010) Flocculation of protein-stabilized oil-in-water emulsions. Colloids Surf., B 81 130-140.
55. S. Dierckx and A. Huyghebaert (2002) Effects of sucrose and sorbitol on the gel formation of a whey protein isolate. Food Hydrocolloids 16 489-497.
56. A. Divsalar and A.A. Saboury (2005) Comparative structural and conformational studies on two forms of β-lactoglobulin (A and B) upon interaction with lead ion. FEBS J. 272 340.
57. A. Divsalar, A.A. Saboury, H. Mansoori-Torshizi and B. Hemmatinejad (2006) Comparative and structural analysis of the interaction between β-lactoglobulin type A and B with a new anticancer component (2, 2′-bipyridin n-hexyl dithiocarbamato Pd(II) nitrate). Bull. Korean Chem. Soc. 27 1801-1808.
58. A. Divsalar, A.A. Saboury and A.A. Moosavi-Movahedi (2006) A study on the interaction between β-lactoglobulin a and a new antitumor reagent (2, 2-bipyridinglycinato Pd(II) chloride). FEBS J. 273 333.
59. E. Dufour and T. Haertle (1990) Alcohol induced changes of β-lactoglobulin-retinol-binding stoichiometry. Protein Eng. 4 185-190.
60. E. Dufour, G.H.B. Hoa and T. Haertle (1994) High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescence. Biochim. Biophys. Acta 1206 166-172.
61. E. Dufour and T. Haertle (1991) Binding of retinoids and β-carotene to β-lactoglobulin. Influence of protein modifications. Biochim. Biophys. Acta 1079 316-320.
62. E.M. Dumay, M.T. Kalichevsky and J.C. Cheftel (1994) High-pressure unfolding and aggregation of β-lactoglobulin and the baroprotective effects of sucrose. J. Agric. Food Chem. 42 1861-1868.
63. E.M. Dumay, M.T. Kalichevsky and J.C. Cheftel (1998) Characteristics of pressure-induced gels of β-lactoglobulin at various times after pressure release. Food. Sci. Technol. —LWT 31 10-19.
64. C. Ebel, H. Eisenberg and R. Ghirlando (2000) Probing protein-sugar interactions. Biophys. J. 78 385-393.
65. A.O. Elzoghby, W.S. Abo El-Fotoh and N.A. Elgindy (2011) Casein-based formulations as promising controlled release drug delivery systems. J. Control. Release 153 206-216.
66. A.O. Elzoghby, W.M. Samy and N.A. Elgindy (2013) Novel spray-dried genipin-crosslinked casein nanoparticles for prolonged release of alfuzosin hydrochloride. Pharm. Res. 30 512-522.
67. R.J. FitzGerald (1998) Potential uses of caseinophosphopeptides. Int. Dairy J. 8 451-457.
68. F. Fogolari, L. Ragona, S. Licciardi, S. Romagnoli, R. Michelutti, R. Ugolini and H. Molinari (2000) Electrostatic properties of bovine β-lactoglobulin. Proteins: Struct., Funct., Genet. 39 317-330.
69. J. Fontecha and H.E. Swaisgood (1995) Interaction of sucrose ester with casein micelles as characterized by size-exclusion chromatography. J. Dairy Sci. 78 2660-2665.
70. J.E. Ford (1974) Some observations on possible nutritional significance of vitamin-B12-binding and folate-binding proteins in milk. Br. J. Nutr. 31 243-257.
71. S.A. Forrest, R.Y. Yada and D. Rousseau (2005) Interactions of vitamin D3 with bovine β-lactoglobulin a and β-casein. J. Agric. Food Chem. 53 8003-8009.
72. K.L. Franzen and J.E. Kinsella (1974) Parameters affecting binding of volatile flavor compounds in model food systems 1. Proteins. J. Agric. Food Chem. 22 675-678.
73. D. Frapin, E. Dufour and T. Haertle (1993) Probing the fatty acid binding site of β-lactoglobulins. J. Protein Chem. 12 443-449.
74. S. Futterman and J. Heller (1972) The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin, and the retinol-binding protein of human plasma. J. Biol. Chem. 247 5168-5172.
75. E. Guichard and S. Langourieux (2000) Interactions between β-lactoglobulin and flavour compounds. Food Chem. 71 301-308.
76. H. Guth and R. Fritzler (2004) Binding studies and computer-aided modelling of macromolecule/odorant interactions. Chemical Biodiversity 1 2001-2023.
77. H.K. Ha, J.W. Kim, M.R. Lee and W.J. Lee (2013) Formation and characterization of quercetin-loaded chitosan oligosaccharide/β-lactoglobulin nanoparticle. Food Res. Int. 52 82-90.
78. M. Haham, S. Ish-Shalom, M. Nodelman, I. Duek, E. Segal, M. Kustanovich and Y.D. Livney (2012) Stability and bioavailability of vitamin D nanoencapsulated in casein micelles. Food Funct. 3 737-744.
79. H.O. Hammou, I.M. Plaza del Pino and J.M. Sanchez-Ruiz (1998) Hydration changes upon protein unfolding: Cosolvent effect analysis. New J. Chem. 22 1453-1461.
80. J.G. Hansted, P.L. Wejse, H. Bertelsen and D.E. Otzen (2011) Effect of protein-surfactant interactions on aggregation of β-lactoglobulin. Biochim. Biophys. Acta, Proteins Proteomics 1814 713-723.
81. P. Havea, H. Singh and L.K. Creamer (2001) Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment. J. Dairy Res. 68 483-497.
82. L. He, J. Zheng, T.P. Labuza and H. Xiao (2013) A surface enhanced Raman spectroscopic study of interactions between casein and polymethoxyflavones. J. Raman Spectrosc 531-535.
83. M.R. Housaindokht, J. Chamani, A.A. Saboury, A.A. Moosavi-Movahedi and M. Bahrololoom (2001) Three binding sets analysis of α-lactalbumin by interaction of tetradecyl trimethyl ammonium bromide. Bull. Korean Chem. Soc. 22 145-148.
84. T. Huppertz, P.F. Fox, K.G. de Kruif and A.L. Kelly (2006) High pressure-induced changes in bovine milk proteins: A review. Biochim. Biophys. Acta, Proteins Proteomics 1764 593-598.
85. E. Jasinski and A. Kilara (1985) Flavor binding by whey proteins. Milchwissenschaft 40 596-599.
86. M.N. Jones and A. Wilkinson (1976) The interaction between β-lactoglobulin and sodium n-dodecylsulfate. Biochem J. 153 713-718.
87. K.D. Jou and W.J. Harper (1996) Effect of di-saccharides on the thermal properties of whey proteins determined by differential scanning calorimetry (DSC). Milchwissenschaft 51 509-511.
88. E. Jouenne and J. Crouzet (2000) Determination of apparent binding constants for aroma compounds with β-lactoglobulin by dynamic coupled column liquid chromatography. J. Agric. Food Chem. 48 5396-5400.
89. D.M. Jung, J.S. de Ropp and S.E. Ebeler (2002) Application of pulse field gradient NMR techniques for investigating binding of flavor compounds to macromolecules. J. Agric. Food Chem. 50 4262-4269.
90. D.M. Jung and S.E. Ebeler (2003) Investigation of binding behaviour of α- and β-ionones to β-lactoglobulin at different pH values using a diffusion-based NOE pumping technique. J. Agric. Food Chem. 51 1988-1993.
91. T. Kamiyama, Y. Sadahide, Y. Nogusa and K. Gekko (1999) Polyol-induced molten globule of cytochrome C: An evidence for stabilization by hydrophobic interaction. Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. 1434 44-57.
92. C.D. Kanakis, I. Hasni, P. Bourassa, P.A. Tarantilis, M.G. Polissiou and H.A. Tajmir-Riahi (2011) Milk β-lactoglobulin complexes with tea polyphenols. Food Chem. 127 1046-1055.
93. C. Kanno, N. Kanehara, K. Shirafuji, R. Tanji and T. Imai (1991) Binding form of vitamin-B2 in bovine-milk—its concentration, distribution and binding linkage. J. Nutr. Sci. Vitaminol. 37 15-27.
94. J.K. Kaushik and R. Bhat (1998) Thermal stability of proteins in aqueous polyol solutions: Role of the surface tension of water in the stabilizing effect of polyols. J. Phys. Chem. B 102 7058-7066.
95. R.D. Keenan, D.J. Young, C.M. Tier, A.D. Jones and J. Underdown (2001) Mechanism of pressure-induced gelation of milk. J. Agric. Food Chem. 49 3394-3402.
96. J.J. Kehoe and E.A. Foegeding (2011) Interaction between beta-casein and whey proteins as a function of pH and salt concentration. J. Agric. Food Chem. 59 349-355.
97. I. Kibangou, S. Bouhallab, F. Bureau, S. Allouche, G. Thouvenin and D. Bouglé (2008) Caseinophosphopeptide-bound iron: Protective effect against gut peroxidation. Ann. Nutr. Metab. 52 177-180.
98. I. Klaassen, R.H. Brakenhoff, S.J. Smeets, G.B. Snow and B.J.M. Braakhuis (1999) Considerations for in vitro retinoid experiments: Importance of protein interaction. Biochim. Biophys. Acta, Gen. Subj. 1427 265-275.
99. G. Kontopidis, C. Holt and L. Sawyer (2004) Invited review: β-lactoglobulin: Binding properties, structure, and function. J. Dairy Sci. 87 785-796.
100. T. Konuma, M. Sakurai and Y. Goto (2007) Promiscuous binding of ligands by β-lactoglobulin involves hydrophobic interactions and plasticity. J. Mol. Biol. 368 209-218.
101. J. Kühn, T. Considine and H. Singh (2006) Interactions of milk proteins and volatile compounds: Implications in the development of protein foods. J. Food Sci. 71 R72-R82.
102. A. Kulmyrzaev, C. Bryant and D.J. McClements (2000) Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins. J. Agric. Food Chem. 48 1593-1597.
103. E. Lamiot, E. Dufour and T. Haertle (1994) Insect sex pheromone binding by bovine β-lactoglobulin. J. Agric. Food Chem. 42 695-699.
104. J.C. Lee and S.N. Timasheff (1981) The stabilization of proteins by sucrose. J. Biol. Chem. 256 7193-7201.
105. A. Lerbret, P. Bordat, F. Affouard, M. Descamps and F. Migliardo (2005) How homogeneous are the trehalose, maltose, and sucrose water solutions? An insight from molecular dynamics simulations. J. Phys. Chem. B 109 11046-11057.
106. E. Lietaer, A. Poiffait and J. Adrian (1991) Studies on the interaction between casein and vitamin A. Food. Sci. Technol.—LWT 24 39-45.
107. T.Y. Lin and S.N. Timasheff (1996) On the role of surface tension in the stabilization of globular proteins. Protein Sci. 5 372-381.
108. R.A. Lindner, A. Kapur and J.A. Carver (1997) The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine-lactalbumin. J. Biol. Chem. 272 27722-27729.
109. K. Lišková, M.A.E. Auty, V. Chaurin, S. Min, K.H. Mok, N. O’Brien, A.L. Kelly and A. Brodkorb (2011) Cytotoxic complexes of sodium oleate with β-lactoglobulin. Eur. J. Lipid Sci. Technol. 113 1207-1218.
110. X. Liu, J.R. Powers, B.G. Swanson, H.H. Hill and S. Clark (2005) Modification of whey protein concentrate hydrophobicity by high hydrostatic pressure. Innov. Food Sci. Emerging Technol. 6 310-317.
111. Y.D. Livney (2010) Milk proteins as vehicles for bioactives. Curr. Opin. Colloid Interface Sci. 15 73-83.
112. Livney, Y.D., and Dalgleish, D.G. 2007. Casein micelles for nanoencapsulation of hydrophobic compounds. Patent application WO2007122613 A1.
113. J.I. Loch, A. Polit, P. Bonarek, D. Olszewska, K. Kurpiewska, M. Dziedzicka-Wasylewska and K. Lewiski (2012) Structural and thermodynamic studies of binding saturated fatty acids to bovine β-lactoglobulin. Int. J. Bio. Macromol. 50 1095-1102.
114. S.M. Loveday, M.A. Rao and H. Singh (2012) Food protein nanoparticles: Formation, properties and applications. B. Bhandari, Y.H. Roos (Eds) Food materials science and engineering Oxford: Blackwell Publishing 263-294.
115. S.M. Loveday, A. Sarkar and H. Singh (2013) Innovative yoghurts: Novel processing technologies for improving acid milk gel texture. Trends Food Sci. Tech. 33 5-20.
116. S.M. Loveday and H. Singh (2008) Recent advances in technologies for vitamin A protection in foods. Trends Food Sci. Tech. 19
117. R.-C. Lu, A.-N. Cao, L.-H. Lai and J.-X. Xiao (2006) Effect of cationic surfactants on the interaction between sodium perfluorooctanoate and β-lactoglobulin. J. Colloid Interface Sci. 293 61-68.
118. L. Mata, L. Sanchez and M. Calvo (1997) Interaction of mercury with human and bovine milk proteins. Biosci. Biotechol. Biochem. 61 1641-1645.
119. S. Maulik, D.S.P. Moulik and D.K. Chattoraj (1996) Biopolymer—surfactant interaction: 4 kinetics of binding of cetyltrimethyl ammonium bromide with gelatin, hemoglobin, β-lactoglobulin and lysozyme. J. Biomol. Struct. Dyn. 13 771-780.
120. D.J. McClements (2002) Modulation of globular protein functionality by weakly interacting cosolvents. Crit. Rev. Food Sci. Nutr. 42 417-471.
121. V.L. McNeill and K.A. Schmidt (1993) Vanillin interaction with milk protein isolates in sweetened drinks. J. Food Sci. 58 1142-1144. 1147
122. D. Mercadante, L.D. Melton, G.E. Norris, T.S. Loo, M.A.K. Williams, R.C.J. Dobson and G.B. Jameson (2012) Bovine β-lactoglobulin is dimeric under imitative physiological conditions: Dissociation equilibrium and rate constants over the pH range of 2.5–7.5. Biophys. J. 103 303-312.
123. K.A. Mohammadzadeh, G.M. Smith and R.E. Feeney (1969) Hydrophobic binding of hydrocarbons by proteins II. Relationship of protein structure. Biochim. Biophys. Acta 194 256-264.
124. M.S. Mohan, J.L. Jurat-Fuentes and F. Harte (2013) Binding of vitamin A by casein micelles in commercial skim milk. J. Dairy Sci. 96 790-798.
125. H.L. Monaco, G. Zanotti, P. Spadon, M. Bolognesi, L. Sawyer and E.E. Eliopoulos (1987) Crystal structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 197 695-706.
126. A. Mora-Gutierrez and H.M. Farrell (2000) Sugar–casein interaction in deuterated solutions of bovine and caprine casein as determined by oxygen-17 and carbon-13 nuclear magnetic resonance: A case of preferential interactions. J. Agric. Food Chem. 48 3245-3255.
127. S. Muresan, A. van der Bent and F.A. de Wolf (2001) Interaction of β-lactoglobulin with small hydrophobic ligands as monitored by fluorometry and equilibrium dialysis: Nonlinear quenching effects related to protein–protein association. J. Agric. Food Chem. 49 2609-2618.
128. B.S. Murray and H.J. Liang (1999) Enhancement of the foaming properties of protein dried in the presence of trehalose. J. Agric. Food Chem. 47 4984-4991.
129. Y. Nagasako, H. Saito, Y. Tamura, S. Shimamura and M. Tomita (1993) Iron-binding properties of bovine lactoferrin in iron-rich solution. J. Dairy Sci. 76 1876-1881.
130. K. Nagy, M.C. Courtet-Compondu, G. Williamson, S. Rezzi, M. Kussmann and A. Rytz (2012) Non-covalent binding of proteins to polyphenols correlates with their amino acid sequence. Food Chem. 132 1333-1339.
131. M. Narayan and L.J. Berliner (1997) Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin. Biochemistry 36 1906-1911.
132. M. Narayan and L.J. Berliner (1998) Mapping fatty acid binding to β-lactoglobulin: Ligand binding is restricted by modification of cys 121. Protein Sci. 7 150-157.
133. P.F. Nixon, M. Jones and D.J. Winzor (2004) Quantitative description of the interaction between folate and the folate-binding protein from cow's milk. Biochem J. 382 215-221.
134. J.E. O’Connell and P.F. Fox (2003) Heat-induced coagulation of milk. P.F. Fox, P.L.H. McSweeney (Eds) Advanced Dairy Chemistry—Proteins New York: Kluwer Academic/Plenum Publishers 879-945.
135. T.E. O’Neill and J.E. Kinsella (1987) Binding of alkanone favors to β-lactoglobulin-effects of conformational and chemical modification. J. Agric. Food Chem. 35 770-774.
136. B.A. Oelrichs, C.C. Kratzing, J.D. Kelly and D.J. Winzor (1984) The binding of ascorbate to bovine serum-albumin. Int. J. Vitam. Nutr. Res. 54 61-64.
137. M.Z. Papiz, L. Sawyer, E.E. Eliopoulos, A.C.T. North, J.B.C. Findlay, R. Sivaprasadarao, T.A. Jones, M.E. Newcomer and P.J. Kraulis (1986) The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324 383-385.
138. J.M. Peres, S. Bouhallab, C. Petit, F. Bureau, J.L. Maubois, P. Arhan and D. Bougle (1998) Improvement of zinc intestinal absorption and reduction of zinc/iron interaction using metal bound to the caseinophosphopeptide 1-25 of β-casein. Reprod., Nutr., Dev. 38 465-472.
139. M.D. Pérez and M. Calvo (1995) Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: A review. J. Dairy Sci. 78 978-988.
140. M.D. Pérez, C. Diaz de Villegas, L. Sanchez, P. Aranda, J.M. Ena and M. Calvo (1989) Interaction of fatty acids with β-lactoglobulin and albumin from ruminant milk. J. Biochem. 106 1094-1097.
141. M.D. Pérez, P. Puyol, J.M. Ena and M. Calvo (1993) Comparison of the ability to bind lipids of β-lactoglobulin and serum-albumin of milk from ruminant and non-ruminant species. J. Dairy Res. 60 55-63.
142. M.D. Pérez, L. Sanchez, P. Aranda, J.M. Ena and M. Calvo (1990) Synthesis and evolution of concentration of β-lactoglobulin and α-lactalbumin from cow and sheep colostrums and milk throughout early lactation. Cell. Mol. Biol. 36 205-212.
143. M.D. Pérez, L. Sanchez, P. Aranda, J.M. Ena, R. Oria and M. Calvo (1992) Effect of β-lactoglobulin on the activity of pregastric lipase. A possible role for this protein in ruminant milk. Biochim. Biophys. Acta 1123 151-155.
144. E.A. Permyakov, L.A. Morozova, L.P. Kahnichenko and V.Y. Derezhkov (1988) Interaction of α-lactalbumin with Cu2+. Biophys. Chem. 32 37-42.
145. A. Poiffait and J. Adrian (1991) Interaction between casein and vitamin A during food processing. Adv. Exp. Med. Biol. 289 61-73.
146. R. Politi and D. Harries (2010) Enthalpically driven peptide stabilization by protective osmolytes. Chem. Comm. 46 6449-6451.
147. P. Puyol, M.D. Perez, L. Mata and M. Calvo (1994) Study on interaction between β-lactoglobulin and other bovine whey proteins with ascorbic acid. Milchwissenschaft 49 25-27.
148. P. Puyol, M.D. Perez, J.M. Peiro and M. Calvo (1991) Interaction of bovine β-lactoglobulin and other bovine and human whey proteins with retinol and fatty acids. Agric. Biol. Chem. 55 2515-2520.
149. B.Y. Qin, L.K. Creamer, E.N. Baker and G.B. Jameson (1998) 12-bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin. FEBS Lett. 438 272-278.
150. L. Ragona, F. Fogolari, L. Zetta, D.M. Perez, P. Puyol, K. De Kruif, F. Lohr, H. Ruterjans and H. Molinari (2000) Bovine β-lactoglobulin: Interaction studies with palmitic acid. Protein Sci. 9 1347-1356.
151. S. Rahimi Yazdi and M. Corredig (2012) Heating of milk alters the binding of curcumin to casein micelles. A fluorescence spectroscopy study. Food Chem. 132 1143-1149.
152. N. Raica Jr., M.G. Vavich and A.R. Kemmerer (1959) The effects of several milk components and similar compounds on the utilization of carotene by the rat. Arch. Biochem. Biophys. 83 376-380.
153. G.A. Reineccius and S.T. Coulter (1969) Flavour rentention during drying. J. Dairy Sci. 52 1219-1223.
154. M.R. Rodríguez Niño and J.M. Rodríguez Patino (2002) Effect of the aqueous phase composition on the adsorption of bovine serum albumin to the air–water interface. Ind. Eng. Chem. Res. 41 1489-1495.
155. C.M. Romero, J.M. Lozano, J. Sancho and G.I. Giraldo (2007) Thermal stability of β-lactoglobulin in the presence of aqueous solution of alcohols and polyols. Int. J. Bio. Macromol. 40 423-428.
156. J. Rösgen (2007) Molecular basis of osmolyte effects on protein and metabolites. Methods Enzymol. 428 459-486.
157. S. Roufik, S.F. Gauthier, X. Leng and S.L. Turgeon (2006) Thermodynamics of binding interactions between bovine β-lactoglobulin a and the antihypertensive peptide β-lg f142-148. Biomacromolecules 7 419-426.
158. M. Sahihi, Y. Ghayeb and A.-K. Bordbar (2012) Fluorescence spectroscopic study on interaction of retinol with β-lactoglobulin in the presence of cetylpyridinium chloride. Spectroscopy 27 27-34.
159. M.J. Sáiz-Abajo, C. González-Ferrero, A. Moreno-Ruiz, A. Romo-Hualde and C.J. González-Navarro (2013) Thermal protection of β-carotene in re-assembled casein micelles during different processing technologies applied in food industry. Food Chem. 138 1581-1587.
160. D.N. Salter and A. Mowlem (1983) Neonatal role of milk folate-binding protein—studies on the course of digestion of goats milk folate binder in the 6-d-old kid. Br. J. Nutr. 50 589-596.
161. E.P. Schokker, H. Singh, D.N. Pinder, G.E. Norris and L.K. Creamer (1999) Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin ab at neutral pH. Int. Dairy J. 9 791-800.
162. M.G. Semenova, A.S. Antipova and L.E. Belyakova (2002) Food protein interactions in sugar solutions. Curr. Opin. Colloid Interface Sci. 7 438-444.
163. A. Shapira, Y.G. Assaraf, D. Epstein and Y.D. Livney (2010) β-casein nanoparticles as an oral delivery system for chemotherapeutic drugs: Impact of drug structure and properties on co-assembly. Pharm. Res. 27 2175-2186.
164. M. Shimoyamada, H. Yoshimura, K. Tomida and K. Watanabe (1996) Stabilities of bovine β-lactoglobulin/retinol or retinoic acid complexes against tryptic hydrolysis, heating and light-induced oxidation. Lebensm. -Wiss. Technol. 29 763-766.
165. H. Singh and J. Flanagan (2005) Milk proteins. Y.H. Hui (Eds) Handbook of Food Science, Technology and Engineering New York: CRC Press 1-23.
166. H. Singh and P. Havea (2003) Thermal denaturation, aggregation and gelation of whey proteins. P.F. Fox, P.L.H. McSweeney (Eds) Advanced Dairy Chemistry—Proteins New York: Kluwer Academic/Plenum Publishers 1261-1287.
167. L.R. Singh, N.K. Poddar, T.A. Dar, R. Kumar and F. Ahmad (2011) Protein and DNA destabilization by osmolytes: The other side of the coin. Life Sci. 88 117-125.
168. A.H. Sneharani, J.V. Karakkat, S.A. Singh and A.G.A. Rao (2010) Interaction of curcumin with β-lactoglobulin; stability, spectroscopic analysis, and molecular modeling of the complex. J. Agric. Food Chem. 58 11130-11139.
169. K. Sostmann and E. Guichard (1998) Immobilized β-lactoglobulin on a HPLC-column: A rapid way to determine protein-flavour interactions. Food Chem. 62 509-513.
170. A.A. Spector (1975) Fatty acid binding to plasma albumin. J. Lipid Res. 16 165-179.
171. A.A. Spector, K. John and J.E. Fletcher (1969) Binding of long-chain fatty acids to bovine serum albumin. J. Lipid Res. 10 56-67.
172. T. Spiegel (1999) Whey protein aggregation under shear conditions—effects of lactose and heating temperature on aggregate size and structure. Int. J. Food Sci. Technol. 34 523-531.
173. Y. Sreelakshmi and K.K. Sharma (2001) Interaction of α-lactalbumin with mini-αa-crystallin. J. Protein Chem. 20 123-130.
174. M. Sugiarto, A. Ye and H. Singh (2009) Characterisation of binding of iron to sodium caseinate and whey protein isolate. Food Chem. 114 1007-1013.
175. M. Sugiarto, A. Ye, M.W. Taylor and H. Singh (2010) Milk protein-iron complexes: Inhibition of lipid oxidation in an emulsion. Dairy Sci. Technol. 90 87-98.
176. H.E. Swaisgood (2001) Protein ingredient for carrying lipophilic nutrients. United States Patent 6 290 274.
177. H.E. Swaisgood (2003) Chemistry of the caseins. P.F. Fox, P.L.H. McSweeney (Eds) Advanced Dairy Chemistry—Proteins New York: Kluwer Academic/Plenum Publishers 139-201.
178. J.B. Swaney and I.M. Klotz (1970) Amino acid sequence adjoining the lone tryptophan of human serum albumin. A binding site of the protein. Biochem J. 9 2570-2574.
179. A. Taheri-Kafrani, A.-K. Bordbar, S.H.-A. Mousavi and T. Haertle (2008) β-lactoglobulin structure and retinol binding changes in presence of anionic and neutral detergents. J. Agric. Food Chem. 56 7528-7534.
180. X. Tang and M.J. Pikal (2005) Measurement of the kinetics of protein unfolding in viscous systems and implications for protein stability in freeze-drying. Pharm. Res. 22 1176-1185.
181. S.N. Timasheff (1993) The control of protein stability and association by weak-interactions with water - how do solvents affect these processes. Annu. Rev. Biophys. Biomol. Struct. 22 67-97.
182. S.N. Timasheff (1998) Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated. Adv. Protein Chem. 51 355-432.
183. S.N. Timasheff (2002) Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry 41 13473-13482.
184. A. Tiwari and R. Bhat (2006) Stabilization of yeast hexokinase A by polyol osmolytes: Correlation with the physicochemical properties of aqueous solutions. Biophys. Chem. 124 90-99.
185. T. Toyosaki and T. Mineshita (1988) Antioxidant effects of protein-bound riboflavin and free riboflavin. J. Food Sci. 53 1851-1853.
186. T. Tukamoto, S. Ozeki, F. Hattori and T. Ishida (1974) Drug interactions. 1. Binding of ascorbic-acid and fatty-acid ascorbyl esters to bovine serum-albumin. Chem. Pharm. Bull. 22 385-389.
187. H.M. Ueno, N. Ueda, M. Morita, Y. Kakehi and T. Kobayashi (2012) Thermal stability of the iron-lactoferrin complex in aqueous solution is improved by soluble soybean polysaccharide. Food Biophysics 7 183-189.
188. S.M. van Ruth, G. de Vries, M. Geary and P. Giannouli (2002) Influence of composition and structure of oil-in-water emulsions on retention of aroma compounds. J. Sci. Food Agric. 82 1028-1035.
189. G.E. Vegarud, T. Langsrud and C. Svenning (2000) Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics. Br. J. Nutr. 84(Suppl 1), S91-98.
190. M.I. Viseu, E.P. Melo, T.I. Carvalho, R.F. Correia and S.M.B. Costa (2007) Unfolding kinetics of β-lactoglobulin induced by surfactant and denaturant: A stopped-flow/fluorescence study. Biophys. J. 93 3601-3612.
191. A. Voilley, V. Beghin, C. Charpentier and D. Peyron (1991) Interaction between aroma substances and macromolecules in model wine. Lebensm. -Wiss. Technol. 24 469-472.
192. Q. Wang, J.C. Allen and H.E. Swaisgood (1999) Binding of lipophilic nutrients to β-lactoglobulin prepared by bioselective adsorption. J. Dairy Sci. 82 257-264.
193. Q.W. Wang, J.C. Allen and H.E. Swaisgood (1997) Binding of retinoids to β-lactoglobulin isolated by bioselective adsorption. J. Dairy Sci. 80 1047-1053.
194. Q.W. Wang, J.C. Allen and H.E. Swaisgood (1997) Binding of vitamin D and cholesterol to β-lactoglobulin. J. Dairy Sci. 82 257-264.
195. X. Wang, M. Li, M. Li, X. Mao, J. Zhou and F. Ren (2011) Preparation and characteristics of yak casein hydrolysate-iron complex. Int. J. Food Sci. Technol. 46 1705-1710.
196. R. Waninge, M. Paulsson, T. Nylander, B. Ninham and P. Sellers (1998) Binding of sodium dodecyl sulfate and dodecyl trimethyl ammonium chloride to β-lactoglobulin: A calorimetric study. Int. Dairy J. 8 141-148.
197. H. Weiser and G. Somorjai (1992) Bioactivity of cis and dicis isomers of vitamin A esters. Int. J. Vitam. Nutr. Res. 62 201-208.
198. J.R. Wendorf, C.J. Radke and H.W. Blanch (2004) Reduced protein adsorption at solid interfaces by sugar excipients. Biotechnol. Bioeng. 87 565-573.
199. S.Y. Wu, M.D. Perez, P. Puyol and L. Sawyer (1999) β-Lactoglobulin binds palmitate within its central cavity. J. Biol. Chem. 274 170-174.
200. X. Wu, R. Dey, H. Wu, Z. Liu, Q. He and X. Zeng (2013) Studies on the interaction of -epigallocatechin-3-gallate from green tea with bovine β-lactoglobulin by spectroscopic methods and docking. Int. J. Dairy Technol. 66 7-13.
201. X. Wu, H. Wu, M. Liu, Z. Liu, H. Xu and F. Lai (2011) Analysis of binding interaction between (-)-epigallocatechin (EGC) and β-lactoglobulin by multi-spectroscopic method. Spectrochim. Acta, Part A 82 164-168.
202. G. Xie and S.N. Timasheff (1997) The thermodynamic mechanism of protein stabilization by trehalose. Biophys. Chem. 64 25-43.
203. G.F. Xie and S.N. Timasheff (1997) Mechanism of the stabilization of ribonuclease A by sorbitol: Preferential hydration is greater for the denatured than for the native protein. Protein Sci. 6 211-221.
204. Y. Xie, A. Kosinska, H. Xu and W. Andlauer (2013) Milk enhances intestinal absorption of green tea catechins in in vitro digestion/Caco-2 cells model. Food Res. Int. 793-800.
205. M.C. Yang, H.H. Guan, M.Y. Liu, Y.H. Lin, J.M. Yang, W.L. Chen, C.J. Chen and S.J.T. Mao (2008) Crystal structure of a secondary vitamin D3 binding site of milk β-lactoglobulin. Proteins: Struct., Funct., Genet. 71 1197-1210.
206. X. Zhang, X. Fu, H. Zhang, C. Liu, W. Jiao and Z. Chang (2005) Chaperone-like activity of β-casein. Int. J. Biochem. Cell Biol. 37 1232-1240.
207. Y. Zhang and Q. Zhong (2013) Encapsulation of bixin in sodium caseinate to deliver the colorant in transparent dispersions. Food Hydrocolloids 33 1-9.
208. Y. Zhang and Q. Zhong (2013) Probing the binding between norbixin and dairy proteins by spectroscopy methods. Food Chem. 139 611-616.
209. Z.H. Zhang, X.P. Wang, W.Y. Ayman, W.L. Munyendo, H.X. Lv and J.P. Zhou (2013) Studies on lactoferrin nanoparticles of gambogic acid for oral delivery. Drug Delivery 20 86-93.
210. J. Zhou, X. Wang, T. Ai, X. Cheng, H.Y. Guo, G.X. Teng and X.Y. Mao (2012) Preparation and characterization of β-lactoglobulin hydrolysate-iron complexes. J. Dairy Sci. 95 4230-4236.
211. X.Q. Zhu (2003) Interactions between flavour compounds and milk proteins. Palmerston North, New Zealand: Institute of Food, Nutrition and Human Health. Massey University
212. P. Zimet, D. Rosenberg and Y.D. Livney (2011) Re-assembled casein micelles and casein nanoparticles as nano-vehicles for ω-3 polyunsaturated fatty acids. Food Hydrocolloids 25 1270-1276.
213. F. Zsila, E. Hazai and L. Sawyer (2005) Binding of the pepper alkaloid piperine to bovine β-lactoglobulin: Circular dichroism spectroscopy and molecular modeling study. J. Agric. Food Chem. 53 10179-10185.
214. F. Zsila, T. Imre, B.Z. Szabo and M. Simonyi (2002) Induced chirality upon binding of cis-parinaric acid to bovine β-lactoglobulin: Spectroscopic characterization of the complex. FEBS Lett. 520 81-87.