45. Hendrix T, Griko YV, Privalov PL (2000) A calorimetric study of the influence of calcium on
the stability of bovine α lactalbumin. Biophys Chem 84:27–34
46. Hiraoka Y, Secawa T, Kuwajima K et al (1980) α-Lactalbumin: a metalloprotein. Biochem
Biophys Res Commun 95(3):1098–1104
47. Bernal V, Jelen P (1984) Effect of calcium binding on thermal denaturation of bovine
α-lactalbumin. J Dairy Sci 67:2452–2454
48. DeWit JN, Klarenbeek G (1984) Effects of various heat treatments on structure and solubility
of whey proteins. J Dairy Sci 67:2701–2710
49. Griko YV, Remeta DP (1999) Energetics of solvent and ligand induced conformational
changes in α-lactalbumin. Protein Sci 8(3):554–561
50. Warner RC (1954) In: Neurath H, Bailey K (eds) The proteins, vol 2. Academic, New York,
p 443
51. Li Chan E, Nakai S (1989) Biochemical basis for the properties of egg white. Crit Rev Poult
Biol 2:21–57
52. Narita K, Ishii J (1962) N terminal sequence in ovalbumin. J Biochem (Tokyo) 52:367–373
53. Nisbet AD, Saundry RH, Moir AJ et al (1981) The complete amino acid sequence of hen
ovalbumin. Eur J Biochem 115:335–345
54. Stein PE, Leslie AG, Finch JT et al (1990) Crystal structure of ovalbumin as a model for the
reactive centre of serpins. Nature 347:99–102
55. Stein PE, Leslie AG, Finch JT et al (1991) Crystal structure of uncleaved ovalbumin at 1.95 A ˚
resolution. J Mol Biol 221:941–959
56. Matsumoto T, Chiba J, Inoue H (1992) Effect of pH on colloidal properties of native ovalbumin
aqueous systems. Colloid Polym Sci 270:687–693
57. Farrel HM Jr, Qi PX, Uversky VN (2006) New views of protein structure: applications to the
caseins: protein structure and functionality. In: Fishman ML, Qi PX, Wisker L (eds)
Advances in biopolymers: molecules, clusters, networks, and interactions. American Chemical Society, Washington, DC, pp 52–70
58. Holt C, Sawyer L (1993) Caseins as rheomorphic proteins: interpretation of the primary and
secondary structures of the α S1 , β and κ-caseins. J Chem Soc Faraday Trans 89:2683–2692
59. Fox PF, Brodkorb A (2008) The casein micelle: historical aspects, current concepts and
significance. Int Dairy J 18:677–684
60. Moore SA, Anderson BF, Groom CR et al (1997) Three-dimensional structure of diferric
bovine lactoferrin at 2.8 A ˚ resolution. J Mol Biol 274(2):222–236
61. Baker EN (1994) Structure and reactivity of transferrins. Adv Inorg Chem 41:389–463
62. Baker EN, Baker HM (2009) A structural framework for understanding the multifunctional
character of lactoferrin. Biochimie 91(1):3–10
63. Spik G, Coddeville B, Mazurier J et al (1994) Primary and three-dimensional structure of
lactotransferrin (lactoferrin) glycans. Adv Exp Med Biol 357:21–32
64. Antonini G, Rossi P, Pitari G et al (2000) Role of glycan in bovine lactoferrin. In: Shimakaki
K, Tsuda H, Tomita M, Kuwata T, Perraudin JP (eds) Lactoferrin: structure, function and
applications. Elsevier Science, Amsterdam, pp 3–16
65. Rossi P, Giansanti F, Boffi A et al (2002) Ca
2+ Binding to bovine lactoferrin enhances protein
stability and influences the release of bacterial lipopolysaccharide. Biochem Cell Biol
80:41–48
66. Chaufer B, Rabiller-Baudry M, Lucas D et al (2000) Selective extraction of lysozyme from a
mixture with lactoferrin by ultrafiltration. Role of the physico-chemical environment. Lait
80:197–203
67. Mela I, Aumaitre E, Williamson A-M et al (2010) Charge reversal by salt-induced aggregation in aqueous lactoferrin solutions. Colloids Surf B 78(1):53–60
68. Wang J, Dauter M, Alkire H (2007) Triclinic lysozyme at 0.65 A ˚ resolution. Acta Cristallogr
D 63(12):1254–1268
69. Canfield RE, Liu AK (1965) The disulfide bonds of egg white lysozyme (muramidase). J Biol
Chem 240:1997–2002
Spontaneous Assembly and Induced Aggregation of Food Proteins
97
the stability of bovine α lactalbumin. Biophys Chem 84:27–34
46. Hiraoka Y, Secawa T, Kuwajima K et al (1980) α-Lactalbumin: a metalloprotein. Biochem
Biophys Res Commun 95(3):1098–1104
47. Bernal V, Jelen P (1984) Effect of calcium binding on thermal denaturation of bovine
α-lactalbumin. J Dairy Sci 67:2452–2454
48. DeWit JN, Klarenbeek G (1984) Effects of various heat treatments on structure and solubility
of whey proteins. J Dairy Sci 67:2701–2710
49. Griko YV, Remeta DP (1999) Energetics of solvent and ligand induced conformational
changes in α-lactalbumin. Protein Sci 8(3):554–561
50. Warner RC (1954) In: Neurath H, Bailey K (eds) The proteins, vol 2. Academic, New York,
p 443
51. Li Chan E, Nakai S (1989) Biochemical basis for the properties of egg white. Crit Rev Poult
Biol 2:21–57
52. Narita K, Ishii J (1962) N terminal sequence in ovalbumin. J Biochem (Tokyo) 52:367–373
53. Nisbet AD, Saundry RH, Moir AJ et al (1981) The complete amino acid sequence of hen
ovalbumin. Eur J Biochem 115:335–345
54. Stein PE, Leslie AG, Finch JT et al (1990) Crystal structure of ovalbumin as a model for the
reactive centre of serpins. Nature 347:99–102
55. Stein PE, Leslie AG, Finch JT et al (1991) Crystal structure of uncleaved ovalbumin at 1.95 A ˚
resolution. J Mol Biol 221:941–959
56. Matsumoto T, Chiba J, Inoue H (1992) Effect of pH on colloidal properties of native ovalbumin
aqueous systems. Colloid Polym Sci 270:687–693
57. Farrel HM Jr, Qi PX, Uversky VN (2006) New views of protein structure: applications to the
caseins: protein structure and functionality. In: Fishman ML, Qi PX, Wisker L (eds)
Advances in biopolymers: molecules, clusters, networks, and interactions. American Chemical Society, Washington, DC, pp 52–70
58. Holt C, Sawyer L (1993) Caseins as rheomorphic proteins: interpretation of the primary and
secondary structures of the α S1 , β and κ-caseins. J Chem Soc Faraday Trans 89:2683–2692
59. Fox PF, Brodkorb A (2008) The casein micelle: historical aspects, current concepts and
significance. Int Dairy J 18:677–684
60. Moore SA, Anderson BF, Groom CR et al (1997) Three-dimensional structure of diferric
bovine lactoferrin at 2.8 A ˚ resolution. J Mol Biol 274(2):222–236
61. Baker EN (1994) Structure and reactivity of transferrins. Adv Inorg Chem 41:389–463
62. Baker EN, Baker HM (2009) A structural framework for understanding the multifunctional
character of lactoferrin. Biochimie 91(1):3–10
63. Spik G, Coddeville B, Mazurier J et al (1994) Primary and three-dimensional structure of
lactotransferrin (lactoferrin) glycans. Adv Exp Med Biol 357:21–32
64. Antonini G, Rossi P, Pitari G et al (2000) Role of glycan in bovine lactoferrin. In: Shimakaki
K, Tsuda H, Tomita M, Kuwata T, Perraudin JP (eds) Lactoferrin: structure, function and
applications. Elsevier Science, Amsterdam, pp 3–16
65. Rossi P, Giansanti F, Boffi A et al (2002) Ca
2+ Binding to bovine lactoferrin enhances protein
stability and influences the release of bacterial lipopolysaccharide. Biochem Cell Biol
80:41–48
66. Chaufer B, Rabiller-Baudry M, Lucas D et al (2000) Selective extraction of lysozyme from a
mixture with lactoferrin by ultrafiltration. Role of the physico-chemical environment. Lait
80:197–203
67. Mela I, Aumaitre E, Williamson A-M et al (2010) Charge reversal by salt-induced aggregation in aqueous lactoferrin solutions. Colloids Surf B 78(1):53–60
68. Wang J, Dauter M, Alkire H (2007) Triclinic lysozyme at 0.65 A ˚ resolution. Acta Cristallogr
D 63(12):1254–1268
69. Canfield RE, Liu AK (1965) The disulfide bonds of egg white lysozyme (muramidase). J Biol
Chem 240:1997–2002
Spontaneous Assembly and Induced Aggregation of Food Proteins
97