23. Lara C, Adamcik J, Jordens S et al (2011) General self-assembly mechanism converting
hydrolyzed globular proteins into giant multistranded amyloid ribbons. Biomacromolecules
12:1868–1875
24. Gummel J, Cousin F, Boue ´ F (2007) Counterions release from electrostatic complexes of
polyelectrolytes and proteins of opposite charge: a direct measurement. J Am Chem Soc
129:5806–5807
25. Semenova MG (2007) Thermodynamic analysis of the impact of molecular interactions on
the functionality of food biopolymers in solution and in colloidal systems. Food Hydrocolloid
21:23–45
26. Viney C (2004) Self-assembly as a route to fibrous materials: concepts, opportunities and
challenges. Curr Opin Solid State Mater Sci 8:95–101
27. Velikov KP, Pelan E (2008) Colloidal delivery systems for micronutrients and nutraceuticals.
Soft Matter 4:1964–1980
28. Gummel J, Boue ´ F, Clemens D et al (2008) Finite size and inner structure controlled by
electrostatic screening in globular complexes of proteins and polyelectrolytes. Soft Matter
4(8):1653–1664
29. Doubliez JL, Garnier C, Renard D et al (2000) Protein-polysaccharide interactions. Curr Opin
Colloid Interface Sci 5:202–214
30. de Kruif CG, Weinbreck F, de Vries R (2004) Complex coacervation of proteins and anionic
polysaccharides. Curr Opin Colloid Interface Sci 9:340–349
31. Cooper CL, Dubin PL, Kayitmazer AB et al (2005) Polyelectrolyte-protein complexes. Curr
Opin Colloid Interface Sci 10:52–78
32. de Vries R, Cohen Stuart M (2006) Theory and simulations of macroion complexation. Curr
Opin Colloid Interface Sci 11:295–301
33. Hales K, Pochan DJ (2006) Using polyelectrolyte block copolymers to tune nanostructure
assembly. Curr Opin Colloid Interface Sci 11:330–336
34. Turgeon SL, Schmitt C, Sanchez C (2007) Protein-polysaccharide complexes and
coacervates. Curr Opin Colloid Interface Sci 12(4–5):166–178
35. Jones GO, McClements DJ (2010) Functional biopolymer particles: design, fabrication, and
application. Compr Rev Food Sci Food Safety 9:374–397
36. Brownlow S, Cabral JHM, Cooper R et al (1997) Bovine β-lactoglobulin at 1.8 Angstrom
resolution – still an enigmatic lipocalin. Structure 5(4):481–495
37. Sawyer L, Kontopidis G (2000) The core lipocalin, bovine β-lactoglobulin. Biochem Biophys
Acta 1482:136–148
38. Kontopidis G, Holt G, Sawyer L (2002) The ligand-binding site of bovine β-lactoglobulin:
evidence for a function? J Mol Biol 318(4):1043–1055
39. Papiz MZ, Sawyer L, Eliopoulos EE et al (1986) The structure of beta-lactoglobulin and its
similarity to plasma retinol-binding protein. Nature 324:383–385
40. Kitabatake N, Wada R, Fujita Y (2001) Reversible conformational change in betalactoglobulin modified with N-ethylmaleimide and resistance to molecular aggregation on
heating. J Agric Food Chem 49:4011–4018
41. Jayat D, Gaudin JC, Chobert JM et al (2004) A recombinant C121S mutant of bovine
β-lactoglobulin is more susceptible to peptic digestion and to denaturation by reducing
agent and heating. Biochemistry 43:6312–6321
42. Qi XL, Holt C, Mcnulty D et al (1997) Effect of temperature on the secondary structure of
beta-lactoglobulin at pH 6.7, As determined by CD and IR spectroscopy: a test of the molten
globule hypothesis. Biochem J 324:341–346
43. Mattison KW, Dubin PL, Brittain IJ (1998) Complex formation between bovine serum
albumin and strong polyelectrolytes: effect of polymer charge density. J Phys Chem B
102:3830–3836
44. Brew K, Vanaman TC, Hill RL (1967) Comparison of the amino acid sequence of bovine
α-lactalbumin and hen egg white lysozyme. J Biol Chem 242:3747–3748
96
S. Bouhallab and T. Croguennec
hydrolyzed globular proteins into giant multistranded amyloid ribbons. Biomacromolecules
12:1868–1875
24. Gummel J, Cousin F, Boue ´ F (2007) Counterions release from electrostatic complexes of
polyelectrolytes and proteins of opposite charge: a direct measurement. J Am Chem Soc
129:5806–5807
25. Semenova MG (2007) Thermodynamic analysis of the impact of molecular interactions on
the functionality of food biopolymers in solution and in colloidal systems. Food Hydrocolloid
21:23–45
26. Viney C (2004) Self-assembly as a route to fibrous materials: concepts, opportunities and
challenges. Curr Opin Solid State Mater Sci 8:95–101
27. Velikov KP, Pelan E (2008) Colloidal delivery systems for micronutrients and nutraceuticals.
Soft Matter 4:1964–1980
28. Gummel J, Boue ´ F, Clemens D et al (2008) Finite size and inner structure controlled by
electrostatic screening in globular complexes of proteins and polyelectrolytes. Soft Matter
4(8):1653–1664
29. Doubliez JL, Garnier C, Renard D et al (2000) Protein-polysaccharide interactions. Curr Opin
Colloid Interface Sci 5:202–214
30. de Kruif CG, Weinbreck F, de Vries R (2004) Complex coacervation of proteins and anionic
polysaccharides. Curr Opin Colloid Interface Sci 9:340–349
31. Cooper CL, Dubin PL, Kayitmazer AB et al (2005) Polyelectrolyte-protein complexes. Curr
Opin Colloid Interface Sci 10:52–78
32. de Vries R, Cohen Stuart M (2006) Theory and simulations of macroion complexation. Curr
Opin Colloid Interface Sci 11:295–301
33. Hales K, Pochan DJ (2006) Using polyelectrolyte block copolymers to tune nanostructure
assembly. Curr Opin Colloid Interface Sci 11:330–336
34. Turgeon SL, Schmitt C, Sanchez C (2007) Protein-polysaccharide complexes and
coacervates. Curr Opin Colloid Interface Sci 12(4–5):166–178
35. Jones GO, McClements DJ (2010) Functional biopolymer particles: design, fabrication, and
application. Compr Rev Food Sci Food Safety 9:374–397
36. Brownlow S, Cabral JHM, Cooper R et al (1997) Bovine β-lactoglobulin at 1.8 Angstrom
resolution – still an enigmatic lipocalin. Structure 5(4):481–495
37. Sawyer L, Kontopidis G (2000) The core lipocalin, bovine β-lactoglobulin. Biochem Biophys
Acta 1482:136–148
38. Kontopidis G, Holt G, Sawyer L (2002) The ligand-binding site of bovine β-lactoglobulin:
evidence for a function? J Mol Biol 318(4):1043–1055
39. Papiz MZ, Sawyer L, Eliopoulos EE et al (1986) The structure of beta-lactoglobulin and its
similarity to plasma retinol-binding protein. Nature 324:383–385
40. Kitabatake N, Wada R, Fujita Y (2001) Reversible conformational change in betalactoglobulin modified with N-ethylmaleimide and resistance to molecular aggregation on
heating. J Agric Food Chem 49:4011–4018
41. Jayat D, Gaudin JC, Chobert JM et al (2004) A recombinant C121S mutant of bovine
β-lactoglobulin is more susceptible to peptic digestion and to denaturation by reducing
agent and heating. Biochemistry 43:6312–6321
42. Qi XL, Holt C, Mcnulty D et al (1997) Effect of temperature on the secondary structure of
beta-lactoglobulin at pH 6.7, As determined by CD and IR spectroscopy: a test of the molten
globule hypothesis. Biochem J 324:341–346
43. Mattison KW, Dubin PL, Brittain IJ (1998) Complex formation between bovine serum
albumin and strong polyelectrolytes: effect of polymer charge density. J Phys Chem B
102:3830–3836
44. Brew K, Vanaman TC, Hill RL (1967) Comparison of the amino acid sequence of bovine
α-lactalbumin and hen egg white lysozyme. J Biol Chem 242:3747–3748
96
S. Bouhallab and T. Croguennec