94. Domike KR, Donald AM (2007) Thermal dependence of thermally induced protein spherulite
formation and growth: kinetics of β-lactoglobulin and insulin. Biomacromolecules
8:3930–3937
95. Bromley E, Krebs M, Donald A (2006) Mechanisms of structure formation in particulate gels
of β-lactoglobulin formed near the isoelectric point. Soft Matter 21:145–152
96. Krebs MRH, Devlin GL, Donald AM (2007) Protein particulates: another generic form of
protein aggregation? Biophys J 92:1336–1342
97. Bengoechea C, Peinado I, McClements DJ (2011) Formation of nanoparticles by controlled
heat treatment of lactoferrin: factors affecting particles characteristics. Food Hydrocolloid
25:1354–1360
98. Baussay K, Le Bon C, Nicolai T et al (2004) Influence of ionic strength on the heat-induced
aggregation of the globular protein β-lactoglobulin at pH 7.0. Int J Biol Macromol 34:21–28
99. Pouzot M, Nicolai T, Visschers RW et al (2005) X-ray and light scattering study of the
structure of large protein aggregates at neutral pH. Food Hydrocolloid 19:231–238
100. Donato L, Schmitt C, Bovetto L et al (2009) Mechanism of formation of stable heat-induced
β-lactoglobulin microgels. Int Dairy J 19:295–306
101. Le Bon C, Nicolaı ¨ T, Durand D (1999) Growth and structure of aggregates of heat-denatured
β-lactoglobulin. Int J Food Sci Technol 34:451–465
102. Mossa S, Sciortino F, Tartaglia P et al (2004) Ground-state clusters for short-range attractive
and lon-range repulsive potentials. Langmuir 20:10756–10763
103. Sun XS, Wang D, Zhang L et al (2008) Morpholgy and phase separation of hydrophobic
clusters of soy globular protein polymers. Macromol Biosci 2008:295–303
104. Zuniga RN, Tolkach A, Kulozik U et al (2010) Kinetics of formation and physicochemical
characterization of thermally-induced β-lactoglobulin aggregates. J Food Sci 75:E261–E268
105. Yu S, Yao P, Jiang M et al (2006) Nanogels prepared by self-assembly of oppositely charged
globular proteins. Biopolymers 83:148–158
106. Hu J, Yu S, Yao P (2007) Stable amphoteric nanogels made of ovalbumin and ovotransferrin
via self-assembly. Langmuir 23:6358–6364
107. Pan XY, Yu S, Yao P et al (2007) Self-assembly of β-casein and lysozyme. J Colloid Interface
Sci 316:405–412
108. Scanlon S, Aggeli A (2008) Self-assembling peptide nanotubes. Nano Today 3:22–30
109. Ipsen R, Otte J, Qvist KB (2001) Molecular self-assembly of partially hydrolysed α-lactalbumin resulting in strong gels with a novel microstructure. J Dairy Res 68:277–286
110. Ubbink J, Burbidge A, Mezzenga R (2008) Food structure and functionality: a soft matter
perspective. Soft Matter 4:1569–1581
111. Jones GO, McClements DJ (2011) Recent progress in biopolymer nanoparticle and microparticle formation by heat-treating electrostatic protein–polysaccharide complexes. Adv
Colloid Interfac 67:49–62
112. Schmitt C, Turgeon SL (2011) Protein/polysaccharide complexes and coacervates in food
systems. Adv Colloid Interface 167:63–70
113. Voets IK, de Keizer A, Cohen Stuart MA (2009) Complex coacervate core micelles. Adv
Colloid Interface 147–148:300–318
114. Becker AL, Henzler K, Welsch N et al (2012) Proteins and polyelectrolytes: a charged
relationship. Curr Opin Colloid Interface Sci 17:90–96
115. Sperber BLHM, Cohen Stuart MA, Schols HA et al (2010) Overall charge and local charge
density of pectin determines the enthalpic and entropic contributions to complexation with
β-lactoglobulin. Biomacromolecules 11:3578–3583
116. Ball V, Winterhalter M, Schwinte P et al (2002) Complexation mechanism of bovine serum
albumin and poly(allylamine hydrochloride). J Phys Chem B 106:2357–2364
117. Muthukumar M (1995) Pattern recognition by polyelectrolytes. J Chem Phys 103:4723–4731
118. Romanini D, Braia M, Angarte RG et al (2007) Interaction of lysozyme with negatively
charged flexible chain polymers. J Chromatogr B 857:25–31
Spontaneous Assembly and Induced Aggregation of Food Proteins
99
formation and growth: kinetics of β-lactoglobulin and insulin. Biomacromolecules
8:3930–3937
95. Bromley E, Krebs M, Donald A (2006) Mechanisms of structure formation in particulate gels
of β-lactoglobulin formed near the isoelectric point. Soft Matter 21:145–152
96. Krebs MRH, Devlin GL, Donald AM (2007) Protein particulates: another generic form of
protein aggregation? Biophys J 92:1336–1342
97. Bengoechea C, Peinado I, McClements DJ (2011) Formation of nanoparticles by controlled
heat treatment of lactoferrin: factors affecting particles characteristics. Food Hydrocolloid
25:1354–1360
98. Baussay K, Le Bon C, Nicolai T et al (2004) Influence of ionic strength on the heat-induced
aggregation of the globular protein β-lactoglobulin at pH 7.0. Int J Biol Macromol 34:21–28
99. Pouzot M, Nicolai T, Visschers RW et al (2005) X-ray and light scattering study of the
structure of large protein aggregates at neutral pH. Food Hydrocolloid 19:231–238
100. Donato L, Schmitt C, Bovetto L et al (2009) Mechanism of formation of stable heat-induced
β-lactoglobulin microgels. Int Dairy J 19:295–306
101. Le Bon C, Nicolaı ¨ T, Durand D (1999) Growth and structure of aggregates of heat-denatured
β-lactoglobulin. Int J Food Sci Technol 34:451–465
102. Mossa S, Sciortino F, Tartaglia P et al (2004) Ground-state clusters for short-range attractive
and lon-range repulsive potentials. Langmuir 20:10756–10763
103. Sun XS, Wang D, Zhang L et al (2008) Morpholgy and phase separation of hydrophobic
clusters of soy globular protein polymers. Macromol Biosci 2008:295–303
104. Zuniga RN, Tolkach A, Kulozik U et al (2010) Kinetics of formation and physicochemical
characterization of thermally-induced β-lactoglobulin aggregates. J Food Sci 75:E261–E268
105. Yu S, Yao P, Jiang M et al (2006) Nanogels prepared by self-assembly of oppositely charged
globular proteins. Biopolymers 83:148–158
106. Hu J, Yu S, Yao P (2007) Stable amphoteric nanogels made of ovalbumin and ovotransferrin
via self-assembly. Langmuir 23:6358–6364
107. Pan XY, Yu S, Yao P et al (2007) Self-assembly of β-casein and lysozyme. J Colloid Interface
Sci 316:405–412
108. Scanlon S, Aggeli A (2008) Self-assembling peptide nanotubes. Nano Today 3:22–30
109. Ipsen R, Otte J, Qvist KB (2001) Molecular self-assembly of partially hydrolysed α-lactalbumin resulting in strong gels with a novel microstructure. J Dairy Res 68:277–286
110. Ubbink J, Burbidge A, Mezzenga R (2008) Food structure and functionality: a soft matter
perspective. Soft Matter 4:1569–1581
111. Jones GO, McClements DJ (2011) Recent progress in biopolymer nanoparticle and microparticle formation by heat-treating electrostatic protein–polysaccharide complexes. Adv
Colloid Interfac 67:49–62
112. Schmitt C, Turgeon SL (2011) Protein/polysaccharide complexes and coacervates in food
systems. Adv Colloid Interface 167:63–70
113. Voets IK, de Keizer A, Cohen Stuart MA (2009) Complex coacervate core micelles. Adv
Colloid Interface 147–148:300–318
114. Becker AL, Henzler K, Welsch N et al (2012) Proteins and polyelectrolytes: a charged
relationship. Curr Opin Colloid Interface Sci 17:90–96
115. Sperber BLHM, Cohen Stuart MA, Schols HA et al (2010) Overall charge and local charge
density of pectin determines the enthalpic and entropic contributions to complexation with
β-lactoglobulin. Biomacromolecules 11:3578–3583
116. Ball V, Winterhalter M, Schwinte P et al (2002) Complexation mechanism of bovine serum
albumin and poly(allylamine hydrochloride). J Phys Chem B 106:2357–2364
117. Muthukumar M (1995) Pattern recognition by polyelectrolytes. J Chem Phys 103:4723–4731
118. Romanini D, Braia M, Angarte RG et al (2007) Interaction of lysozyme with negatively
charged flexible chain polymers. J Chromatogr B 857:25–31
Spontaneous Assembly and Induced Aggregation of Food Proteins
99