References
1. Graveland-Bikker JF, Ipsen R, Otte J et al (2004) Influence of calcium on the self-assembly of
partially hydrolyzed α-lactalbumin. Langmuir 20:6841–6846
2. Graveland-Bikker JF, de Kruifs CG (2006) Unique milk protein based nanotubes: food and
nanotechnology meet. Trends Food Sci Technol 17:196–203
3. Nigen M, Croguennec T, Renard D et al (2007) Temperature affects the supramolecular
structures resulting from alpha-lactalbumin-lysozyme interaction. Biochemistry
46:1248–1255
4. Ipsen R, Otte J (2007) Self-assembly of partially hydrolysed alpha-lactalbumin. Biotechnol
Adv 25:602–605
5. Desfouge `res Y, Croguennec T, Lechevalier V et al (2010) Charge and size drive spontaneous
self-assembly of oppositely charged globular proteins into microspheres. J Phys Chem
114:4138–4144
6. Zhang S (2003) Fabrication of novel biomaterials through molecular self-assembly. Nat
Biotechnol 21(10):1171–1178
7. Donald AM (2008) Aggregation in β-lactoglobulin. Soft Matter 4:1147–1150
8. Krebs MRH, Domike KR, Cannon D et al (2008) Common motif in protein self-assembly.
Faraday Discuss 139:265–274
9. Dickinson E, Semenova MG, Belyakova LE et al (2001) Analysis of light scattering data on
the calcium ion sensitivity of caseinate solution thermodynamics: relationship to emulsion
flocculation. J Colloid Interface Sci 239(1):87–97
10. Unterhaslberger G, Schmitt C, Sanchez C et al (2006) Heat denaturation and aggregation of
beta-lacto globulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl
at pH 4.0 and 7.0. Food Hydrocolloid 20:1006–1019
11. Yang F Jr, Zhang M, Zhou BR et al (2006) Oleic acid inhibits amyloid formation of the
intermediate of alpha-lactalbumin at moderately acidic pH. J Mol Biol 362:821–834
12. Nigen M, Croguennec T, Bouhallab S (2009) Formation and stability of alpha-lactalbuminlysozyme spherical particles: involvement of electrostatic forces. Food Hydrocolloid
23:510–518
13. Thorn DC, Meehan S, Sunde M et al (2005) Amyloid fibril formation by bovine milk k-casein
and its inhibition by the molecular chaperones αs- and β-casein. Biochemistry 44:17027–17036
14. Le ´onil J, Henry G, Jouanneau D et al (2008) Kinetics of fibril formation of bovine κ-casein
indicate a conformational rearrangement as a critical step in the process. J Mol Biol
381:1267–1280
15. Schmitt C, Bovay C, Vuilliomenet A-M et al (2011) Influence of protein and mineral
composition on the formation of whey protein heat-induced microgels. Food Hydrocolloid
25:558–567
16. Keskin O, Gursoy A, Ma B (2008) Principles of protein-protein interactions: what are the
preferred ways for proteins to interact? Chem Rev 108(4):1225–1244
17. Min Y, Akbulut M, Kristiansen K et al (2008) The role of interparticle and external forces in
nanoparticle assembly. Nat Mater 7:527–538
18. Krebs MRH, Wilkins DK, Chung EW et al (2000) Formation and seeding of amyloid fibrils
from wild-type hen lysozyme and a peptide fragment from the β-domain. J Mol Biol
300:541–549
19. Gosal WS, Clark AH, Pudney (2002) Novel amyloid fibrillar networks derived from a
globular protein: β-lactoglobulin. Langmuir 18:7174–7181
20. Gosal WS, Clark AH, Ross-Murphy SB (2004) Fibrillar β-lactoglobulin gels: part 1: fibril
formation and structure. Biomacromolecules 5:2408–2419
21. Rasmussen P, Barbiroli A, Bonomi et al (2007) Formation of structured polymers upon
controlled denaturation of β-lactoglobulin with different chaotropes. Biopolymers 86:57–72
22. Akkermans C, van der Goot AJ, Venema P et al (2007) Micrometer-sized fibrillar protein
aggregates from soy glycinin and soy protein isolate. J Agric Food Chem 55:9877–9882
Spontaneous Assembly and Induced Aggregation of Food Proteins
95
1. Graveland-Bikker JF, Ipsen R, Otte J et al (2004) Influence of calcium on the self-assembly of
partially hydrolyzed α-lactalbumin. Langmuir 20:6841–6846
2. Graveland-Bikker JF, de Kruifs CG (2006) Unique milk protein based nanotubes: food and
nanotechnology meet. Trends Food Sci Technol 17:196–203
3. Nigen M, Croguennec T, Renard D et al (2007) Temperature affects the supramolecular
structures resulting from alpha-lactalbumin-lysozyme interaction. Biochemistry
46:1248–1255
4. Ipsen R, Otte J (2007) Self-assembly of partially hydrolysed alpha-lactalbumin. Biotechnol
Adv 25:602–605
5. Desfouge `res Y, Croguennec T, Lechevalier V et al (2010) Charge and size drive spontaneous
self-assembly of oppositely charged globular proteins into microspheres. J Phys Chem
114:4138–4144
6. Zhang S (2003) Fabrication of novel biomaterials through molecular self-assembly. Nat
Biotechnol 21(10):1171–1178
7. Donald AM (2008) Aggregation in β-lactoglobulin. Soft Matter 4:1147–1150
8. Krebs MRH, Domike KR, Cannon D et al (2008) Common motif in protein self-assembly.
Faraday Discuss 139:265–274
9. Dickinson E, Semenova MG, Belyakova LE et al (2001) Analysis of light scattering data on
the calcium ion sensitivity of caseinate solution thermodynamics: relationship to emulsion
flocculation. J Colloid Interface Sci 239(1):87–97
10. Unterhaslberger G, Schmitt C, Sanchez C et al (2006) Heat denaturation and aggregation of
beta-lacto globulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl
at pH 4.0 and 7.0. Food Hydrocolloid 20:1006–1019
11. Yang F Jr, Zhang M, Zhou BR et al (2006) Oleic acid inhibits amyloid formation of the
intermediate of alpha-lactalbumin at moderately acidic pH. J Mol Biol 362:821–834
12. Nigen M, Croguennec T, Bouhallab S (2009) Formation and stability of alpha-lactalbuminlysozyme spherical particles: involvement of electrostatic forces. Food Hydrocolloid
23:510–518
13. Thorn DC, Meehan S, Sunde M et al (2005) Amyloid fibril formation by bovine milk k-casein
and its inhibition by the molecular chaperones αs- and β-casein. Biochemistry 44:17027–17036
14. Le ´onil J, Henry G, Jouanneau D et al (2008) Kinetics of fibril formation of bovine κ-casein
indicate a conformational rearrangement as a critical step in the process. J Mol Biol
381:1267–1280
15. Schmitt C, Bovay C, Vuilliomenet A-M et al (2011) Influence of protein and mineral
composition on the formation of whey protein heat-induced microgels. Food Hydrocolloid
25:558–567
16. Keskin O, Gursoy A, Ma B (2008) Principles of protein-protein interactions: what are the
preferred ways for proteins to interact? Chem Rev 108(4):1225–1244
17. Min Y, Akbulut M, Kristiansen K et al (2008) The role of interparticle and external forces in
nanoparticle assembly. Nat Mater 7:527–538
18. Krebs MRH, Wilkins DK, Chung EW et al (2000) Formation and seeding of amyloid fibrils
from wild-type hen lysozyme and a peptide fragment from the β-domain. J Mol Biol
300:541–549
19. Gosal WS, Clark AH, Pudney (2002) Novel amyloid fibrillar networks derived from a
globular protein: β-lactoglobulin. Langmuir 18:7174–7181
20. Gosal WS, Clark AH, Ross-Murphy SB (2004) Fibrillar β-lactoglobulin gels: part 1: fibril
formation and structure. Biomacromolecules 5:2408–2419
21. Rasmussen P, Barbiroli A, Bonomi et al (2007) Formation of structured polymers upon
controlled denaturation of β-lactoglobulin with different chaotropes. Biopolymers 86:57–72
22. Akkermans C, van der Goot AJ, Venema P et al (2007) Micrometer-sized fibrillar protein
aggregates from soy glycinin and soy protein isolate. J Agric Food Chem 55:9877–9882
Spontaneous Assembly and Induced Aggregation of Food Proteins
95