Design of whey protein nanostructures for incorporation and release of nutraceutical compounds in food

References

• Akkermans, C., Venema, P., van der Goot, A. J., Gruppen, H. and Bakx, E. J. (2008). Peptides are building blocks of heatinduced fibrillar protein aggregates of β-lactoglobulin formed at pH 2. Biomacromolecules 9:1474–1479.
   PubMed Web of Science ®Google Scholar
• Arnaudov, L. N., de Vries, R., Ippel, H. and van Mierlo, C. P. M. (2003). Multiple steps during the formation of β-lactoglobulin fibrils. Biomacromolecules 4:1614–1622.
   PubMed Web of Science ®Google Scholar
• Authority, E. F. S. (2009). Scientific opinion of the scientific committee on a request from the European commission on the potential risks arising from nanoscience and nanotechnologies on food and feed safety. The EFSA Journal 058:1–39.
   Google Scholar
• Balandrán-Quintana, R. R., Valdéz-Covarrubias, M. A., Mendoza-Wilson, A. M. and Sotelo-Mundo, R. R. (2013). α-Lactalbumin hydrolysate spontaneously produces disk-shaped nanoparticles. Int. Dairy J. 32:133–135.
   Web of Science ®Google Scholar
• Ballister, E. R., Lai, A. H., Zuckermann, R. N., Cheng, Y. and Mougous, J. D. (2008). In vitro self-assembly of tailorable nanotubes from a simple protein building block. Proc. Natl. Acad. Sci. U.S.A. 105:3733–3738.
   PubMed Web of Science ®Google Scholar
• Banik, S., Bandyopadhyay, S. and Ganguly, S. (2003). Bioeffects of microwave—a brief review. Bioresour. Technol. 87:155–159.
   PubMed Web of Science ®Google Scholar
• Bateman, L., Ye, A. and Singh, H. (2010). In vitro digestion of beta-lactoglobulin fibrils formed by heat treatment at low pH. J. Agric. Food Chem. 58:9800–9808.
   PubMed Web of Science ®Google Scholar
• Bengoechea, C., Jones, O. G., Guerrero, A. and McClements, D. J. (2011). Formation and characterization of lactoferrin/pectin electrostatic complexes: Impact of composition, pH and thermal treatment. Food Hydrocolloids 25:1227–1232.
   Web of Science ®Google Scholar
• Betz, S. F. (1993). Disulfide bonds and the stability of globular-proteins. Protein Sci. 2:1551–1558.
   PubMed Web of Science ®Google Scholar
• Bodnár, I., Alting, A. C. and Verschueren, M. (2007). Structural effects on the permeability of whey protein films in an aqueous environment. Food Hydrocolloids 21:889–895.
   Web of Science ®Google Scholar
• Bolder, S. G., Hendrickx, H., Sagis, L. and van der Linden, E. (2006a). Ca2+-induced cold-set gelation of whey protein isolate fibrils. Appl. Rheol. 16:258–264.
   Web of Science ®Google Scholar
• Bolder, S. G., Hendrickx, H., Sagis, L. M. C. and van der Linden, E. (2006b). Fibril assemblies in aqueous whey protein mixtures. J. Agric. Food Chem. 54:4229–4234.
   PubMed Web of Science ®Google Scholar
• Bolder, S. G., Vasbinder, A. J., Sagis, L. M. C. and van der Linden, E. (2007). Heat-induced whey protein isolate fibrils: Conversion, hydrolysis, and disulphide bond formation. Int. Dairy J. 17:846–853.
   Web of Science ®Google Scholar
• Bolisetty, S., Harnau, L., Jung, J.-m. and Mezzenga, R. (2012). Gelation, phase behavior, and dynamics of β-lactoglobulin amyloid fibrils at varying concentrations and ionic strengths. Biomacromolecules 13:3241–3252.
   PubMed Web of Science ®Google Scholar
• Bouhallab, S. and Croguennec, T. (2014). Spontaneous assembly and induced aggregation of food proteins. In: Polyelectrolyte Complexes in the Dispersed and Solid State II, pp. 67–101. Müller, M., Ed., Springer, Berlin Heidelberg.
   Google Scholar
• Bouwmeester, H., Dekkers, S., Noordam, M. Y., Hagens, W. I., Bulder, A. S., de Heer, C., ten Voorde, S. E. C. G., Wijnhoven, S. W. P., Marvin, H. J. P. and Sips, A. J. A. M. (2009). Review of health safety aspects of nanotechnologies in food production. Regul. Toxicol. Pharm. 53:52–62.
   PubMed Web of Science ®Google Scholar
• Brown, A. W. (2014). Human nutrition | nutraceuticals. In: Encyclopedia of Meat Sciences, 2nd ed., pp. 130–134. Dikeman, M. and Devine, C., Eds., Academic Press, Oxford.
   Google Scholar
• Bryant, C. M. and McClements, D. J. (1998). Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey. Trends Food Sci. Technol. 9:143–151.
   Web of Science ®Google Scholar
• Castro, A. J., Swanson, B. G. and Barbosa-Cánovas, G. V. (2001). Pulsed electric field modification of milk alkaline phosphatase activity. In: Electric Fields in Food Processing, pp. 65–82. Barbosa-Cánovas, G. V. and Zhang, Q. H., Eds., Technomic, Lancaster, PA.
   Google Scholar
• Cencic, A. and Chingwaru, W. (2010). The Role of Functional Foods, Nutraceuticals, and Food Supplements in Intestinal Health. Nutrients 2:611–625.
   PubMed Web of Science ®Google Scholar
• Cerqueira, M., Pinheiro, A., Silva, H., Ramos, P., Azevedo, M., Flores-López, M., Rivera, M., Bourbon, A., Ramos, Ó. and Vicente, A. (2014). Design of bio-nanosystems for oral delivery of functional compounds. Food. Eng. Rev. 6:1–19.
   Web of Science ®Google Scholar
• Chau, C.-F., Wu, S.-H. and Yen, G.-C. (2007). The development of regulations for food nanotechnology. Trends Food Sci. Technol. 18:269–280.
   Web of Science ®Google Scholar
• Chaudhry, Q., Watkins, R. and Castle, L. (2010). Nanotechnologies in the food arena: New opportunities, new questions, new concerns. In: Nanotechnologies in Food, pp. 1–17. Chaudhry, Q., Castle, L. and Watkins, R., Eds., Royal Society of Chemistry.
   Google Scholar
• Chen, G., Wang, H., Zhang, X. and Yang, S.-T. (2014). Nutraceuticals and functional foods in the management of hyperlipidemia. Crit. Rev. Food Sci. Nutr. 54:1180–1201.
   PubMed Web of Science ®Google Scholar
• Chen, H. (1995). Functional properties and applications of edible films made of milk proteins. J. Dairy Sci. 78:2563–2583.
   PubMed Web of Science ®Google Scholar
• Chen, L., Remondetto, G. E. and Subirade, M. (2006). Food protein-based materials as nutraceutical delivery systems. Trends Food Sci. Technol. 17:272–283.
   Web of Science ®Google Scholar
• Chen, L. Y. and Subirade, M. (2006). Alginate-whey protein granular microspheres as oral delivery vehicles for bioactive compounds. Biomaterials 27:4646–4654.
   PubMed Web of Science ®Google Scholar
• Cho, Y., Singh, H. and Creamer, L. K. (2003). Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system. J. Dairy Res. 70:61–67.
   PubMed Web of Science ®Google Scholar
• Cockburn, A., Bradford, R., Buck, N., Constable, A., Edwards, G., Haber, B., Hepburn, P., Howlett, J., Kampers, F., Klein, C., Radomski, M., Stamm, H., Wijnhoven, S. and Wildemann, T. (2012). Approaches to the safety assessment of engineered nanomaterials (ENM) in food. Food Chem. Toxicol. 50:2224–2242.
   PubMed Web of Science ®Google Scholar
• Commission, E. (2013). Nanotechnology: the invisible giant tackling Europe's future challenges.
   Google Scholar
• Corredig, M. and Dalgleish, D. G. (1996). Effect of temperature and pH on the interactions of whey proteins with casein micelles in skim milk. Food Res. Int. 29:49–55.
   Web of Science ®Google Scholar
• Cramariuc, R., Donescu, V., Popa, M. and Cramariuc, B. (2005). The biological effect of the electrical field treatment on the potato seed: agronomic evaluation. J. Electrostat. 63:837–846.
   Web of Science ®Google Scholar
• Croguennec, T., O'Kennedy, B. T. and Mehra, R. (2004). Heat-induced denaturation/aggregation of beta-lactoglobulin A and B: kinetics of the first intermediates formed. Int. Dairy J. 14:399–409.
   Web of Science ®Google Scholar
• Dave, A. C., Loveday, S. M., Anema, S. G., Loo, T. S., Norris, G. E., Jameson, G. B. and Singh, H. (2013). β-Lactoglobulin self-assembly: Structural changes in early stages and disulfide bonding in fibrils. J. Agric. Food Chem. 61:7817–7828.
   PubMed Web of Science ®Google Scholar
• de la Fuente, M. A., Singh, H. and Hemar, Y. (2002). Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins. Trends Food Sci. Technol. 13:262–274.
   Web of Science ®Google Scholar
• de Pomerai, D. I., Smith, B., Dawe, A., North, K., Smith, T., Archer, D. B., Duce, I. R., Jones, D. and Candido, E. P. M. (2003). Microwave radiation can alter protein conformation without bulk heating. FEBS Lett. 543:93–97.
   PubMed Web of Science ®Google Scholar
• De Volder, M. F., Tawfick, S. H., Baughman, R. H. and Hart, A. J. (2013). Carbon nanotubes: present and future commercial applications. Science 339:535–539.
   PubMed Web of Science ®Google Scholar
• De Wit, J. N. (1990). Thermal stability and functionality of whey proteins. J. Dairy Sci. 73:3602–3612.
   Web of Science ®Google Scholar
• de Wit, J. N. (1998). Nutritional and functional characteristics of whey proteins in food products. J. Dairy Sci. 81:597–608.
   PubMed Web of Science ®Google Scholar
• Debeaufort, F., Quezada-Gallo, J. A. and Voilley, A. (1998). Edible films and coatings: Tomorrow's packagings: A review. Crit. Rev. Food Sci. Nutr. 38:299–313.
   PubMed Web of Science ®Google Scholar
• Dickinson, E. (2003). Colloidal aggregation: Mechanism and implications. In: Food Colloids, Biopolymers and Materials, pp. 68–83. Dickinson, E., Vlie, T. van, Ed., Royal Society of Chemistry, Cambridge.
   Google Scholar
• Dissanayake, M. and Vasiljevic, T. (2009). Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing. J. Dairy Sci. 92:1387–1397.
   PubMed Web of Science ®Google Scholar
• Dobson, C. M. (2003). Protein folding and misfolding. Nature 426:884–890.
   PubMed Web of Science ®Google Scholar
• Doi, E. (1993). Gels and gelling of globular proteins. Trends Food Sci. Technol. 4:1–5.
   Web of Science ®Google Scholar
• Domike, K. R., Hardin, E., Armstead, D. N. and Donald, A. M. (2009). Investigating the inner structure of irregular \beta -lactoglobulin spherulites. Eur. Phys. J. E 29:173–182.
   PubMed Web of Science ®Google Scholar
• Dumay, E. M., Kalichevsky, M. T. and Cheftel, J. C. (1998). Characteristics of pressure-induced gels of β-lactoglobulin at various times after pressure release. LWT-Food Sci. Technol. 31:10–19.
   Web of Science ®Google Scholar
• EC, 2013. Nanotechnology: the Invisible Giant Tackling Europe's Future Challenges (1–44). Brussels: European Commission. ISBN 978-92-79-28892-0; doi:10.2777/62323.
   Google Scholar
• Edwards, P. J. B. and Jameson, G. B. (2014). Chapter 7 - Structure and stability of whey proteins. In: Milk Proteins, 2nd ed., pp. 201–242. Singh, H., Boland, M. and Thompson, A., Eds., Academic Press, San Diego.
   Google Scholar
• Elfagm, A. A. and Wheelock, J. V. (1978). Heat interaction between α-lactalbumin, β-lactoglobulin and casein in bovine milk. J. Dairy Sci. 61:159–163.
   Web of Science ®Google Scholar
• Esmaeilzadeh, P., Fakhroueian, Z., Esmaeilzadeh, P. and Mohammadi, N. (2013). Synthesis and characterization of various protein α-lactalbumin nanotubes structures by chemical hydrolysis method. ANP. 2:154–164.
   Google Scholar
• Famelart, M.-H., Tomazewski, J., Piot, M. and Pezennec, S. (2003). Comparison of rheological properties of acid gels made from heated casein combined with β-lactoglobulin or egg ovalbumin. Int. Dairy J. 13:123–134.
   Web of Science ®Google Scholar
• Feng, W. and Ji, P. (2011). Enzymes immobilized on carbon nanotubes. Biotechnol. Adv. 29:889–895.
   PubMed Web of Science ®Google Scholar
• Ferry, J. D. (1948). Protein gels. Adv. Protein Chem. 4:1–76.
   PubMedGoogle Scholar
• Filipcsei, G., Csetneki, I., Szilágyi, A. and Zrínyi, M. (2007). Magnetic field-responsive smart polymer composites. In: Oligomers—Polymer Composites—Molecular Imprinting, 137–189. Springer Berlin Heidelberg.
   Google Scholar
• Foegeding, E. A. (2006). Food biophysics of protein gels: A challenge of nano and macroscopic proportions. Food Biophys. 1:41–50.
   Web of Science ®Google Scholar
• Foegeding, E. A. and Davis, J. P. (2011). Food protein functionality: A comprehensive approach. Food Hydrocolloid. 25:1853–1864.
   Web of Science ®Google Scholar
• Giroux, H. J. and Britten, M. (2011). Encapsulation of hydrophobic aroma in whey protein nanoparticles. J. Microencapsulation 28:337–343.
   PubMed Web of Science ®Google Scholar
• Goers, J., Permyakov, S. E., Permyakov, E. A., Uversky, V. N. and Fink, A. L. (2002). Conformational prerequisites for α-Lactalbumin fibrillation†. Biochemistry 41:12546–12551.
   PubMed Web of Science ®Google Scholar
• Gomaa, A. I., Sedman, J. and Ismail, A. A. (2013). An investigation of the effect of microwave treatment on the structure and unfolding pathways of β-lactoglobulin using FTIR spectroscopy with the application of two-dimensional correlation spectroscopy (2D-COS). Vib. Spectrosc. 65:101–109.
   Web of Science ®Google Scholar
• Gosal, W. S., Clark, A. H. and Ross-Murphy, S. B. (2004). Fibrillar β-lactoglobulin gels: Part 1. Fibril formation and structure. Biomacromolecules 5:2408–2419.
   PubMed Web of Science ®Google Scholar
• Gounga, M. E., Xu, S.-Y. and Wang, Z. (2007). Whey protein isolate-based edible films as affected by protein concentration, glycerol ratio and pullulan addition in film formation. J. Food Eng. 83:521–530.
   Web of Science ®Google Scholar
• Graveland-Bikker, J. F. (2005). Self-Assembly of Hydrolysis α-Lactalbumin into Nanotubes. PhD, Utrecht University: The Netherlands.
   Google Scholar
• Graveland-Bikker, J. F. and de Kruif, C. G. (2006). Unique milk protein based nanotubes: Food and nanotechnology meet. Trends Food Sci. Technol. 17:196–203.
   Web of Science ®Google Scholar
• Graveland-Bikker, J. F., Ipsen, R., Otte, J. and de Kruif, C. G. (2004). Influence of calcium on the self-assembly of partially hydrolyzed alpha-lactalbumin. Langmuir. 20:6841–6846.
   PubMed Web of Science ®Google Scholar
• Guilmineau, F. and Kulozik, U. (2006). Impact of a thermal treatment on the emulsifying properties of egg yolk. Part 2: Effect of the environmental conditions. Food Hydrocolloids 20:1114–1123.
   Web of Science ®Google Scholar
• Gülseren, İ., Fang, Y. and Corredig, M. (2012a). Whey protein nanoparticles prepared with desolvation with ethanol: Characterization, thermal stability and interfacial behavior. Food Hydrocolloids 29:258–264.
   Web of Science ®Google Scholar
• Gülseren, İ., Fang, Y. and Corredig, M. (2012b). Zinc incorporation capacity of whey protein nanoparticles prepared with desolvation with ethanol. Food Chem. 135:770–774.
   PubMed Web of Science ®Google Scholar
• Gunasekaran, S., Ko, S. and Xiao, L. (2007). Use of whey proteins for encapsulation and controlled delivery applications. J. Food Eng. 83:31–40.
   Web of Science ®Google Scholar
• Gunasekaran, S., Xiao, L. and Ould Eleya, M. M. (2006). Whey protein concentrate hydrogels as bioactive carriers. J. Appl. Polym. Sci. 99:2470–2476.
   Web of Science ®Google Scholar
• Gyarmati, B., Némethy, Á. and Szilágyi, A. (2013). Reversible disulphide formation in polymer networks: A versatile functional group from synthesis to applications. Eur. Polym. J. 49:1268–1286.
   Web of Science ®Google Scholar
• Hennink, W. E. and van Nostrum, C. F. (2002). Novel crosslinking methods to design hydrogels. Adv. Drug Delivery Rev. 54:13–36.
   PubMed Web of Science ®Google Scholar
• Hoare, T. R. and Kohane, D. S. (2008). Hydrogels in drug delivery: Progress and challenges. Polymer 49:1993–2007.
   Web of Science ®Google Scholar
• Hoffman, A. S. (2002). Hydrogels for biomedical applications. Adv. Drug Delivery Rev. 54:3–12.
   PubMed Web of Science ®Google Scholar
• Hoffmann, M. A. M. and van Mil, P. J. J. M. (1997). Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulfide bonds. J. Agric. Food Chem. 45:2942–2948.
   Web of Science ®Google Scholar
• Huang, G., Gao, J., Hu, Z., St John, J. V., Ponder, B. C. and Moro, D. (2004). Controlled drug release from hydrogel nanoparticle networks. J. Control Release 94:303–311.
   PubMed Web of Science ®Google Scholar
• Huffman, L. M. (1996). Processing whey protein for use as a food ingredient. Food Technol. 50:49–52.
   Web of Science ®Google Scholar
• Huppertz, T., Fox, P. F., de Kruif, K. G. and Kelly, A. L. (2006). High pressure-induced changes in bovine milk proteins: A review. BBA-Proteins Proteom. 1764:593–598.
   PubMed Web of Science ®Google Scholar
• Ikeda, S. and Morris, V. J. (2002). Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy. Biomacromolecules 3:382–389.
   PubMed Web of Science ®Google Scholar
• Ipsen, R. and Otte, J. (2007). Self-assembly of partially hydrolysed alpha-lactalbumin. Biotechnol Adv. 25:602–605.
   PubMed Web of Science ®Google Scholar
• Ipsen, R., Otte, J. and Qvist, K. B. (2001). Molecular self-assembly of partially hydrolysed alpha-lactalbumin resulting in strong gels with a novel microstructure. J. Dairy Res. 68:277–286.
   PubMed Web of Science ®Google Scholar
• Jaeger, H., Reineke, K., Schoessler, K. and Knorr, D. (2012). Effects of Emerging Processing Technologies on Food Material Properties, In: Food Materials Science and Engineering (pp. 222–262). Bhandari, B. and Roos, Y. H. Eds. Wiley-Blackwell: Oxford, UK.
   Google Scholar
• Jo, C., Kang, H., Lee, N. Y., Kwon, J. H. and Byun, M. W. (2005). Pectin- and gelatin-based film: effect of gamma irradiation on the mechanical properties and biodegradation. Radiat. Phys. Chem. 72:745–750.
   Web of Science ®Google Scholar
• Jovanovic, S., Barac, M., Macej, O., Vucic, T. and Lacnjevac, C. (2007). SDS-PAGE Analysis of soluble proteins in reconstituted milk exposed to different heat treatments. Sensors 7:371–383.
   Web of Science ®Google Scholar
• Karshikoff, A. (2006a). Electrostatic interactions. In: Non-Covalent Interactions in Proteins, pp. 129–176. Karshikoff, A. Ed. Imperial College Press, London, UK.
   Google Scholar
• Karshikoff, A. (2006b). Electrostatic interactions and stability of proteins. In: Non-Covalent Interactions in Proteins, pp. 255–282. Karshikoff, A. Ed. Imperial College Press, London, UK.
   Google Scholar
• Karshikoff, A. (2006c). Hydrophobic interactions. In: Non-Covalent Interactions in Proteins, pp. 91–128. Karshikoff, A. Ed, Imperial College Press, London, UK.
   Google Scholar
• Karshikoff, A. (2006d). Non-Covalent Interactions in Proteins (Vol.). Imperial College Press, London.
   Google Scholar
• Kavanagh, G. M., Clark, A. H. and Ross-Murphy, S. B. (2000). Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH β-lactoglobulin gels. Int. J. Biol. Macromol. 28:41–50.
   PubMed Web of Science ®Google Scholar
• Kaya-Celiker, H. and Mallikarjunan, K. (2012). Better Nutrients and therapeutics delivery in food through nanotechnology. Food. Eng. Rev. 4:114–123.
   Web of Science ®Google Scholar
• Kinsella, J. E. and Whitehead, D. M. (1989). Proteins in whey: chemical, physical, and functional properties. Adv. Food Nutr. Res. 33:343–438.
   PubMedGoogle Scholar
• Kitabatake, N., Wada, R. and Fujita, Y. (2001). Reversible conformational change in beta-lactoglobulin A modified with N-ethylmaleimide and resistance to molecular aggregation on heating. J. Agric. Food Chem. 49:4011–4018.
   PubMed Web of Science ®Google Scholar
• Kopeček, J. (2003). Smart and genetically engineered biomaterials and drug delivery systems. Eur. J. Pharm. Sci. 20:1–16.
   PubMed Web of Science ®Google Scholar
• Lara, C. C., Adamcik, J., Jordens, S. and Mezzenga, R. (2011). General self-assembly mechanism converting hydrolyzed globular proteins into giant multistranded amyloid ribbons. Biomacromolecules 12:1868–1875.
   PubMed Web of Science ®Google Scholar
• Leadley, C. (2008). Novel commercial preservation methods. In: Food Biodeterioration and Preservation, pp. 211–244. Tucker, G. S. Ed. Blackwell Publishing Ltd: Oxford, UK.
   Google Scholar
• Lefèvre, T. and Subirade, M. (2000). Molecular differences in the formation and structure of fine-stranded and particulate β-lactoglobulin gels. Biopolymers 54:578–586.
   PubMed Web of Science ®Google Scholar
• Li, B., Du, W., Jin, J. and Du, Q. (2012). Preservation of (−)-epigallocatechin-3-gallate antioxidant properties loaded in heat treated β-lactoglobulin nanoparticles. J. Agric. Food Chem. 60:3477–3484.
   PubMed Web of Science ®Google Scholar
• Lin, C.-C. and Metters, A. T. (2006). Hydrogels in controlled release formulations: Network design and mathematical modeling. Adv. Drug Delivery Rev. 58:1379–1408.
   PubMed Web of Science ®Google Scholar
• Liu, F. and Urban, M. W. (2010). Recent advances and challenges in designing stimuli-responsive polymers. Prog. Polym. Sci. 35:3–23.
   Web of Science ®Google Scholar
• Liu, G. and Zhong, Q. (2013). Dispersible and thermal stable nanofibrils derived from glycated whey protein. Biomacromolecules 14:2146–2153.
   PubMed Web of Science ®Google Scholar
• Livney, Y. D. (2010). Milk proteins as vehicles for bioactives. Curr. Opin. Colloid Interface Sci. 15:73–83.
   Web of Science ®Google Scholar
• Livney, Y. D. (2012). Biopolymeric amphiphiles and their assemblies as functional food ingredients and nutraceutical delivery systems. In: Encapsulation Technologies and Delivery Systems for Food Ingredients and Nutraceuticals, pp. 252–273. Garti, N. and McClements, D. J., Eds., Woodhead Publishing: Cambridge UK.
   Google Scholar
• Livney, Y. D. and Dalgleish, D. G. (2004). Specificity of disulfide bond formation during thermal aggregation in solutions of β-Lactoglobulin B and κ-casein A. J. Agric. Food Chem. 52:5527–5532.
   PubMed Web of Science ®Google Scholar
• Lopez-Fandiño, R., Carrascosa, A. V. and Olano, A. (1996). The effects of high pressure on whey protein denaturation and cheese-making properties of raw milk. J. Dairy Sci. 79:929–936.
   Web of Science ®Google Scholar
• Loveday, S. M., Rao, M. A., Creamer, L. K. and Singh, H. (2009). Factors affecting rheological characteristics of fibril gels: the case of beta-lactoglobulin and alpha-lactalbumin. J. Food Sci. 74:R47–55.
   PubMed Web of Science ®Google Scholar
• Loveday, S. M., Rao, M. A. and Singh, H. (2012a). Food protein nanoparticles: Formation, properties and applications. In: Food Materials Science and Engineering, pp. 263–294. Bhandari B. and Roos Y. H. Eds. pp. 222–262. Wiley-Blackwell: Oxford, UK.
   Google Scholar
• Loveday, S. M., Su, J., Rao, M. A., Anema, S. G. and Singh, H. (2011). Effect of calcium on the morphology and functionality of whey protein nanofibrils. Biomacromolecules 12:3780–3788.
   PubMed Web of Science ®Google Scholar
• Loveday, S. M., Wang, X. L., Rao, M. A., Anema, S. G., Creamer, L. K. and Singh, H. (2010). Tuning the properties of β-lactoglobulin nanofibrils with pH, NaCl and CaCl2. Int. Dairy J. 20:571–579.
   Web of Science ®Google Scholar
• Loveday, S. M., Wang, X. L., Rao, M. A., Anema, S. G. and Singh, H. (2012b). β-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions. Food Hydrocolloids 27:242–249.
   Web of Science ®Google Scholar
• Machado, L. F., Pereira, R. N., Martins, R. C., Teixeira, J. A. and Vicente, A. A. (2010). Moderate electric fields can inactivate Escherichia coli at room temperature. J. Food Eng. 96:520–527.
   Web of Science ®Google Scholar
• Madureira, A. R., Pereira, C. I., Gomes, A. M. P., Pintado, M. E. and Xavier Malcata, F. (2007). Bovine whey proteins—Overview on their main biological properties. Food Res. Int. 40:1197–1211.
   Web of Science ®Google Scholar
• Maltais, A., Remondetto, G. E., Gonzalez, R. and Subirade, M. (2005). Formation of soy protein isolate cold-set gels: Protein and salt effects. J. Food Sci. 70:C67–C73.
   Web of Science ®Google Scholar
• Masson, P. (1992). Pressure denaturation of proteins. In: High Pressure and Biotechnology, pp. 89–99. Balny, C., Hayashi, K., Heremans, K. and Masson, P. Eds., Colloque Inserm/ John Libbey Eurotext: London, UK.
   Google Scholar
• Matalanis, A., Jones, O. G. and McClements, D. J. (2011). Structured biopolymer-based delivery systems for encapsulation, protection, and release of lipophilic compounds. Food Hydrocolloids 25:1865–1880.
   Web of Science ®Google Scholar
• McSwiney, M., Singh, H., Campanella, O. and Creamer, L. K. (1994). Thermal gelation and denaturation of bovine β-lactoglobulins A and B. J. Dairy Res. 61:221–232.
   Web of Science ®Google Scholar
• Mody, C. C. M. (2008). The larger world of nano. Physics Today 61:38–43.
   Web of Science ®Google Scholar
• Mohamed, M. E. A. and Eissa, A. H. A. (2012). Pulsed Electric Fields for Food Processing Technology, Structure and Function of Food Engineering, In: InTech pp. 275–306. Ayman Amer Eissa (Ed.), Chapter 11, DOI: 10.5772/48678. Available from: http://www.intechopen.com/books/structure-and-function-of-food-engineering/pulsed-electric-fields-for-food-processing-technology
   Google Scholar
• Morr, C. V. (1985). Functionality of heated milk proteins in dairy and related foods. J. Dairy Sci. 68:2773–2781.
   PubMed Web of Science ®Google Scholar
• Mozhaev, V. V., Lange, R., Kudryashova, E. V. and Balny, C. (1996). Application of high hydrostatic pressure for increasing activity and stability of enzymes. Biotechnol. Bioeng. 52:320–331.
   PubMed Web of Science ®Google Scholar
• Mulvihill, D. M. and Kinsella, J. E. (1988). Gelation of β-lactoglobulin: Effects of sodium chloride and calcium chloride on the rheological and structural properties of gels. J. Food Sci. 53:231–236.
   Web of Science ®Google Scholar
• Mulvihill, D. M., Rector, D. and Kinsella, J. E. (1991). Mercaptoethanol, N-ethylmaleimide, propylene-Glycol and urea effects on rheological properties of thermally induced beta-lactoglobulin gels at alkaline Ph. J. Food Sci. 56:1338–1341.
   Web of Science ®Google Scholar
• Nagpal, R., Behare, P., Rana, R., Kumar, A., Kumar, M., Arora, S., Morotta, F., Jain, S. and Yadav, H. (2011). Bioactive peptides derived from milk proteins and their health beneficial potentials: an update. Food Funct. 2:18–27.
   PubMed Web of Science ®Google Scholar
• Nicolai, T., Britten, M. and Schmitt, C. (2011). β-Lactoglobulin and WPI aggregates: Formation, structure and applications. Food Hydrocolloids 25:1945–1962.
   Web of Science ®Google Scholar
• Nicolai, T. and Durand, D. (2013). Controlled food protein aggregation for new functionality. Curr. Opin. Colloid Interface Sci. 18:249–256.
   Web of Science ®Google Scholar
• Oh, J. K., Lee, D. I. and Park, J. M. (2009). Biopolymer-based microgels/nanogels for drug delivery applications. Prog. Polym. Sci. 34:1261–1282.
   Web of Science ®Google Scholar
• Otte, J., Ipsen, R., Bauer, R., Bjerrum, M. J. and Waninge, R. (2005). Formation of amyloid-like fibrils upon limited proteolysis of bovine α-lactalbumin. Int. Dairy J. 15:219–229.
   Web of Science ®Google Scholar
• Otte, J., Lomholt, S. B., Ipsen, R., Stapelfeldt, H., Bukrinsky, J. T. and Qvist, K. B. (1997). Aggregate formation during hydrolysis of β-lactoglobulin with a Glu and Asp specific protease from bacillus licheniformis. J. Agric. Food Chem. 45:4889–4896.
   Web of Science ®Google Scholar
• Otte, J., Schumacher, E., Ipsen, R., Ju, Z. Y. and Qvist, K. B. (1999). Protease-induced gelation of unheated and heated whey proteins: effects of pH, temperature, and concentrations of protein, enzyme and salts. Int. Dairy J. 9:801–812.
   Web of Science ®Google Scholar
• Parrott, D. L. (1992). Use of Ohmic heating for aseptic processing of food particulates. Food Technol. 46:68–72.
   Web of Science ®Google Scholar
• Peppas, N. A., Hilt, J. Z., Khademhosseini, A. and Langer, R. (2006). Hydrogels in biology and medicine: From molecular principles to bionanotechnology. Adv. Mater. 18:1345–1360.
   Web of Science ®Google Scholar
• Pereira, R. N., Souza, B. W. S., Cerqueira, M. A., Teixeira, J. A. and Vicente, A. A. (2010). Effects of electric fields on protein unfolding and aggregation: Influence on edible films formation. Biomacromolecules 11:2912–2918.
   PubMed Web of Science ®Google Scholar
• Pereira, R. N., Teixeira, J. A. and Vicente, A. A. (2011). Exploring the denaturation of whey proteins upon application of moderate electric fields: A kinetic and thermodynamic study. J. Agric. Food Chem. 59:11589–11597.
   PubMed Web of Science ®Google Scholar
• Pereira, R. N. and Vicente, A. A. (2010). Environmental impact of novel thermal and non-thermal technologies in food processing. Food Res. Int. 43:1936–1943.
   Web of Science ®Google Scholar
• Pérez-Gago, M. B., Nadaud, P. and Krochta, J. M. (1999). Water vapor permeability, solubility, and tensile properties of heat-denatured versus native whey protein films. J. Food Sci. 64:1034–1037.
   Web of Science ®Google Scholar
• Phan-Xuan, T., Durand, D., Nicolai, T., Donato, L., Schmitt, C. and Bovetto, L. (2013). Tuning the structure of protein particles and gels with calcium or sodium ions. Biomacromolecules 14:1980–1989.
   PubMed Web of Science ®Google Scholar
• Pizones, R.-H., Víctor, M., Martinez, M. J., Carrera, S. C., Rodríguez, P., Juan, M. and Pilosof, A. M. R. (2014). Mixed soy globulins and β-lactoglobulin systems behaviour in aqueous solutions and at the air—water interface. Food Hydrocolloids 35:106–114.
   Web of Science ®Google Scholar
• Puyol, P., Pérez, M. D. and Horne, D. S. (2001). Heat-induced gelation of whey protein isolates (WPI): effect of NaCl and protein concentration. Food Hydrocolloids 15:233–237.
   Web of Science ®Google Scholar
• Ramos, O. L., Fernandes, J. C., Silva, S. I., Pintado, M. E. and Malcata, F. X. (2012a). Edible films and coatings from whey proteins: a review on formulation, and on mechanical and bioactive properties. Crit. Rev. Food Sci. Nutr. 52:533–552.
   PubMed Web of Science ®Google Scholar
• Ramos, O. L., Pereira, J. O., Silva, S. I., Amorim, M. M., Fernandes, J. C., Lopes-da-Silva, J. A., Pintado, M. E. and Malcata, F. X. (2012b). Effect of composition of commercial whey protein preparations upon gelation at various pH values. Food Res. Int. 48:681–689.
   Web of Science ®Google Scholar
• Ramos, Ó. L., Reinas, I., Silva, S. I., Fernandes, J. C., Cerqueira, M. A., Pereira, R. N., Vicente, A. A., Poças, M. F., Pintado, M. E. and Malcata, F. X. (2013). Effect of whey protein purity and glycerol content upon physical properties of edible films manufactured therefrom. Food Hydrocolloids 30:110–122.
   Web of Science ®Google Scholar
• Relkin, P. and Shukat, R. (2012). Food protein aggregates as vitamin-matrix carriers: Impact of processing conditions. Food Chem. 134:2141–2148.
   PubMed Web of Science ®Google Scholar
• Remondetto, G. E., Beyssac, E. and Subirade, M. (2004). Iron availability from whey protein hydrogels:  An in vitro study. J. Agric. Food Chem. 52:8137–8143.
   PubMed Web of Science ®Google Scholar
• Remondetto, G. E., Paquin, P. and Subirade, M. (2002). Cold Gelation of β-lactoglobulin in the presence of iron. J. Food Sci. 67:586–595.
   Web of Science ®Google Scholar
• Remondetto, G. E. and Subirade, M. (2003). Molecular mechanisms of Fe2+-induced beta-lactoglobulin cold gelation. Biopolymers 69:461–469.
   PubMed Web of Science ®Google Scholar
• Rodrigues, R. M., Martins, A. J., Ramos, O. L., Malcata, F. X., Teixeira, J. A., Vicente, A. A. and Pereira, R. N. (2015). Influence of moderate electric fields on gelation of whey protein isolate. Food Hydrocolloids 43:329–339.
   Web of Science ®Google Scholar
• Roefs, S. P. F. M. and De Kruif, K. G. (1994). A model for the denaturation and aggregation of β-lactoglobulin. Eur. J. Biochem. 226:883–889.
   PubMedGoogle Scholar
• Rubinstein, M. and Colby, R. H. (2003). Polymer Physics (Vol.). Oxford University Press, Oxford.
   Google Scholar
• Sadeghi, R., Kalbasi, A., Emam-jomeh, Z., Razavi, S. H., Kokini, J. and Moosavi-Movahedi, A. A. (2013). Biocompatible nanotubes as potential carrier for curcumin as a model bioactive compound. J. Nanopart. Res. 15:1–11.
   Web of Science ®Google Scholar
• Sagis, L. M., Veerman, C. and van der Linden, E. (2004). Mesoscopic properties of semiflexible amyloid fibrils. Langmuir. 20:924–927.
   PubMed Web of Science ®Google Scholar
• Sahiner, N., Alb, A. M., Graves, R., Mandal, T., McPherson, G. L., Reed, W. F. and John, V. T. (2007). Core–shell nanohydrogel structures as tunable delivery systems. Polymer 48:704–711.
   Web of Science ®Google Scholar
• Said, H. M., Abd Alla, S. G. and El-Naggar, A. W. M. (2004). Synthesis and characterization of novel gels based on carboxymethyl cellulose/acrylic acid prepared by electron beam irradiation. React. Funct. Polym. 61:397–404.
   Web of Science ®Google Scholar
• Sanghoon, K. and Sundaram, G. (2009). In situ microstructure evaluation during gelation of β-lactoglobulin. J. Food Eng. 90:161–170.
   Web of Science ®Google Scholar
• Santos, M. J., Teixeira, J. A. and Rodrigues, L. R. (2012). Fractionation of the major whey proteins and isolation of β-Lactoglobulin variants by anion exchange chromatography. Sep. Purif. Technol. 90:133–139.
   Web of Science ®Google Scholar
• Sarkar, A., Goh, K. K. T., Singh, R. P. and Singh, H. (2009). Behaviour of an oil-in-water emulsion stabilized by β-lactoglobulin in an in vitro gastric model. Food Hydrocolloids 23:1563–1569.
   Web of Science ®Google Scholar
• Sasso, L., Suei, S., Domigan, L., Healy, J., Nock, V., Williams, M. A. K. and Gerrard, J. A. (2014). Versatile multi-functionalization of protein nanofibrils for biosensor applications. Nanoscale 6:1629–1634.
   PubMed Web of Science ®Google Scholar
• Sawyer, W. H. (1968). Heat denaturation of bovine β-lactoglobulins and relevance of disulfide aggregation. J. Dairy Sci. 51:323–329.
   Web of Science ®Google Scholar
• Schuetz, Y. B., Gurny, R. and Jordan, O. (2008). A novel thermoresponsive hydrogel based on chitosan. Eur. J. Pharm. Biopharm. 68:19–25.
   PubMed Web of Science ®Google Scholar
• Sharma, R. (2012). Food structures and delivery of nutrients. In: Food Materials Science and Engineering, pp. 204–221. Bhandari, B. and Roos, Y. H., Eds., Wiley-Blackwell: Oxford, UK.
   Google Scholar
• Shiga, T. (1997). Deformation and viscoelastic behavior of polymer gels in electric fields. In: Neutron Spin Echo Spectroscopy Viscoelasticity Rheology, pp. 131–163. Springer, Berlin Heidelberg.
   Google Scholar
• Shimada, K. and Cheftel, J. C. (1989). Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate. J. Agric. Food Chem. 37:161–168.
   Web of Science ®Google Scholar
• Shpigelman, A., Cohen, Y. and Livney, Y. D. (2012). Thermally-induced β-lactoglobulin—EGCG nanovehicles: Loading, stability, sensory and digestive-release study. Food Hydrocolloids 29:57–67.
   Web of Science ®Google Scholar
• Shpigelman, A., Israeli, G. and Livney, Y. D. (2010). Thermally-induced protein–polyphenol co-assemblies: beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG. Food Hydrocolloids 24:735–743.
   Web of Science ®Google Scholar
• Smilowitz, J. T., Dillard, C. J. and German, J. B. (2005). Milk beyond essential nutrients: The metabolic food. Aust. J. Dairy Technol. 60:77–83.
   Web of Science ®Google Scholar
• Somchue, W., Sermsri, W., Shiowatana, J. and Siripinyanond, A. (2009). Encapsulation of α-tocopherol in protein-based delivery particles. Food Res. Int. 42:909–914.
   Web of Science ®Google Scholar
• Stading, M. and Hermansson, A.-M. (1990). Viscoelastic behaviour of β-lactoglobulin gel structures. Food Hydrocolloids 4:121–135.
   Web of Science ®Google Scholar
• Stading, M. and Hermansson, A.-M. (1991). Large deformation properties of β-lactoglobulin gel structures. Food Hydrocolloids 5:339–352.
   Web of Science ®Google Scholar
• Stading, M., Langton, M. and Hermansson, A.-M. (1992). Inhomogeneous fine-stranded β-lactoglobulin gels. Food Hydrocolloids 6:455–470.
   Web of Science ®Google Scholar
• Stokes, J. R. (2012). Food biopolymer gels, microgel and nanogel structures, formation and rheology. In: Food Materials Science and Engineering, pp. 151–176. Bhandari, B. and Roos, Y. H., Eds., Wiley-Blackwell: Oxford, UK.
   Google Scholar
• Svendsen, I. and Breddam, K. (1992). Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis. Eur. J. Biochem. 204:165–171.
   PubMedGoogle Scholar
• Tanaka, N. and Kunugi, S. (1996). Effect of pressure on the deuterium exchange reaction of α-lactalbumin and β-lactoglobulin. Int. J. Biol. Macromol. 18:33–39.
   PubMed Web of Science ®Google Scholar
• Tarhan, O., Tarhan, E. and Harsa, S. (2014). Investigation of the structure of alpha-lactalbumin protein nanotubes using optical spectroscopy. J. Dairy Res. 81:98–106.
   PubMed Web of Science ®Google Scholar
• Tavares, G. M., Croguennec, T., Carvalho, A. F. and Bouhallab, S. (2014). Milk proteins as encapsulation devices and delivery vehicles: Applications and trends. Trends Food Sci. Technol. 37:5–20.
   Web of Science ®Google Scholar
• TNS-BMRB - Food Standards Agency and BMRB Ltd. (2011). FSA citizens’ forums: nanotechnology and food. In: FSA Citizens Forums: Nanotechnology and Food, p. 39 (JN21986). Food Standards Agency. (available at: http://www.food.gov.uk/multimedia/pdfs/publication/fsacfnanotechnologyfood.pdf)
   Google Scholar
• Toepfl, S., Heinz, V. and Knorr, D. (2007). High intensity pulsed electric fields applied for food preservation. Chem. Eng. Process. 46:537–546.
   Web of Science ®Google Scholar
• Toepfla, S., Mathysa, A., Heinzb, V. and Knorr, D. (2006). Review: Potential of high hydrostatic pressure and pulsed electric fields for energy efficient and environmentally friendly food processing. Food Res. Int. 22:405–423.
   Web of Science ®Google Scholar
• Tokarev, I. and Minko, S. (2009). Stimuli-responsive hydrogel thin films. Soft Matter 5:511–524.
   Web of Science ®Google Scholar
• Totosaus, A., Montejano, J. G., Salazar, J. A. and Guerrero, I. (2002). A review of physical and chemical protein-gel induction. Int. J. Food Sci. Technol. 37:589–601.
   Web of Science ®Google Scholar
• Vadivambal, R. and Jayas, D. S. (2010). Non-uniform temperature distribution during microwave heating of food materials—A review. Food Bioprocess Technol. 3:161–171.
   Web of Science ®Google Scholar
• Veerman, C., Sagis, L. M. C., Heck, J. and van der Linden, E. (2003). Mesostructure of fibrillar bovine serum albumin gels. Int. J. Biol. Macromol. 31:139–146.
   PubMed Web of Science ®Google Scholar
• Velusamy, V. and Palaniappan, L. (2011). Compositional analysis α-lactalbumin. Amer. J. Biochem. Mol. Biol. 1:106–120.
   Google Scholar
• Vermonden, T., Censi, R. and Hennink, W. E. (2012). Hydrogels for protein delivery. Chem. Rev. 112:2853–2888.
   PubMed Web of Science ®Google Scholar
• Villamiel, M., Corzo, N., Martínez-Castro, I. and Olano, A. (1996). Chemical changes during microwave treatment of milk. Food Chem. 56:385–388.
   Web of Science ®Google Scholar
• Vinogradov, S. V., Bronich, T. K. and Kabanov, A. V. (2002). Nanosized cationic hydrogels for drug delivery: preparation, properties and interactions with cells. Adv. Drug Delivery Rev. 54:135–147.
   PubMed Web of Science ®Google Scholar
• Wehbi, Z., Perez, M. D., Sanchez, L., Pocovi, C., Barbana, C. and Calvo, M. (2005). Effect of heat treatment on denaturation of bovine alpha-lactalbumin: determination of kinetic and thermodynamic parameters. J. Agric. Food Chem. 53:9730–9736.
   PubMed Web of Science ®Google Scholar
• Wildman, R. E. C. (2006). Handbook of Nutraceuticals and Functional Foods (Vol.). CRC Press, Boca Raton FL.
   Google Scholar
• Ye, A., Singh, H., James Oldfield, D. and Anema, S. (2004). Kinetics of heat-induced association of β-lactoglobulin and α-lactalbumin with milk fat globule membrane in whole milk. Int. Dairy J. 14:389–398.
   Web of Science ®Google Scholar
• Zeng, X. A., Yu, S. J., Zhang, L. and Chen, X. D. (2008). The effects of AC electric field on wine maturation. Innovat. Food Sci. Emerg. Tech. 9:463–468.
   Web of Science ®Google Scholar
• Zhao, C., Zhuang, X., He, P., Xiao, C., He, C., Sun, J., Chen, X. and Jing, X. (2009). Synthesis of biodegradable thermo- and pH-responsive hydrogels for controlled drug release. Polymer 50:4308–4316.
   Web of Science ®Google Scholar
• Zimet, P. and Livney, Y. D. (2009). Beta-lactoglobulin and its nanocomplexes with pectin as vehicles for ω-3 polyunsaturated fatty acids. Food Hydrocolloids 23:1120–1126.
   Web of Science ®Google Scholar