pH-Dependent Behavior and Stability of Protein-Based Particles in Aqueous Media

Year 2020, Volume: 16 Issue: 1, 95 - 102, 27.03.2020

Alev Emine İnce Coşkun Özgül Özdestan Ocak Buğra Ocak Semih Ötleş

Abstract

Protein particles could enhance the stability of
dispersions. This review focused on the characteristics of protein particles
from different sources, their structural stability and the stability of
dispersions at different pH values. Whey protein, sodium caseinate and gelatin
particles were investigated. To create particles from these proteins,
controlled aggregation and gelation were used in several methods. As chemical
structures of these proteins are all different, their gelation properties also
vary. Whey proteins are globular, caseins have a random structure, and gelatin in
gelled form has triple helix structure. Whey proteins undergo thermal
denaturation above 68ᵒC, therefore heat-set gelatin was often used for particle
preparation. When whey protein particles were prepared at the iso-electric
point (IEP) of proteins, they became dense and small; whereas at other pH
values, particles were soft and spherical due to increased repulsive forces
between proteins. Such particles could swell when the pH of the aqueous phase
was away from the IEP. Sodium caseinate is more heat stable compared to whey
proteins; however it is pH-sensitive. When sodium caseinate particles were
prepared through acidification, particles were stable against disintegration
only around the IEP of proteins. More stable caseinate particles could be
produced using enzymatic crosslinking. On the other hand, gelatin particles,
which were prepared via cold-set gelation, were stable over a wide pH range;
however, as they were thermo-sensitive, particles disintegrated above 30ᵒC.
This review explained the chemical differences of proteins, preparation of
particles using different methods, and stability of particles and their
dispersions at different conditions. 

Keywords

aggregation, gelatin, microstructure, sodium caseinate, whey protein

References

• 1. Haug, A, Hostmark, AT, Harstad, OM. 2007. Bovine milk in human nutrition – a review. Lipids in Health and Disease; 6: 25-40.
• 2. Hammann, F, Schmid, M. 2014. Determination and quantification of molecular interactions in protein films: A review. Materials; 7: 7975-7996.
• 3. Pelegrine, DHG, Gasparetto, CA. 2005. Whey protein solubility as function of temperature and pH. LWT-Food Science and Technology; 38(1): 77-80.
• 4. Horne, DS. 2006. Casein micelle structure: Models and muddles. Current Opinion in Colloid and Interface Science; 11: 148-153.
• 5. Broyard, C, Gaucheron, F. 2015. Modifications of structures and functions of caseins: a scientific and technological challenge. Dairy Science and Technology; 95: 831-862.
• 6. Thorn, DC, Meehan, S, Sunde, M, Rekas, A, Gras, SL, MacPhee, CE, Dobson, CM, Wilson MR, Carver JA. 2005. Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein. Biochemistry; 44(51): 17027-36.
• 7. Braga, ALM, Menossi, M, Cunha, RL. 2006. The effect of the glucono-δ-lactone/caseinate ratio on sodium caseinate gelation. International Dairy Journal; 16: 389-398.
• 8. Chu, B, Zhou, Z, Wu, G, Farrell Jr, HM. 1995. Laser light scattering of model casein solutions: Effects of high temperature. Journal of Colloid and Interface Science; 170(1): 102-112.
• 9. Guo, MR, Fox, PF, Flynn, PF, Kindstedt, PS. 1996. Heat-induced modifications of the functional properties of sodium caseinate. International Dairy Journal; 6(5): 473-483.
• 10. Stanic, D, Monogioudi, E, Dilek, E, Radosavljevic, J, Atanaskovic-Markovic, M, Vuckovic, O, Raija, L, Mattinen, L, Buchert, J, Cirkovic Velickovic, T. 2010. Digestibility and allergenicity assessment of enzymatically crosslinked β-casein. Molecular Nutrition and Food Research; 54: 1273–1284.
• 11. O’Kennedy, BT, Mounsey, JS, Murphy, F, Duggan, E, Kelly, PM. 2006. Factors affecting the acid gelation of sodium caseinate. International Dairy Journal; 16(10): 1132-1141.
• 12. Dickinson, E, Golding, M. 1997. Rheology of sodium caseinate stabilized oil-in-water emulsions. Journal of Colloid and Interface Science; 191(1): 166-176.
• 13. Gomez-Guillen, MC, Gimenez, B, Lopez-Caballero, ME, Montero, MP. 2011. Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids; 25: 1813-1827.
• 14. Nikoo, M, Benjakul, S, Ocen, D, Yang, N, Xu, B, Zhang, L, Xu, X. 2013. Physical and chemical properties of gelatin from the skin of cultured Amur sturgeon (Acipenser schrenckii). Journal of Applied Ichthyology; 29: 943-950.
• 15. Gornall, JL, Terentjev, EM. 2008. Helix-coil transition of gelatin: helical morphology and stability. Soft Matter; 4: 544-549.
• 16. Gomez-Guillen, MC, Turnay, J, Fernandez-Diaz, MD, Ulmo, N, Lizarbe, MA, Montero P. 2002. Structural and physical properties of gelatin extracted from different marine species: a comparative study. Food Hydrocolloids; 16(1): 25-34.
• 17. Seçkin, AK, Baladura, E. 2011. Süt ve süt ürünlerinin fonksiyonel özellikleri. Celal Bayar University Journal of Science; 7.1:27-38.
• 18. Güy, N. 2018. Papain immobilization on NiFe2O4 magnetic nanoparticles functionalized with gallic acid and microwave assisted digestion of bovine serum albumin. Celal Bayar University Journal of Science; 14(4): 449-454.
• 19. Kapusuz, D, Ercan, B. 2019. Calcium phosphate mineralization on calcium carbonate particle incorporated silk-fibroin composites. Celal Bayar University Journal of Science; 15(3): 301-306.
• 20. Büyüköz, M, Alsoy Altınkaya, S. 2015. Jelatin doku iskelesinin mekanik özellikleri üzerine gözenek oluşturucu ajanın boyutu ve bağlantı süresinin etkileri. Celal Bayar University Journal of Science; 11(2): 167-173.
• 21. Mehalebi, S, Nicolai, T, Durand, D. 2008. Light scattering study of heat- denatured globular protein aggregates. International Journal of Biological Macromolecules; 43: 129-135.
• 22. Schmitt, C, Bovay, C, Vuilliomenet, AM, Rouvet, M, Bovetto, L. 2011. Influence of protein and mineral composition on the formation of whey protein heat-induced microgels. Food Hydrocolloids; 25: 558-567.
• 23. Dill, KA. 1990. Dominant forces in protein folding. Biochemistry; 29: 7133-7155.
• 24. Moitzi, C, Donato, L, Schmitt, C, Bovetto, L, Gillies, G, Stradner, A. 2011. Structure of -lactoglobulin microgels formed during heating as revealed by small-angle X-ray scattering and light scattering. Food Hydrocolloids; 25: 1766-1774.
• 25. Nicolai, T, Durand, D. 2013. Controlled food protein aggregation for new functionality. Current Opinion in Colloid and Interface Science; 18: 249-256.
• 26. Phan-Xuan, T, Durand, D, Nicolai, T. 2013. Tuning the structure of protein particles and gels with calcium or sodium ions. Biomacromolecules; 14: 1980-1989.
• 27. Ruis, HGM, Venema, P, van der Linden, E. 2007. Relation between pH-induced stickiness and gelation behaviour of sodium caseinate aggregates as determined by light scattering and rheology. Food Hydrocolloids; 21: 545-554.
• 28. Lee, WJ, Lucey, JA. 2010. Formation and physical properties of yogurt. Asian-Australian Journal of Animal Science; 23: 1127-1136.
• 29. Xu, J, Li, T, Tao, F, Cui, Y, Xia, Y. 2013. Structure evolution of gelatin particles induced by pH and ionic strength. Microscopy Research and Technique; 76: 272-281.
• 30. Dumetz, AC, Snellinger-O'brien, AM, Kaler, EW, Lenhoff, AM. 2007. Patterns of protein protein interactions in salt solutions and implications for protein crystallization. Protein Science; 16: 1867-1877.
• 31. Lorenzen, PC. 2007. Effects of varying time/temperature-conditions of pre-heating and enzymatic cross-linking on techno-functional properties of reconstituted dairy ingredients. Food Research International; 40: 700-708.
• 32. Zhang, W, Zhong, Q. 2009. Microemulsions as nanoreactors to produce whey protein nanoparticles with enhanced heat stability by sequential enzymatic cross-linking and thermal pretreatment. Journal of Agricultural and Food Chemistry; 57: 9181-9189.
• 33. Nivala, O, Mäkinen, OE, Kruus, K, Nordlund, E, Ercili-Cura, D. 2017. Structuring colloidal oat and faba bean protein particles via enzymatic modification. Food Chemistry; 231: 87-95.
• 34. Alting, AC, de Jongh, HHJ, Visschers, RW, Simons, JWFA. 2002. Physical and chemical interactions in cold gelation of food proteins. Journal of Agricultural and Food Chemistry; 50: 4682-4689.
• 35. Lucey, JA, van Vliet, T, Grolle, K, Geurts, T, Walstra, P. 1997. Properties of acid casein gels made by acidification with glucono-δ-lactone. 1. Rheological properties. International Dairy Journal; 7: 381-388.
• 36. Andoyo, R, Guyomarc'h, F, Cauty, C, Famelart, MH. 2014. Model mixtures evidence the respective roles of whey protein particles and casein micelles during acid gelation. Food Hydrocolloids; 37: 203-212.
• 37. Guldbrand, L, Jönsson, B, Wennerström, H, Linse, P. 1984. Electrical double layer forces. A Monte Carlo study. The Journal of Chemical Physics; 80: 2221-2228.
• 38. Zhang, W, Zhong, Q. 2010. Microemulsions as nanoreactors to produce whey protein nanoparticles with enhanced heat stability by thermal pretreatment. Food Chemistry; 119: 1318-1325.
• 39. Sağlam, D, Venema, P, de Vries, R, Sagis, LMC, van der Linden, E. 2011. Preparation of high protein micro-particles using two-step emulsification. Food Hydrocolloids; 25: 1139-1148.
• 40. Ince Coskun, AE, Sağlam, D, Venema, P, van der Linden, E, Scholten, E. 2015. Preparation, structure and stability of sodium caseinate and gelatin micro-particles. Food Hydrocolloids; 45: 291-300.
• 41. Purwanti, N, Peters, JPC, van der Goot, AJ. 2013. Protein micro-structuring as a tool to texturize protein foods. Food and Function; 4: 277-282.
• 42. Wagoner, T, Vardhanabhuti, B, Foegeding, EA. 2016. Designing whey protein-polysaccharide particles for colloidal stability. Annual Review of Food Science and Technology; 7: 93-116.
• 43. Sağlam, D, Venema, P, de Vries, R, Shi, J, van der Linden, E. 2013. Concentrated whey protein particle dispersions: Heat stability and rheological properties. Food Hydrocolloids; 30: 100-109.
• 40. Sağlam, D, Venema, P, de Vries, R, van Aelst, A, van der Linden, E. 2012. Relation between gelation conditions and the physical properties of whey protein particles. Langmuir; 28: 6551-6560.
• 44. Liu, BT, Hsu, JP. 2009. Stability of soft colloidal particles in a salt-free medium. Langmuir; 25: 9045-9050.
• 45. Sağlam, D, Venema, P, de Vries, R, van der Linden, E. 2014. Exceptional heat stability of high protein content dispersions containing whey protein particles. Food Hydrocolloids; 34: 68-77.
• 46. Sağlam, D, Venema, P, de Vries, R, van der Linden, E. 2013. The influence of pH and ionic strength on the swelling of dense protein particles. Soft Matter; 9: 4598-4606.
• 47. Patel, AR, Bouwens, ECM, Velikov, KP. 2010. Sodium caseinate stabilized zein colloidal particles. Journal of Agricultural and Food Chemistry; 58: 12497-12503.
• 48. Li, F, Chen, Y, Liu, S, Qi, J, Wang, W, Wang, C, Zhong, R, Chen, Z, Li, X, Guan, Y, Kong, W, Zhang, Y. 2017. Size-controlled fabrication of zein nano/microparticles by modified anti-solvent precipitation with/without sodium caseinate. International Journal of Nanomedicine; 12: 8197-8209.
• 49. Ching, SH, Bhandari, B, Webb, R, Bansal, N. 2015. Visualizing the interaction between sodium caseinate and calcium alginate microgel particles. Food Hydrocolloids; 43: 165-171.
• 50. Ma, H, Forssell, P, Partanen, R, Seppanen, R, Buchert, J, Boer, H. 2009. Sodium caseinates with an altered isoelectric point as emulsifiers in oil/water systems. Journal of Agricultural and Food Chemistry; 57: 3800-3807.
• 51. Van der Linden, E, Parker, A. 2005. Elasticity due to semiflexible protein assemblies near the critical gel concentration and beyond. Langmuir; 21(21):9792-9794.
• 52. Farrugia, CA, Groves, MJ. 1999. Gelatin behaviour in dilute aqueous solution: Designing a nanoparticulate formulation. Journal of Pharmacy and Pharmacology; 51: 643-649.
• 53. Ahsan, SM, Rao, CM. 2017. The role of surface charge in the desolvation process of gelatin: implications in nanoparticle synthesis and modulation of drug release. International Journal of Nanomedicine; 12: 795-808.