1932

Abstract

Interactions between whey proteins and polysaccharides, in particular the formation of food-grade soluble complexes, are of interest because of potential functional and health benefits. A specific application that has not received much attention is the use of complexes for enhanced colloidal stability of protein sols, such as protein-containing beverages. In beverages, the primary goal is the formation of complexes that remain dispersed after thermal processing and extended storage. This review highlights recent progress in the area of forming whey protein–polysaccharide soluble complexes that would be appropriate for beverage applications. Research in this area indicates that soluble complexes can be formed and stabilized that are reasonably small in size and possess a large surface charge that would predict colloidal stability. Selection of specific proteins and polysaccharides can be tailored to desired conditions. The principal challenges involve overcoming restrictions on protein concentration and ensuring that protein remains bioavailable.

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2016-02-28
2024-04-27
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Literature Cited

  1. Anderson DMW, Bridgeman MME, Farquhar JGK, NcNab CGA. 1983. The chemical characterization of the test article used in toxicological studies of gum arabic [Acacia senegal (L.) Willd]. Int. Tree Crops J. 2:3–4245–54 [Google Scholar]
  2. Barnea E, Mizrahi J. 1973. A generalized approach to the fluid dynamics of particulate systems: Part 1. General correlation for fluidization and sedimentation in solid multiparticle systems. Chem. Eng. J. 5:2171–89 [Google Scholar]
  3. Beecher JW, Drake MA, Luck PJ, Foegeding EA. 2008. Factors regulating astringency of whey protein beverages. J. Dairy Sci. 91:72553–60 [Google Scholar]
  4. Bengoechea C, Jones OG, Guerrero A, McClements DJ. 2011. Formation and characterization of lactoferrin/pectin electrostatic complexes: impact of composition, pH and thermal treatment. Food Hydrocoll. 25:51227–32 [Google Scholar]
  5. Benichou A, Aserin A, Lutz R, Garti N. 2007. Formation and characterization of amphiphilic conjugates of whey protein isolate (WPI)/xanthan to improve surface activity. Food Hydrocoll. 21:3379–91 [Google Scholar]
  6. Bernal V, Jelen P. 1985. Thermal stability of whey proteins - a calorimetric study. J. Dairy Sci. 68:112847–52 [Google Scholar]
  7. Biesheuvel PM, Cohen Stuart MA. 2004. Electrostatic free energy of weakly charged macromolecules in solution and intermacromolecular complexes consisting of oppositely charged polymers. Langmuir 20:72785–91 [Google Scholar]
  8. Borrega R, Tribet C, Audebert R. 1999. Reversible gelation in hydrophobic polyelectrolyte/protein mixtures: an example of cross-links between soft and hard colloids. Macromolecules 32:237798–806 [Google Scholar]
  9. Campo VL, Kawano DF, da Silva DB, Carvalho I. 2009. Carrageenans: biological properties, chemical modifications and structural analysis: a review. Carbohydr. Polym. 77:2167–80 [Google Scholar]
  10. Champagne CP, Fustier P. 2007. Microencapsulation for the improved delivery of bioactive compounds into foods. Curr. Opin. Biotechnol. 18:2184–90 [Google Scholar]
  11. Chanasattru W, Jones OG, Decker EA, McClements DJ. 2009. Impact of cosolvents on formation and properties of biopolymer nanoparticles formed by heat treatment of β-lactoglobulin-pectin complexes. Food Hydrocoll. 23:82450–57 [Google Scholar]
  12. Chung C, Degner B, Decker EA, McClements DJ. 2013. Oil-filled hydrogel particles for reduced-fat food applications: fabrication, characterization, and properties. Innov. Food Sci. Emerg. Technol. 20:324–34 [Google Scholar]
  13. Cooper CL, Dubin PL, Kayitmazer AB, Turksen S. 2005. Polyelectrolyte-protein complexes. Curr. Opin. Colloid Interface Sci. 10:1–252–78 [Google Scholar]
  14. da Silva FLB, Jönsson B. 2009. Polyelectrolyte-protein complexation driven by charge regulation. Soft Matter 5:152862–68 [Google Scholar]
  15. da Silva FLB, Lund M, Jönsson B, Åkesson T. 2006. On the complexation of proteins and polyelectrolytes. J. Phys. Chem. B 110:94459–64 [Google Scholar]
  16. de Jong S, van de Velde F. 2007. Charge density of polysaccharide controls microstructure and large deformation properties of mixed gels. Food Hydrocoll. 21:71172–87 [Google Scholar]
  17. de Kruif CG, Tuinier R. 2001. Polysaccharide protein interactions. Food Hydrocoll. 15:4–6555–63 [Google Scholar]
  18. de Kruif CG, Weinbreck F, de Vries R. 2004. Complex coacervation of proteins and anionic polysaccharides. Curr. Opin. Colloid Interface Sci. 9:5340–49 [Google Scholar]
  19. Dickinson E. 2008. Interfacial structure and stability of food emulsions as affected by protein-polysaccharide interactions. Soft Matter 4:5932–42 [Google Scholar]
  20. Dills WL. 1989. Sugar alcohols as bulk sweeteners. Annu. Rev. Nutr. 9:161–86 [Google Scholar]
  21. Doublier JL, Garnier C, Renard D, Sanchez C. 2000. Protein-polysaccharide interactions. Curr. Opin. Colloid Interface Sci. 5:3–4202–14 [Google Scholar]
  22. Endreß HU, Christensen SH. 2009. Pectin. Handbook of Hydrocolloids GO Phillips, PA Williams 274–97 Boca Raton, FL: CRC Press, 2nd ed.. [Google Scholar]
  23. Eratte D, Wang B, Dowling K, Barrow CJ, Adhikari BP. 2014. Complex coacervation with whey protein isolate and gum arabic for the microencapsulation of omega-3 rich tuna oil. Food Funct. 5:112743–50 [Google Scholar]
  24. Etzel MR. 2004. Manufacture and use of dairy protein fractions. J. Nutr. 134:4996S–1002S [Google Scholar]
  25. Evans M, Ratcliffe I, Williams PA. 2013. Emulsion stabilisation using polysaccharide-protein complexes. Curr. Opin. Colloid Interface Sci. 18:4272–82 [Google Scholar]
  26. Fioramonti SA, Perez AA, Aríngoli EE, Rubiolo AC, Santiago LG. 2014. Design and characterization of soluble biopolymer complexes produced by electrostatic self-assembly of a whey protein isolate and sodium alginate. Food Hydrocoll. 35:129–36 [Google Scholar]
  27. Fox PF, McSweeney PLH. 2003. Advanced Dairy Chemistry 1 Cork, Irel: Kluwer Acad./Plenum Publ, 3rd ed..
  28. Funami T, Nakauma M, Ishihara S, Tanaka R, Inoue T, Phillips GO. 2011. Structural modifications of sugar beet pectin and the relationship of structure to functionality. Food Hydrocoll. 25:2221–29 [Google Scholar]
  29. Gentès M-C, St-Gelais D, Turgeon SL. 2010. Stabilization of whey protein isolate–pectin complexes by heat. J. Agric. Food Chem. 58:117051–58 [Google Scholar]
  30. Girard M, Turgeon SL, Gauthier SF. 2002. Interbiopolymer complexing between β-lactoglobulin and low- and high-methylated pectin measured by potentiometric titration and ultrafiltration. Food Hydrocoll. 16:6585–91 [Google Scholar]
  31. Goh KKT, Sarkar A, Singh H. 2014. Milk protein–polysaccharide interactions. Milk Proteins H Singh, M Boland, A Thompson 387–419 San Diego: Acad. Press, 2nd ed.. [Google Scholar]
  32. Grabitske HA, Slavin JL. 2009. Gastrointestinal effects of low-digestible carbohydrates. Crit. Rev. Food Sci. Nutr. 49:4327–60 [Google Scholar]
  33. Grasdalen H, Larsen B, Smidsrød O. 1979. A p.m.r. study of the composition and sequence of uronate residues in alginates. Carbohydr. Res. 68:123–31 [Google Scholar]
  34. Gromer A, Penfold R, Gunning AP, Kirby AR, Morris VJ. 2010. Molecular basis for the emulsifying properties of sugar beet pectin studied by atomic force microscopy and force spectroscopy. Soft Matter 6:163957–69 [Google Scholar]
  35. Gu YS, Decker EA, McClements DJ. 2005. Influence of pH and carrageenan type on properties of β-lactoglobulin stabilized oil-in-water emulsions. Food Hydrocoll. 19:183–91 [Google Scholar]
  36. Gummel J, Boué F, Clemens D, Cousin F. 2008. Finite size and inner structure controlled by electrostatic screening in globular complexes of proteins and polyelectrolytes. Soft Matter 4:81653–64 [Google Scholar]
  37. Guzey D, McClements DJ. 2006. Characterization of β-lactoglobulin-chitosan interactions in aqueous solutions: a calorimetry, light scattering, electrophoretic mobility and solubility study. Food Hydrocoll. 20:1124–31 [Google Scholar]
  38. Ha E, Zemel MB. 2003. Functional properties of whey, whey components, and essential amino acids: mechanisms underlying health benefits for active people (review). J. Nutr. Biochem. 14:5251–58 [Google Scholar]
  39. Hallberg RK, Dubin PL. 1998. Effect of pH on the binding of β-lactoglobulin to sodium polystyrenesulfonate. J. Phys. Chem. B 102:438629–33 [Google Scholar]
  40. Hébrard G, Hoffart V, Beyssac E, Cardot JM, Alric M, Subirade M. 2010. Coated whey protein/alginate microparticles as oral controlled delivery systems for probiotic yeast. J. Microencapsul. 27:4292–302 [Google Scholar]
  41. Hirt S, Jones OG. 2014. Effects of chloride, thiocyanate and sulphate salts on β-lactoglobulin-pectin associative complexes. Int. J. Food Sci. Technol. 49:112391–98 [Google Scholar]
  42. Hong YH, McClements DJ. 2007. Formation of hydrogel particles by thermal treatment of β-lactoglobulin–chitosan complexes. J. Agric. Food Chem. 55:145653–60 [Google Scholar]
  43. Imeson AP, Watson PR, Mitchell JR, Ledward DA. 1978. Protein recovery from blood plasma by precipitation with polyuronates. Int. J. Food Sci. Technol. 13:4329–38 [Google Scholar]
  44. Jacobs C, Kayser O, Müller RH. 2000. Nanosuspensions as a new approach for the formulation for the poorly soluble drug tarazepide. Int. J. Pharm. 196:2161–64 [Google Scholar]
  45. Jansson PE, Kenne L, Lindberg B. 1975. Structure of the extracellular polysaccharide from Xanthomonas campestris. Carbohydr. Res. 45:1275–82 [Google Scholar]
  46. Jones O, Decker EA, McClements DJ. 2010a. Thermal analysis of β-lactoglobulin complexes with pectins or carrageenan for production of stable biopolymer particles. Food Hydrocoll. 24:2–3239–48 [Google Scholar]
  47. Jones OG, Decker EA, McClements DJ. 2009. Formation of biopolymer particles by thermal treatment of β-lactoglobulin–pectin complexes. Food Hydrocoll. 23:51312–21 [Google Scholar]
  48. Jones OG, Lesmes U, Dubin P, McClements DJ. 2010b. Effect of polysaccharide charge on formation and properties of biopolymer nanoparticles created by heat treatment of β-lactoglobulin–pectin complexes. Food Hydrocoll. 24:4374–83 [Google Scholar]
  49. Jones OG, McClements DJ. 2010a. Functional biopolymer particles: design, fabrication, and applications. Compr. Rev. Food Sci. Food Saf. 9:4374–97 [Google Scholar]
  50. Jones OG, McClements DJ. 2010b. Biopolymer nanoparticles from heat-treated electrostatic protein-polysaccharide complexes: factors affecting particle characteristics. J. Food Sci. 75:2N36–43 [Google Scholar]
  51. Jones OG, McClements DJ. 2011. Recent progress in biopolymer nanoparticle and microparticle formation by heat-treating electrostatic protein-polysaccharide complexes. Adv. Colloid Interface Sci. 167:1–249–62 [Google Scholar]
  52. Joye IJ, McClements DJ. 2014. Biopolymer-based nanoparticles and microparticles: fabrication, characterization, and application. Curr. Opin. Colloid Interface Sci. 19:5417–427 [Google Scholar]
  53. Kazmierski M, Wicker L, Corredig M. 2003. Interactions of β-lactoglobulin and high-methoxyl pectins in acidified systems. J. Food Sci. 68:51673–79 [Google Scholar]
  54. Kizilay E, Kayitmazer AB, Dubin PL. 2011. Complexation and coacervation of polyelectrolytes with oppositely charged colloids. Adv. Colloid Interface Sci. 167:1–224–37 [Google Scholar]
  55. Klein M, Aserin A, Ishai PB, Garti N. 2010. Interactions between whey protein isolate and gum arabic. Colloids Surf. B Biointerfaces 79:2377–83 [Google Scholar]
  56. Krzeminski A, Prell KA, Busch-Stockfisch M, Weiss J, Hinrichs J. 2014a. Whey protein–pectin complexes as new texturising elements in fat-reduced yoghurt systems. Int. Dairy J. 36:2118–27 [Google Scholar]
  57. Krzeminski A, Prell KA, Weiss J, Hinrichs J. 2014b. Environmental response of pectin-stabilized whey protein aggregates. Food Hydrocoll. 35:332–40 [Google Scholar]
  58. Kulmyrzaev A, Bryant C, McClements DJ. 2000. Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins. J. Agric. Food Chem. 48:51593–97 [Google Scholar]
  59. Lahaye M. 2001. Chemistry and physico-chemistry of phycocolloids. Cah. Biol. Mar. 42:137–57 [Google Scholar]
  60. Laneuville SI, Paquin P, Turgeon SL. 2005. Formula optimization of a low-fat food system containing whey protein isolate–xanthan gum complexes as fat replacer. J. Food Sci. 70:8S513–19 [Google Scholar]
  61. Langendorff V, Cuvelier G, Launay B, Michon C, Parker A, de Kruif CG. 1999. Casein micelle/iota carrageenan interactions in milk: influence of temperature. Food Hydrocoll. 13:3211–18 [Google Scholar]
  62. Langendorff V, Cuvelier G, Michon C, Launay B, Parker A, de Kruif CG. 2000. Effects of carrageenan type on the behaviour of carrageenan/milk mixtures. Food Hydrocoll. 14:4273–80 [Google Scholar]
  63. Laos K, Brownsey GJ, Ring SG. 2007. Interactions between furcellaran and the globular proteins bovine serum albumin and β-lactoglobulin. Carbohydr. Polym. 67:1116–23 [Google Scholar]
  64. Li X, Fang Y, Al-Assaf S, Phillips GO, Yao X. et al. 2012. Complexation of bovine serum albumin and sugar beet pectin: structural transitions and phase diagram. Langmuir 28:2710164–76 [Google Scholar]
  65. Loveday SM, Ye A, Anema SG, Singh H. 2013. Heat-induced colloidal interactions of whey proteins, sodium caseinate and gum arabic in binary and ternary mixtures. Food Res. Int. 54:1111–17 [Google Scholar]
  66. Marshall K. 2004. Therapeutic applications of whey protein. Altern. Med. Rev. J. Clin. Ther. 9:2136–56 [Google Scholar]
  67. Mascotti DP, Lohman TM. 1990. Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acids. PNAS 87:83142–46 [Google Scholar]
  68. Mattison KW, Brittain IJ, Dubin PL. 1995. Protein-polyelectrolyte phase boundaries. Biotechnol. Prog. 11:6632–37 [Google Scholar]
  69. McClements DJ, Decker EA, Park Y, Weiss J. 2009. Structural design principles for delivery of bioactive components in nutraceuticals and functional foods. Crit. Rev. Food Sci. Nutr. 49:6577–606 [Google Scholar]
  70. Mekhloufi G, Sanchez C, Renard D, Guillemin S, Hardy J. 2005. pH-Induced structural transitions during complexation and coacervation of β-lactoglobulin and acacia gum. Langmuir 21:1386–94 [Google Scholar]
  71. Paulsson MA, Svensson U, Kishore AR, Satyanarayan Naidu A. 1993. Thermal behavior of bovine lactoferrin in water and its relation to bacterial interaction and antibacterial activity. J. Dairy Sci. 76:123711–20 [Google Scholar]
  72. Peinado I, Lesmes U, Andrés A, McClements JD. 2010. Fabrication and morphological characterization of biopolymer particles formed by electrostatic complexation of heat treated lactoferrin and anionic polysaccharides. Langmuir 26:129827–34 [Google Scholar]
  73. Pereyra R, Schmidt KA, Wicker L. 1997. Interaction and stabilization of acidified casein dispersions with low and high methoxyl pectins. J. Agric. Food Chem. 45:93448–51 [Google Scholar]
  74. Qi PX, Chau HK, Fishman ML, Wickham ED, Hotchkiss AT. 2014. Investigation of molecular interactions between β-lactoglobulin and sugar beet pectin by multi-detection HPSEC. Carbohydr. Polym. 107:198–208 [Google Scholar]
  75. Rajam R, Karthik P, Parthasarathi S, Joseph GS, Anandharamakrishnan C. 2012. Effect of whey protein–alginate wall systems on survival of microencapsulated Lactobacillus plantarum in simulated gastrointestinal conditions. J. Funct. Foods 4:4891–98 [Google Scholar]
  76. Rinaudo M. 2006. Chitin and chitosan: properties and applications. Prog. Polym. Sci. 31:7603–32 [Google Scholar]
  77. Ru Q, Wang Y, Lee J, Ding Y, Huang Q. 2012. Turbidity and rheological properties of bovine serum albumin/pectin coacervates: effect of salt concentration and initial protein/polysaccharide ratio. Carbohydr. Polym. 88:3838–46 [Google Scholar]
  78. Salminen H, Weiss J. 2013. Effect of pectin type on association and pH stability of whey protein–pectin complexes. Food Biophys. 9:129–38 [Google Scholar]
  79. Sanchez C, Mekhloufi G, Renard D. 2006. Complex coacervation between β-lactoglobulin and acacia gum: a nucleation and growth mechanism. J. Colloid Interface Sci. 299:2867–73 [Google Scholar]
  80. Santipanichwong R, Suphantharika M, Weiss J, McClements DJ. 2008. Core-shell biopolymer nanoparticles produced by electrostatic deposition of beet pectin onto heat-denatured β-lactoglobulin aggregates. J. Food Sci. 73:623–30 [Google Scholar]
  81. Schmitt C, Sanchez C, Desobry-Banon S, Hardy J. 1998. Structure and technofunctional properties of protein-polysaccharide complexes: a review. Crit. Rev. Food Sci. Nutr. 38:8689–753 [Google Scholar]
  82. Schmitt C, Turgeon SL. 2011. Protein/polysaccharide complexes and coacervates in food systems. Adv. Colloid Interface Sci. 167:1–263–70 [Google Scholar]
  83. Seyrek E, Dubin PL, Tribet C, Gamble EA. 2003. Ionic strength dependence of protein-polyelectrolyte interactions. Biomacromolecules 4:2273–82 [Google Scholar]
  84. Skepö M, Linse P. 2002. Dissolution of a polyelectrolyte-macroion complex by addition of salt. Phys. Rev. E 66:5051807 [Google Scholar]
  85. Smidsrød O, Haug A. 1971. Estimation of the relative stiffness of the molecular chain in polyelectrolytes from measurements of viscosity at different ionic strengths. Biopolymers 10:71213–27 [Google Scholar]
  86. Sperber BLHM, Cohen Stuart MA, Schols HA, Voragen AGJ, Norde W. 2009. Binding of β-lactoglobulin to pectins varying in their overall and local charge density. Biomacromolecules 10:123246–52 [Google Scholar]
  87. Stone AK, Nickerson MT. 2012. Formation and functionality of whey protein isolate–(kappa-, iota-, and lambda-type) carrageenan electrostatic complexes. Food Hydrocoll. 27:2271–77 [Google Scholar]
  88. Swaisgood HE. 1982. Chemistry of milk protein. Developments in Dairy Chemistry PF Fox 1–59 London: Appl. Sci. Publ. [Google Scholar]
  89. Tromp RH, de Kruif CG, van Eijk M, Rolin C. 2004. On the mechanism of stabilisation of acidified milk drinks by pectin. Food Hydrocoll. 18:4565–72 [Google Scholar]
  90. Turgeon SL, Laneuville SI. 2009. Protein + polysaccharide coacervates and complexes: from scientific background to their application as functional ingredients in food products. Modern Biopolymer Science S Kasapis, IT Norton, JB Ubbink 327–63 Oxford: Acad. Press [Google Scholar]
  91. Turgeon SL, Schmitt C, Sanchez C. 2007. Protein-polysaccharide complexes and coacervates. Curr. Opin. Colloid Interface Sci. 12:4–5166–78 [Google Scholar]
  92. Velikov KP, Pelan E. 2008. Colloidal delivery systems for micronutrients and nutraceuticals. Soft Matter 4:101964–80 [Google Scholar]
  93. Wakabayashi H, Oda H, Yamauchi K, Abe F. 2014. Lactoferrin for prevention of common viral infections. J. Infect. Chemother. 20:11666–71 [Google Scholar]
  94. Wang Z, Zhang S, Vardhanabhuti B. 2015. Foaming properties of whey protein isolate and λ-carrageenan mixed systems. J. Food Sci. 80:81893–902 [Google Scholar]
  95. Weinbreck F, de Vries R, Schrooyen P, de Kruif CG. 2003a. Complex coacervation of whey proteins and gum arabic. Biomacromolecules 4:2293–303 [Google Scholar]
  96. Weinbreck F, Minor M, de Kruif CG. 2004a. Microencapsulation of oils using whey protein/gum arabic coacervates. J. Microencapsul. 21:6667–79 [Google Scholar]
  97. Weinbreck F, Nieuwenhuijse H, Robijn GW, de Kruif CG. 2003b. Complex formation of whey proteins: exocellular polysaccharide EPS B40. Langmuir 19:229404–10 [Google Scholar]
  98. Weinbreck F, Nieuwenhuijse H, Robijn GW, de Kruif CG. 2004b. Complexation of whey proteins with carrageenan. J. Agric. Food Chem. 52:113550–55 [Google Scholar]
  99. Whistler RL, BeMiller. 1993. Industrial Gums: Polysaccharides and Their Derivatives San Diego, CA: Acad. Press
  100. Xie YR, Hettiarachchy NS. 1997. Xanthan gum effects on solubility and emulsification properties of soy protein isolate. J. Food Sci. 62:61101–4 [Google Scholar]
  101. Zhang S, Vardhanabhuti B. 2014. Intragastric gelation of whey protein–pectin alters the digestibility of whey protein during in vitro pepsin digestion. Food Funct. 5:1102–10 [Google Scholar]
  102. Zhang S, Zhang Z, Lin M, Vardhanabhuti B. 2012. Raman spectroscopic characterization of structural changes in heated whey protein isolate upon soluble complex formation with pectin at near neutral pH. J. Agric. Food Chem. 60:4812029–35 [Google Scholar]
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