Food Science and Biotechnology

, Volume 24, Issue 4, pp 1209–1218 | Cite as

Formation and functionality of canola protein isolate with both high- and low-methoxyl pectin under associative conditions

  • Andrea K. Stone
  • Anzhelika Teymurova
  • Chang Chang
  • Lamlam Cheung
  • Michael T. NickersonEmail author
Research Article


Electrostatic interactions within mixtures of a canola protein isolate (CPI) and both low (LMP) and high-methoxyl (HMP) pectin were investigated as a function of mixing ratio (1:1 to 30:1; CPI-pectin) and pH (8.0-1.5) using turbidity and electrophoretic mobility measurements during an acid titration. The rheological (flow behavior) and functional (solubility, foaming, and emulsifying properties) attributes of CPI-pectin complexes were also studied. Increasing biopolymer mixing ratios shifted critical pH values associated with formation of soluble and insoluble complexes to higher values until plateauing at approximately 10:1. Maximum coacervation of CPI-HMP and CPI-LMP mixtures occurred at pH values of 5.3 and 4.8, respectively, and at a 10:1 mixing ratio. The functionality of formed complexes was similar to CPI alone, except for a slight increase in solubility for the CPI-HMP system and a reduction in foaming capacity for CPI-LMP mixtures. For both mixed systems, viscosity was enhanced relative to CPI alone, showing greater pseudoplastic behavior.


coacervation canola pectin functionality 


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  1. 1.
    Tolstoguzov VB. Functional properties of food proteins and role of protein-polysaccharide interaction. Food Hydrocolloid. 4: 429–468 (1991)CrossRefGoogle Scholar
  2. 2.
    Schmitt C, Sanchez C, Desobry-Banon S, Hardy J. Structure and technofunctional properties of protein-polysaccharide complexes: A review. Crit. Rev. Food Sci. 38: 689–753 (1998)CrossRefGoogle Scholar
  3. 3.
    de Kruif CG, Weinbreck F, de Vries R. Complex coacervation of proteins and anionic polysaccharides. Curr. Opin. Colloid In. 9: 340–349 (2004)CrossRefGoogle Scholar
  4. 4.
    Li YJ, Xia JL, Dubin PL. Complex formation between polyelectrolyte and oppositely charged mixed micelles: Static and dynamic light scattering study of the effect of polyelectrolyte molecular weight and concentration. Macromolecules 27: 7049–7055 (1994)CrossRefGoogle Scholar
  5. 5.
    Liu S, Low NH, Nickerson MT. Effect of pH, salt, and biopolymer ratio on the formation of pea protein isolate-gum arabic complexes. J. Agr. Food Chem. 57: 1521–1526 (2009)CrossRefGoogle Scholar
  6. 6.
    Weinbreck F, Tromp RH, de Kruif CG. Composition and structure of whey protein/gum arabic coacervates. Biomacromolecules 5: 1437–1445 (2004)CrossRefGoogle Scholar
  7. 7.
    Bohidar H, Dubin PL, Majhi PR, Tribet C, Jaeger W. Effects of protein-polyelectrolyte affinity and polyelectrolyte molecular weight on dynamic properties of bovine serum albumin-poly(diallyldimethylammonium chloride) coacervates. Biomacromolecules 6: 1573–1585 (2005)CrossRefGoogle Scholar
  8. 8.
    Lizarraga MS, Vicin PD, Gonzalez R, Rubiolo A, Santiago LG. Rheological behaviour of whey protein concentrate and ëcarrageenan aqueous mixtures. Food Hydrocolloid. 20: 740–748 (2006)CrossRefGoogle Scholar
  9. 9.
    Wang XY, Lee JY, Wang YW, Huang QR. Composition and rheological properties of beta-lactoglobulin/pectin coacervates: Effects of salt concentration and initial protein/polysaccharide ratio. Biomacromolecules 8: 992–997 (2007)CrossRefGoogle Scholar
  10. 10.
    Ru Q, Wang Y, Lee J, Ding Y, Huang Q. Turbidity and rheological properties of bovine serum albumin/pectin coacervates: Effect of salt concentration and initial protein/polysaccharide ratio. Carbohyd. Polym. 88: 838–846 (2012)CrossRefGoogle Scholar
  11. 11.
    Ye A. Complexation between milk proteins and polysaccharides via electrostatic interaction: Principles and applications-A review. Int. J. Food Sci. Tech. 43: 406–415 (2008)CrossRefGoogle Scholar
  12. 12.
    Yuan Y, Wan Z-L, Yin S-W, Yang X-Q, Qi J-R, Liu G-Q, Zhang Y. Characterization of complexes of soy protein and chitosan heated at low pH. LWT-Food Sci. Technol. 50: 657–664 (2013)CrossRefGoogle Scholar
  13. 13.
    Ortiz SE, Puppo MC, Wagner JR. Relationship between structural changes and functional properties of soy protein isolatescarrageenan systems. Food Hydrocolloid. 18: 1045–1053 (2004)CrossRefGoogle Scholar
  14. 14.
    Plashchina IG, Mrachkovskaya TA, Danilenko AN, Kozhevnikov GO, Starodubrovskaya NY, Braudo EE, Schwenke KD. Complex formation of faba bean legumin with chitosan: Activity and emulsion properties of complexes. pp. 293–303. In: Food Colloids: Fundamentals of Formulation. Dickinson E, Miller R (eds). Royal Society of Chemistry, London, UK (2001)CrossRefGoogle Scholar
  15. 15.
    Uruakpa FO, Arntfield SD. Emulsifying characteristics of commercial canola protein-hydrocolloid systems. Food Res. Int. 38: 659–672 (2005)CrossRefGoogle Scholar
  16. 16.
    Li X, Fang Y, Al-Assaf S, Phillips GO, Jiang F. Complexation of bovine serum albumin and sugar beet pectin: Stabilizing oil-in-water emulsions. J. Colloid Interf. Sci. 388: 103–111 (2012)CrossRefGoogle Scholar
  17. 17.
    Gu YS, Decker EA, McClements DJ. Influence of pH and carrageenan type on properties of ß-lactoglobulin stabilized oil-inwater emulsions. Food Hydrocolloid. 19: 83–91 (2005)CrossRefGoogle Scholar
  18. 18.
    Ray M, Rousseau D. Stabilization of oil-in-water emulsions using mixtures of denatured soy whey proteins and soluble soybean polysaccharide. Food Res. Int. 52: 298–307 (2013)CrossRefGoogle Scholar
  19. 19.
    Miquelim JN, Lannes SCS, Mezzenga R. pH influence on the stability of foams with protein-polysaccharide complexes at their interfaces. Food Hydrocolloid. 24: 398–405 (2010)CrossRefGoogle Scholar
  20. 20.
    Schmidt I, Novales B, Boue F, Axelos MAV. Foaming properties of protein/pectin electrostatic complexes and foam structure at nanoscale. J Colloid Interf. Sci. 345: 316–324 (2010)CrossRefGoogle Scholar
  21. 21.
    Lampart-Szczapa E. Legume and oilseed proteins. pp. 407–432. In: Chemical and functional properties of food proteins. Sikorski ZE (ed). CRC Press, Boca Raton, FL, USA (2001)Google Scholar
  22. 22.
    Bérot S, Compoint JP, Larré C, Malabat C, Guéguen J. Large scale purification of rapeseed proteins (Brassica napus L.). J. Chromatogr. B 818: 35–42 (2005)CrossRefGoogle Scholar
  23. 23.
    Voragen AGJ, Pilnik W, Thibault JF, Axelos MAV, Renard CMGC. Pectins. pp. 287–339. In: Food Polysaccharides and Their Applications. Stephen AM (ed). Marcel Dekker Inc., New York, NY, USA (1995)Google Scholar
  24. 24.
    Klassen DR, Elmer CM, Nickerson MT. Associative phase separation involving canola protein isolate with both sulphated and carboxylated polysaccharides. Food Chem. 126: 1094–1101 (2011)CrossRefGoogle Scholar
  25. 25.
    Folawiyo YL, Apenten RKO. Effect of pH and ionic strength on the heat stability of rapeseed 12S globulin (cruciferin) by the ANS fluorescence method. J. Sci. Food Agr. 70: 241–246 (1996)CrossRefGoogle Scholar
  26. 26.
    AOAC. Official Method of Analysis of AOAC Intl. 17th ed. Method 925.10. Association of Official Analytical Chemists, Inc., Gaithersburg, MD, USA (2003)Google Scholar
  27. 27.
    AOAC. Official Method of Analysis of AOAC Intl. 17th ed. Method 923.03. Association of Official Analytical Chemists, Inc., Gaithersburg, MD, USA (2003)Google Scholar
  28. 28.
    AOAC. Official Method of Analysis of AOAC Intl. 17th ed. Method 920.87. Association of Official Analytical Chemists, Inc., Gaithersburg, MD, USA (2003)Google Scholar
  29. 29.
    AOAC. Official Method of Analysis of AOAC Intl. 17th ed. Method 920.85. Association of Official Analytical Chemists, Inc., Gaithersburg, MD, USA (2003)Google Scholar
  30. 30.
    Weinbreck F, de Vries R, Schrooyen P, de Kruif CG. Complex coacervation of whey proteins and gum arabic. Biomacromolecules 4: 293–303 (2003)CrossRefGoogle Scholar
  31. 31.
    Morr CV, German B, Kinsella JE, Regenstein JM, Van Buren JP, Kilara A, Lewis BA, Mangino ME. A collaborative study to develop a standardized food protein solubility procedure. J. Food Sci. 50: 1715–1718 (1985)CrossRefGoogle Scholar
  32. 32.
    Liu S, Elmer C, Low NH, Nickerson MT. Effect of pH on the functional behaviour of pea protein isolate-gum Arabic complexes. Food Res. Int. 43: 489–495 (2010)CrossRefGoogle Scholar
  33. 33.
    Stone AK, Cheung L, Chang C, Nickerson MT. Formation and functionality of soluble and insoluble electrostatic complexes within mixtures of canola protein isolate and (Ϋ-, ι- and λ-type) carrageenan. Food Res. Int. 54: 195–202 (2013)CrossRefGoogle Scholar
  34. 34.
    Liu S, Cao Y-L, Ghosh S, Rousseau D, Low NH, Nickerson MT. Intermolecular interaction during complex coacervation of pea protein isolate and gum arabic. J. Agr. Food Chem. 58: 552–556 (2010)CrossRefGoogle Scholar
  35. 35.
    Klassen D R, Nickerson MT. Effect of pH on the formation of electrostatic complexes within admixtures of partially purified pea proteins (legumin and vicilin) and gum Arabic polysaccharides. Food Res. Int. 46: 167–176 (2012)CrossRefGoogle Scholar
  36. 36.
    Aryee FNA, Nickerson MT. Formation of electrostatic complexes involving mixtures of lentil protein isolates and gum Arabic polysaccharides. Food Res. Int. 48: 520–527 (2012)CrossRefGoogle Scholar
  37. 37.
    Girard M, Turgeon SL, Gauthier SF. Interbiopolymer complexing between beta-lactoglobulin and low- and high-methylated pectin measured by potentiometric titration and ultrafiltration. Food Hydrocolloid. 16: 585–591 (2002)CrossRefGoogle Scholar
  38. 38.
    Sperber BLHM, Schols HA, Cohen Stuart MA, Norde WA, Voragen GJ. Influence of the overall charge and local charge density of pectin on the complex formation between pectin and betalactoglobulin. Food Hydrocolloid. 23: 765–772 (2009)CrossRefGoogle Scholar
  39. 39.
    Lutz R, Aserin A, Portnoy Y, Gottlieb M, Garti N. On the confocal images and the rheology of whey protein isolated and modified pectins associated complex. Colloid. Surface. B 69: 43–50 (2009)CrossRefGoogle Scholar
  40. 40.
    Burova TV, Grinberg NV, Grinberg VY, Usov AI, Tolstoguzov VB, de Kruif CG. Conformational changes in iota- and kappa-carrageenan induced by complex formation with bovine beta-casein. Biomacromolecules 8: 368–375 (2007)CrossRefGoogle Scholar

Copyright information

© The Korean Society of Food Science and Technology and Springer Science+Business Media Dordrecht 2015

Authors and Affiliations

  • Andrea K. Stone
    • 1
  • Anzhelika Teymurova
    • 1
  • Chang Chang
    • 1
  • Lamlam Cheung
    • 1
  • Michael T. Nickerson
    • 1
    Email author
  1. 1.Department of Food and Bioproduct SciencesUniversity of SaskatchewanSaskatoonCanada

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