The effect of thermal treatment of whey protein isolate on the characteristics of gum tragacanth- whey protein isolate complexes

Document Type : Complete scientific research article

Authors

1 Department of Food Nanotechnology, Research Institute of Food Science and Technology

2 Department of Food Nanotechnology, Research Institute of Food Science and Technology, Mashhad, Iran

Abstract

Background and objectives:Gum tragacanth (GT) is one of the natural secreted hydrocolloids which have many applications in food and pharmaceutical industries. Unfortunately, there is limited scientific information about the electrostatic interactions of gum tragacanth with proteins, especially the proteins that have been unfolded by physical approaches. In this regard, the main objective of this study is investigation the effect of thermal processing on the whey protein isolate (WPI) properties and their complexation with gum tragacanth.
Materials and methods:The influence ofheating time (0, 5, 10, 15, 20, 25, 30 and 35 min at 80C) on the turbidity of WPI, alone and in the mixture with GT (r = 0.1, pH 4.0 and Cp 0.1 w/w) was surveyed. Then the flow behaviour and viscosity of gum tragacanth-WPI mixture solution in the shear rate of 0-100 S-1 (pH 4.0) was compared with the individual solutions of gum and protein. Since the maximum turbidity was observed in the range of 15-35°C, the impact of heating time at three levels (15, 25 and 35 min) and biopolymer mixing ratio at six levels (2:1, 1:1, 1:2, 1:5, 1:10 and 1:20) on the protein and carbohydrate compositions of precipitation and supernatant were investigated by lowry and phenol-sulphuric acid experiments, repectively.
Results:Turbidity of protein solutions were significantly changed with rising the heating time such that the maximum turbidity achieved after 25 min thermal processing. While these solutions were unstable due to protein-protein interaction and formation of protein aggregates, GT addition leads to meaningful changes in the stability of protein solutions which was as a result of protein-polysaccharied interactions. Similar to protein solutions, the maximum turbidity of the complexes was achieved after 25min thermal processing. The rheological measurements showed that the mixture solution has pseudoplastic behavior with a large hysteresis loop as well as the higher viscosity rather than the blank solutions, all of which indicate the formation of electrostatic interactions between protein and polysaccharide and formation of complexes.By calculation of protein and polysaccharide in the supernatant and precipitation, the least ratio of Pr:PS was observed for the 25-min-treated WPI. Furthermore, the ratio of Pr:PS in the precipitation was increased significantly as Pr:PSratio was increased in the mixture.
Conclusion:Addition ofgum tragacanth to the whey protein isolate will leads to a significant stability in the solution. Due to unfolding of WPI, using thermal processing on the whey protein isloate solution results in the meaningful increasing in the turbidity of protein solution and the efficiency of GT-WPI complex formation.

Keywords

References

  1. Antonov, A.Y., Dmitrochenko, A.P., and Leontiev, A.L. 2006. Interactions and compatibility of 11S globulin from Viciafaba seeds and sodium salt of carboxymethylcellulose in an aqueous medium. International Journal of Biological Macromolecules. 38: 18–24.
  2. Bourriot, S., Garnier, C., and Doublier, J.L. 1999. Phase separation, rheology and structure of micellar casein–galactomannan mixtures. International Dairy Journal. 9: 353–357.
  3. Bourriot. S., Garnier, C., and Doublier, J.L. 1999. Phase separation. Rheology and microstructure of micellar casein-guar gum mixtures. Food Hydrocolloids. 13: 43-49.
  4. Dickinson, E. 1995. Mixed biopolymers at interfaces. P 349-372, In: S.E. Harding, S.E., Hill and J.R. Mitchell (eds), Mixed Biopolymers, Nottingham University Press, Nottingham.
  5. Ercelebi, E.-A. andIbanoglu, E. 2007. Influence of hydrocolloids on phase separation and emulsion properties of whey protein isolate. Journal of Food Engineering. 80: 454–459.
  6. Firooz, M.H., Mohammadifar, M.A., and Haratian, P. 2012. Self-assembly of β-lactoglobulin and the soluble fraction of gum tragacanth in aqueous medium. International Journal of Biological Macromolecules. 50: 925-931.
  7. Gorji, S.G., Gorji, E.G., and Mohammadifar, M.A. 2014. Characterisation of gum tragacanth (Astragalusgossypinus)/sodium caseinate complex coacervation as a function of pH in an aqueous medium. Food Hydrocolloids. 34: 161-168.
  8. Jang, H.D., and Swaisgood, H.E. 1990. Disulfide bond formation between thermally denatured b-lactoblobulin and k-casein in casein micelles. Journal of Dairy Science. 73: 900–904.
  9. Jones, O.G., Lesmes, U., Dubin, P., and McClements, D.J. 2010. Effect of polysaccharide charge on formation and properties of biopolymer nanoparticles created by heat treatment of β-lactoglobulin–pectin complexes. Food Hydrocolloids. 24: 374–383.
  10. Kasapis, S. 2008. Phase separation in biopolymer gels: a low- to high-solid exploration of structural morphology and functionality. Critical Reviews in Food Science and Nutrition. 48: 341–359.
  11. Kim, H.-J., Decker, A.E., and McClements, D.J. 2006. Preparation of multiple emulsions based on thermodynamic incompatibility of heat-denatured whey protein and pectin solutions. Food Hydrocolloids. 20: 586–595.
  12. Kontogiorgos, V., Tosh, S.M., and Wood, P.J. 2009. Phase behaviour of high molecular weight oat b-glucan/whey protein isolate binary mixtures. Food Hydrocoilloids. 23: 949–956.
  13. Laneuville, S.I., Paquin, P., and Turgeon, S.L. 2000. Effect of preparation conditions on the characteristics of whey protein-xanthan gum complexes. Food Hydrocolloids. 14: 305–314.
  14. Lapasin, R., and Pricl, S. 1999. Rheology of polysaccharide systems Rheology of industrial polysaccharides: Theory and applications. United States of America: An Aspen Publication, Pp: 250-309.
  15. Lazaridou, A., and Biliaderis, C.G. 2009. Concurrent phase separation and gelation in mixed oat b-glucans/sodium caseinate and oat β-glucans/pullulandispersions. Food Hydrocolloids. 23: 886–895.
  16. Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J .1951. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry. 193: 265-275.
  17. Mutilangi, W.R.M., and Kilara, A. 1985. Functional properties of heat denatured whey protein. I. Solubility. Milchwissenschaft. 40(6): 338-341.
  18. Nasirpour, A., Amir, M., Hajihashemi, Z., and Fazilati, M. 2013. Complex formation between Tragacanth gum and beta-lactoglobulin in aqueous solution. International Food Research Journal. 20(3):1249-1254.
  19. Pelegrine, D.H.G., and Gomes, M.T.M.S. 2012. Analysis of whey proteins solubility at high temperatures. International Journal of Food Engineering. 8(3).
  20. Perrechil, F.A., Braga, A.L.M., and Cunha, R.L. 2009. Interactions between sodium caseinate and LBG in acidified systems: Rheology and phase behavior. Food Hydrocolloids. 23: 2085–2093.
  21. Phillips, G. O. and Williams, P. A. 2009. Handbook of Hydrocolloids, Cambridge, UK: Woodhead Publishing Ltd, Pp: 483-496.
  22. Samant, S.K., Singhal, R.S., Kulkarn, P.R., and Rege, D. 1993. Protein–polysaccharide interactions: a new approach in food formulations. International Journal of Food Science and Technology. 28(6): 547-562.
  23. Sanchez, C., and Paquin, P. 1997. Protein and protein–polysaccharide microparticles. Food science and technology, New York, Marcel Dekker, Pp: 503–528.
  24. Schmitt, C., and Turgeon, S.L. 2011. Protein/polysaccharide complexes and coacervates in food systems. Advances in Colloid and Interface Science. 167: 63-70.
  25. Shu, Y.-W., Sahara, S., Nakamura, S. and Kato, A. 1996. Effects of the length of polysaccharide chains on the functional properties of the Millard-type lysozyme–polysaccharide conjugate. Journal of Agricultural and Food Chemistry. 44: 2544-2548.
  26. Stauffer, K.R. 1980. Gum Tragacanth, P 11-1–11-30, In: R.L. Davidson (ed), Handbook of water-soluble gums and resins, New York, McGraw-Hill.
  27. Stauffer, K.R., and Andon, S.A. 1975. Comparison of the functional characteristics of two grades of tragacanth. Food Technology. 4: 46-51.
  28. Stone, A.K., and Nickerson, M.T. 2012. Formation and functionality of whey protein isolate (kappa-, iota-, and lambda-type) carrageenan electrostatic complexes. Food Hydrocolloid. 27: 271-277.
  29. Tolstoguzov, V.B. 1996. Structure-property relationships in foods. P 1-14, In:N. Parris, A. Kato, L.K. Creamer and J. Pearce (eds), Macromolecular interactions in food technology, ACS Symposium Series 650. Washington, DC: American Chemical Society.
  30. Tolstoguzov, V.B. 2003. Some thermodynamic considerations in food formulation. Food Hydrocolloids. 17: 1-23.
  31. Weinbreck, F., Wientjes, R.H.W., Nieuwenhuijse, H., Robijn, G.W., and de Kruif, C.G. 2004. Rheological properties of whey protein/gum arabiccoacervates. Journal of Rheology. 48: 6.1215-1228.
  32. Weiping, W. 2000. Tragacanth and karaya. P 231-246, In: Philips, G.O., and Williams, P. A. (eds), Handbook of hydrocolloids, Cambridge, England: CRC Press.
  33. Xia, J., and Dubin, P.L. 1995. Protein–polyelectrolyte complexes. P 247–274, In: P.L. Dubin, J. Bock, R., Davies, D.N. Schulz and C. Thies (eds), Macromolecular complexes in chemistry and biology, Berlin: Springer-Verlag.
  34. Zaitzev, V.S., Izumrudov, V.A., and Zezin, A.B. 1992. A new family of water-soluble protein – polysaccharide complexes. Polymer Science USSR. 34(1): 54–55.
  35. Zhang, G., and Foegeding, E.A. 2003. Heat-induced phase behavior of b-lactoglobulin/polysaccharide mixtures. Food Hydrocolloids. 17: 785–792.
Food Processing and Preservation Journal
Volume 11, Issue 2
January 2020
Pages 133-148

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