Advertisement

Food and Bioprocess Technology

, Volume 12, Issue 5, pp 877–882 | Cite as

Microfluidization as Homogenization Technique in Pea Globulin-Based Emulsions

  • Bonastre OlieteEmail author
  • Francois Potin
  • Eliane Cases
  • Rémi Saurel
Original Paper
  • 102 Downloads

Abstract

The effect of microfluidization pressure (50, 70 and 130 MPa) during emulsification on the properties of native (NP) and soluble thermally aggregated (SA) pea (Pisum sativum L.) globulin-based emulsions at neutral pH was studied. Emulsions were characterized by interfacial protein-adsorption capacity, charge, emulsifying and flocculation properties, and creaming stability. NP- and SA-based emulsions were highly flocculated. Floc size decreased when increasing the microfluidization pressure during emulsification. Shear, turbulence, and collisions due to microfluidization induced modifications in the protein/aggregate association at the O/W interface and decreased the oil droplet size. SA-based emulsions showed higher floc size and smaller oil droplet size and revealed a more effective adsorption of SA at the O/W interface than NP. Creaming stability in NP-based emulsions decreased when increasing microfluidization pressure probably as a consequence of depletion-flocculation phenomena. On the contrary, creaming stability in SA-based emulsions improved when increasing homogenization pressure as a result of the formation of a gel-like network. Microfluidization could be used to modulate the emulsifying properties of pea globulin depending on their initial denaturation state.

Keywords

Pea globulins Aggregates Microfluidization High dynamic pressure Emulsifying properties 

Notes

Funding

This work was supported financially by European Funds for Regional Development (FEDER-FSE Bourgogne 2014/2020), French Inter-Ministerial Unique Funds (FUI), and the Region of Burgundy (France) as part of project LEGUP Lot 3 2015 03 03.

References

  1. Dickinson, E. (2010). Flocculation of protein-stabilized oil-in-water emulsions. Colloids Surf B, 81(1), 130–140.CrossRefGoogle Scholar
  2. Euston, S. R. (2004). Computer simulation of proteins: adsorption, gelation and self-association. Current Opinion in Colloid and Interface Science, 9(5), 321–327.CrossRefGoogle Scholar
  3. Karaca, A. C., Low, N., & Nickerson, M. (2011). Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction. Food Research International, 44(9), 2742–2750.CrossRefGoogle Scholar
  4. Kimura, A., Fukuda, T., Zhang, M., Motoyama, S., Maruyama, N., & Utsumi, S. (2008). Comparison of physicochemical properties of 7S and 11S globulins from pea, fava bean, cowpea, and french bean with those of soybean-French bean 7S globulin exhibits excellent properties. Journal of Agricultural and Food Chemistry, 56(21), 10273–10279.CrossRefGoogle Scholar
  5. Lan, Y., Ohm, J. B., Chen, B., & Rao, J. (2019). Solid dispersion-based spray-drying improves solubility and mitigates beany flavor of pea protein isolate. Food Chemistry, 278, 665–673.CrossRefGoogle Scholar
  6. Liang, H. N., & Tang, C. H. (2013a). pH-dependent emulsifying properties of pea [Pisum sativum (L.)] proteins. Food Hydrocolloids, 33(2), 309–319.CrossRefGoogle Scholar
  7. Liang, H. N., & Tang, C. H. (2013b). Emulsifying and interfacial properties of vicilins: Role of conformational flexibility at quaternary and/or tertiary levels. Journal of Agricultural and Food Chemistry, 61(46), 11140–11150.CrossRefGoogle Scholar
  8. Liang, H. N., & Tang, C. H. (2014). Pea protein exhibits a novel Pickering stabilization for oil-in-water emulsions at pH 3.0. LWT-Food Science and Technology, 58(2), 463–469.CrossRefGoogle Scholar
  9. Ma, Z., Boye, J. I., Simpson, B. K., Prasher, S. O., Monpetit, D., & Malcolmson, L. (2011). Thermal processing effects on the functional properties and microstructure of lentil, chickpea, and pea flours. Food Research International, 44(8), 2534–2544.CrossRefGoogle Scholar
  10. McCarthy, N. A., Kennedy, D., Hogan, S. A., Kelly, P. M., Thapa, K., Murphy, K. M., & Fenelon, M. A. (2016). Emulsification properties of pea protein isolate using homogenization, microfluidization and ultrasonication. Food Research International, 89, 415–421.CrossRefGoogle Scholar
  11. Oliete, B., Cases, E., & Saurel, R. (2017). Improvement of techno-functional properties of pea proteins by microfluidization. International Journal of Food and Biosystems Engineering, 4, 57–68.Google Scholar
  12. Oliete, B., Potin, F., Cases, E., & Saurel, R. (2018). Modulation of the emulsifying properties of pea globulin soluble aggregates by dynamic high-pressure fluidization. Innovative Food Science and Emerging Technologies, 47, 292–300.CrossRefGoogle Scholar
  13. Peng, W., Kong, X., Chen, Y., Zhang, C., Yang, Y., & Hua, Y. (2016). Effects of heat treatment on the emulsifying properties of pea proteins. Food Hydrocolloids, 52, 301–310.CrossRefGoogle Scholar
  14. Rangel, A., Domont, G. B., Pedrosa, C., & Ferreira, S. T. (2003). Functional properties of purified vicilins from cowpea (Vigna unguiculata) and pea (Pisum sativum) and cowpea protein isolate. Journal of Agricultural and Food Chemistry, 51(19), 5792–5797.CrossRefGoogle Scholar
  15. Riddick, T. M. (1968). Control of colloid stability through zeta potential. Wynnewood: Livingston Publishing Company.Google Scholar
  16. Shao, Y., & Tang, C. H. (2014). Characteristics and oxidative stability of soy protein stabilized oil-in-water emulsions: influence of ionic strength and heat pretreatment. Food Hydrocolloids, 37, 149–158.CrossRefGoogle Scholar
  17. Sharif, H. R., Williams, P. A., Sharif, M. K., Abbas, S., Majeed, H., Masamba, K. G., Safdar, W., & Zhong, F. (2018). Current progress in the utilization of native and modified legume proteins as emulsifiers and encapsulants—a review. Food Hydrocolloids, 76, 1–16.CrossRefGoogle Scholar
  18. Shen, L., & Tang, C. H. (2012). Microfluidization as a potential technique to modify surface properties of soy protein isolate. Food Research International, 48(1), 108–118.CrossRefGoogle Scholar
  19. Srinivasan, M., Singh, H., & Munro, P. A. (2002). Formation and stability of sodium caseinate emulsions: influence of retorting (121 °C for 15 min) before or after emulsification. Food Hydrocolloids, 16(2), 153–160.CrossRefGoogle Scholar
  20. Tang, C. H., & Liu, F. (2013). Cold, gel-like soy protein emulsions by microfluidization: emulsion characteristics, rheological and microstructural properties, and gelling mechanism. Food Hydrocolloids, 30(1), 61–72.CrossRefGoogle Scholar
  21. Vrij, A. (1976). Polymers at interfaces and the interactions in colloidal dispersions. Pure and Applied Chemistry, 48(4), 471–483.CrossRefGoogle Scholar
  22. Yang, J., Liu, G., Zeng, H., & Chen, L. (2018). Effects of high pressure homogenization on faba bean protein aggregation in relation to solubility and interfacial properties. Food Hydrocolloids, 83, 275–286.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  1. 1.AgroSup Dijon, PAM UMR A 02.102University Bourgogne Franche-ComtéDijonFrance

Personalised recommendations