Czech J. Food Sci., 2019, 37(3):212-220 | DOI: 10.17221/330/2017-CJFS

Influence of heat treatment on structure, interfacial rheology and emulsifying properties of peanut protein isolateFood Technology and Economy, Engineering and Physical Properties

Yazhen Zhang1,2, Wenfei Xiong1,2, Lingling Lei1,2, Yaqiong Pei1,2, Lingling He1,2, Tingyang Ai1,2, Yan Li1,2, Bin Li1,2,3, Yuan Jiang1,2, Xingnian Liu1,2, Ling Wang*,1,2
1 College of Food Science and Technology, Huazhong Agricultural University, Wuhan, P.R. China
2 Key Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan, P.R. China
3 Hubei Collaborative Innovation Centre for Industrial Fermentation, Hubei University of Technology, Wuhan, P.R. China

The influence of heat treatment on the protein size, zeta potential, surface hydrophobicity, secondary structure, interfacial rheology and creaming stability of peanut protein isolate (PPI) was studied. Heat treatment of PPI increased the protein size, surface hydrophobicity and interface diffusion rate, and decreased the protein zeta potential, particularly heat treatment at 80°C for 30 min (PPI-80), which increased the surface hydrophobicity from 117.33 ± 2.77 to 253.24 ± 2.47. Interfacial rheology results demonstrated that the heat treatment promoted the absorption of PPI at the oil-water interface, which might be due to the increase of surface hydrophobicity. In contrast, the heat treatment at 90°C resulted in slightly lower surface hydrophobicity and Kdiff compared with PPI-80 due to the hydrolysis of partial protein aggregates during high temperature. Moreover, heat-treated PPI showed better emulsifying properties than unheated PPI. These results would be useful to expand the utilization of PPI products in the food processing industry.

Keywords: adsorption; emulsifying property; heat treatment; interfacial rheology; peanut protein isolate

Published: June 30, 2019  Show citation

ACS AIP APA ASA Harvard Chicago Chicago Notes IEEE ISO690 MLA NLM Turabian Vancouver
Zhang Y, Xiong W, Lei L, Pei Y, He L, Ai T, et al.. Influence of heat treatment on structure, interfacial rheology and emulsifying properties of peanut protein isolate. Czech J. Food Sci. 2019;37(3):212-220. doi: 10.17221/330/2017-CJFS.
Share...
Download citation
  • BibTeX (.bib)
  • Bookends (.ris)
  • EasyBib (.ris)
  • EndNote (.enw)
  • EndNote 8 (.xml)
  • ISI WoS (.isi)
  • Medlars (.medlars)
  • Mendeley (.ris)
  • MODS (.xml)
  • Papers (.ris)
  • RefWorks (.txt)
  • RefManager (.ris)
  • RIS (.ris)
  • MS Word (.xml)
  • Zotero (.ris)
    • Open full article

    References

    1. Croguennec T., Renault A., Beaufils S., Dubois J.J., Pezennec S. (2007): Interfacial properties of heat-treated ovalbumin. Journal of Colloid and Interface Science, 315: 627-636. Go to original source... Go to PubMed...
    2. Delahaije R.J., Wierenga P.A., van Nieuwenhuijzen N.H., Giuseppin M.L., Gruppen H. (2013): Protein concentration and protein-exposed hydrophobicity as dominant parameters determining the flocculation of protein-stabilized oil-in-water emulsions. Langmuir, 29: 11567-11574. Go to original source... Go to PubMed...
    3. Delahaije R.J., Gruppen H., Giuseppin M.L., Wierenga P.A. (2014): Quantitative description of the parameters affecting the adsorption behaviour of globular proteins. Colloids and Surfce B-Biointerfaces, 123: 199-206. Go to original source... Go to PubMed...
    4. Feng X.-L., Liu H.-Z., Shi A.-M., Liu L., Wang Q., Adhikari B. (2014): Effects of transglutaminase catalyzed crosslinking on physicochemical characteristics of arachin and conarachin-rich peanut protein fractions. Food Research International, 62: 84-90. Go to original source...
    5. Graham D., Phillips M. (1979): Proteins at liquid interfaces: III. Molecular structures of adsorbed films. Journal of Colloid and Interface Science, 70: 427-439. Go to original source...
    6. Gong K.-J., Shi A.-M., Liu H.-Z., Liu L., Hu H., Adhikari B., Wang Q. (2016): Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate. Journal of Food Engineering, 170: 33-40. Go to original source...
    7. Gonzalo G. Palazolo, D.A.S., Wagner J.R. (2004): Emulsifying properties and surface beavior of native and denatured whey soy proteins in comparision with other proteins. Journal of the American Oil Chemists Society, 81: 427-439. Go to original source...
    8. He X.-H., Liu H.-Z., Liu L., Zhao G.-L., Wang Q., Chen Q.-L. (2014): Effects of high pressure on the physicochemical and functional properties of peanut protein isolates. Food Hydrocolloids, 36:123-129. Go to original source...
    9. Kiokias S., Dimakou C., Oreopoulou V. (2007): Effect of heat treatment and droplet size on the oxidative stability of whey protein emulsions. Food Chemistry, 105: 94-100. Go to original source...
    10. Kyoko S., Masahiko T., Watanabe T. (1975): Food use of soybean 7S and 11S proteins changes in basic groups of soybean proteins by high temperature heating. Journal of Food Science, 40: 541-544. Go to original source...
    11. Li C., Xue H., Chen Z., Ding Q., Wang X. (2014): Comparative studies on the physicochemical properties of peanut protein isolate-polysaccharide conjugates prepared by ultrasonic treatment or classical heating. Food Research International, 57: 1-7. Go to original source...
    12. Li F., Kong X., Zhang C., Hua Y. (2011): Effect of heat treatment on the properties of soy protein-stabilised emulsions. International Journal of Food Science and Technology, 46: 1554-1560. Go to original source...
    13. Mahmoudi N., Axelos M.A., Riaublanc A. (2011): Interfacial properties of fractal and spherical whey protein aggregates. Soft Matter, 7: 7643-7654. Go to original source...
    14. Martinez K., Sanchez C., Ruizhenestrosa V., Rodriguezpatino J., Pilosof A. (2007): Effect of limited hydrolysis of soy protein on the interactions with polysaccharides at the air-water interface. Food Hydrocolloids, 21: 813-822. Go to original source...
    15. Moro A., Báez G.D., Busti P.A., Ballerini G.A., Delorenzi N.J. (2011): Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties. Food Hydrocolloids, 25: 1009-1015. Go to original source...
    16. Murray B.S. (2002): Interfacial rheology of food emulsifiers and proteins. Current Opinion in Colloid & Interface Science, 7: 426-431. Go to original source...
    17. Nicolai T., Britten M., Schmitt C. (2011): β-Lactoglobulin and WPI aggregates: Formation, structure and applications. Food Hydrocolloids, 25: 1945-1962. Go to original source...
    18. 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. Go to original source...
    19. Petruccelli S., Anon M.C. (1995): Thermal aggregation of soy protein isolates. Journal of Agricultural and Food Chemistry, 43: 3035-3041. Go to original source...
    20. Qin L., Xun P., Bujnowski D., Daviglus M., van Horn L., Stamler J., He K. (2011): Higher branched-chain amino acid intake is associated with a lower prevalence of being overweight or obese in middle-aged East Asian and Western adults. Journal of Nutrition, 141: 249-254. Go to original source... Go to PubMed...
    21. Rodríguez Patino J.M., Rosario Rodríguez Niño M., Carrera Sánchez C. (1999): Adsorption of whey protein isolate at the oil-water interface as function of processing conditions a rheokinetic study. Journal of Agricultural and Food Chemistry, 47: 2241-2248. Go to original source... Go to PubMed...
    22. Ruffin E., Schmit T., Lafitte G., Dollat J.M., Chambin O. (2014): The impact of whey protein preheating on the properties of emulsion gel bead. Food Chemistry, 151: 324-332. Go to original source... Go to PubMed...
    23. Stone K., Sellmeyer D., Sebastian A., Cummings S. (2001): A high ratio of dietary animal to vegetable protein increases the rate of bone loss and the risk of fracture in postmenopausal women. American Journal of Clinical Nutrition, 73: 118-122. Go to original source... Go to PubMed...
    24. Tergesen J.F. (2010): Perspective sustainability points to plant proteins. Food Technology, 64: 88.
    25. Wan Z.L., Guo J., Yang X.Q. (2015): Plant protein-based delivery systems for bioactive ingredients in foods. Journal of Functional Foods, 6: 2876-2889. Go to original source... Go to PubMed...
    26. Wang J.M., Xia N., Yang X.Q., Yin S.W., Qi J.R., He X.T., Yuan D.B., Wang L.J. (2012): Adsorption and dilatational rheology of heat-treated soy protein at the oil-water interface: relationship to structural properties. Journal of Agricultural and Food Chemistry, 60: 3302-3310. Go to original source... Go to PubMed...
    27. Wu H., Wang Q., Ma T., Ren J. (2009): Comparative studies on the functional properties of various protein concentrate preparations of peanut protein. Food Research International, 42: 343-348. Go to original source...
    28. Xiao J., Li Y., Li J., Gonzalez A.P., Xia Q., Huang Q. (2014): Structure, morphology, and assembly behavior of kafirin. Journal of Agricultural and Food Chemistry, 63: 216-224. Go to original source... Go to PubMed...
    29. Xiong W., Wang Y., Zhang C., Wan J., Shah B.R., Pei Y., Zhou B., Li J., Li B. (2016): High intensity ultrasound modified ovalbumin: Structure, interface and gelation properties. Ultrasonics Sonochemistry, 31: 302-309. Go to original source... Go to PubMed...
    30. Zhang Q.-T., Tu Z.-C., Xiao H., Wang H., Huang X.-Q., Liu G.-X., Liu C.-M., Shi Y., Fan L.-L., Lin D.-R. (2014): Influence of ultrasonic treatment on the structure and emulsifying properties of peanut protein isolate. Food and Bioproducts Processing, 92: 30-37. Go to original source...

    This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International (CC BY NC 4.0), which permits non-comercial use, distribution, and reproduction in any medium, provided the original publication is properly cited. No use, distribution or reproduction is permitted which does not comply with these terms.


    Return to the content