Czech J. Food Sci., 2015, 33(5):474-479 | DOI: 10.17221/154/2015-CJFS

Modification of structural and functional properties of sunflower 11S globulin hydrolysatesFood Technology and Economy, Engineering and Physical Properties

Jian Ren, Chun-Li Song, Ping Wang, Shuang Li, Narasimha-Kumar Kopparapu, Xi-Qun Zheng
Heilongjiang Provincial Key University Laboratory of Processing Agricultural Products, College of Food and Bioengineering, Qiqihar University, Qiqihar, P.R. China

The structural and functional properties such as solubility, emulsifying properties, foaming properties, oil binding capacity, and surface hydrophobicity of sunflower 11S globulin hydrolysates generated by Alcalase at hydrolysis time of 30, 60, 90, and 120 min were evaluated. Circular dichroism analysis showed the hydrolysates possessed a decreased α-helix and β-structure. The hydrolysates exhibited lower surface hydrophobicity. Hydrolysates with shorter hydrolysis time showed the higher emulsifying activity index, but the same emulsion stability and oil binding capacity compared to the original 11S globulin. The longer hydrolysis resulted in lower foaming and emulsion stability. Thus it was demonstrated that by controlling the hydrolysis time of sunflower 11S globulin, hydrolysate with a desirable functional properties can be obtained.

Keywords: sunflower protein hydrolysates; structure; functionality

Published: October 31, 2015  Show citation

ACS AIP APA ASA Harvard Chicago Chicago Notes IEEE ISO690 MLA NLM Turabian Vancouver
Ren J, Song C, Wang P, Li S, Kopparapu N, Zheng X. Modification of structural and functional properties of sunflower 11S globulin hydrolysates. Czech J. Food Sci. 2015;33(5):474-479. doi: 10.17221/154/2015-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. Adler-Nissen J. (1982): Limited enzymatic degradation of proteins: a new approach in the industrial application of hydrolases. Journal of Chemical Technology & Biotechnology, 32: 138-156. Go to original source...
    2. Adler-Nissen J. (1986): Enzymic Hydrolysis of Food Proteins. New York, Elsevier Applied Science Publishers.
    3. Chabanon G., Chevalot I., Framboisier X., Chenu S., Marc I. (2007): Hydrolysis of rapeseed protein isolates: Kinetics, characterization and functional properties of hydrolysates. Process Biochemistry, 42: 1419-1428. Go to original source...
    4. Chobert J.M., Bertrandharb C., Nicolas M.G. (1988): Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin. Journal of Agricultural and Food Chemistry, 36: 883-892. Go to original source...
    5. Clemente A. (2000): Enzymatic protein hydrolysates in human nutrition. Trends in Food Science & Technology, 11: 254-262. Go to original source...
    6. Conde J.M., Patino J.M.R. (2007): The effect of enzymatic treatment of a sunflower protein isolate on the rate of adsorption at the air-water interface. Journal of Food Engineering, 78: 1001-1009. Go to original source...
    7. Conde J.M., Escobar M.D.Y., Jimenez J.J.P., Rodriguez F.M., Patino J.M.R. (2005a): Effect of enzymatic treatment of extracted sunflower proteins on solubility, amino acid composition, and surface activity. Journal of Agricultural and Food Chemistry, 53: 8038-8045. Go to original source... Go to PubMed...
    8. Conde J.M., Patino J.M.R., Trillo J.M. (2005b): Structural characteristics of hydrolysates of proteins from extracted sunflower flour at the air-water interface. Biomacromolecules, 6: 3137-3145. Go to original source... Go to PubMed...
    9. Frokjaer S. (1994): Use of hydrolysates for protein supplementation. Food Technology, 48: 86-88.
    10. Gbogouri G.A., Linder M., Fanni J., Parmentier M. (2004): Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates. Journal of Food Science, 69: C615-C622. Go to original source...
    11. Gonzalez-Perez S., Vereijken J.M. (2007): Sunflower proteins: overview of their physicochemical, structural and functional properties. Journal of the Science of Food and Agriculture, 87: 2173-2191. Go to original source...
    12. Hartmann R., Meisel H. (2007): Food-derived peptides with biological activity: from research to food applications. Current Opinion in Biotechnology, 18, 163-169. Go to original source... Go to PubMed...
    13. Johnson W.C. (1990): Protein secondary structure and circular dichroism: a practical guide. Proteins: Structure Function and Genetics, 7: 205-214. Go to original source... Go to PubMed...
    14. Kato A., Komatsu K., Fujimoto K., Kobayashi K. (1985): Relationship between surface functional-properties and flexibility of proteins detected by the protease susceptibility. Journal of Agricultural and Food Chemistry, 33: 931-934. Go to original source...
    15. Kristinsson H.G., Rasco B.A. (2000): Fish protein hydrolysates: Production, biochemical, and functional properties. Critical Reviews in Food Science and Nutrition, 40: 43-81. Go to original source... Go to PubMed...
    16. Mahmoud M.I. (1994): Physicochemical and functional properties of protein hydrosylates in nutritional products. Food Technology, 48: 89-95.
    17. Motoi H., Fukudome S., Urabe I. (2004): Continuous production of wheat gluten peptide with foaming properties using immobilized enzymes. European Food Research and Technology, 219: 522-528. Go to original source...
    18. Patino J.M.R., Conde J.M., Linares H.M., Jimenez J.J.P., Sanchez C.C., Pizones V., Rodriguez F.M. (2007): Interfacial and foaming properties of enzyme-induced hydrolysis of sunflower protein isolate. Food Hydrocolloids, 21: 782-793. Go to original source...
    19. Pearce K.N., Kinsella J.E. (1978): Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26: 716-723. Go to original source...
    20. Pickardt C., Neidhart S., Griesbach C., Dube M., Knauf U., Kammerer D.R., Carle R. (2009): Optimisation of mildacidic protein extraction from defatted sunflower (Helianthus annuus L.) meal. Food Hydrocolloids, 23: 1966-1973. Go to original source...
    21. Saetae D., Kleekayai T., Jayasena V., Suntornsuk W. (2011): Functional properties of protein isolate obtained from physic nut (Jatropha curcas L.) seed cake. Food Science and Biotechnology, 20: 29-37. Go to original source...
    22. Sastry M.S., Rao M.N. (1990): Binding of chlorogenic acid by the isolated polyphenol-free 11 S protein of sunflower (Helianthus annuus) seed. Journal of Agricultural and Food Chemistry, 38: 2103-2110. Go to original source...
    23. Schwenke K.D., Paehtz W., Linow K.-J., Raab B., Schultz M. (1979): On seed proteins Part 11. Purification, chemical composition, and some physico-chemical properties of the 11 S globulin (Helianthinin) in sunflower seed. Food/ Nahrung, 23: 241-254. Go to original source...
    24. Song C.L., Zhao X.H. (2014): The preparation of an oligochitosan-glycosylated and cross-linked caseinate obtained by a microbial transglutaminase and its functional properties. International Journal of Dairy Technology, 67: 110-116. Go to original source...
    25. Surowka K., Zmudzinski D., Surowka J. (2004): Enzymic modification of extruded soy protein concentrates as a method of obtaining new functional food components. Trends in Food Science & Technology, 15: 153-160. Go to original source...
    26. Zhao G.L., Liu Y., Zhao M.M., Ren J.Y., Yang B. (2011): Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate. Food Chemistry, 127: 1438-1443. 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