Abstract
The objective of the study was to examine the sensitivity of whey protein functionality to oxidizing radicals. Whey protein isolate (WPI) was oxidatively stressed by incubation at 20 °C for 3, 5, and 10 h in hydroxyl radical-generating media containing 0.1 mM ascorbic acid, 0.1 mM FeCl3, and 1–10 mM H2O2. Protein solubility decreased (P < 0.05) with increasing H2O2 concentrations and oxidation time. Surface properties of WPI, including both emulsifying and foaming activities, exhibited significant improvements (P < 0.05) at H2O2 concentrations up to 5 mM and oxidation time up to 5 h. The longer oxidation time or higher H2O2 concentrations tended to diminish the surface functionality. However, the oxidative stress, though decreasing the onset gelling temperature, had a general detrimental effect on WPI gelation (hardness, springiness, and storage modulus). The results indicated opposing effects of oxidation on WPI: detrimental to hydrodynamic properties (solubility, gelation) but beneficial to surface properties (emulsification, foaming).
Similar content being viewed by others
References
Cayot, P., & Lorient, D. (1997). Structure–function relationship of whey proteins. In S. Damodaran & A. Paraf (Eds.), Food proteins and their applications (pp. 225–256). New York: Marcel Dekker.
Cocup, R. O., & Sanderson, W. B. (1987). Functionality of dairy ingredients in bakery products. Food Technology, 41, 86–90.
Cui, X. H., Xiong, Y. L., Kong, B. H., Zhao, X. H., & Liu, N. (2011). Hydroxyl radical-stressed whey protein isolate: Chemical and structural properties. Food and Bioprocess Technology. doi:10.1007/s11947-011-0515-9.
Damodaran, S. (2007). Amino acids, peptides, and proteins. In S. Damodaran, K. L. Parkin, & O. R. Fennema (Eds.), Fennema's food chemistry (4th ed., pp. 217–329). Boca Raton: CRC.
de Wit, J. N. (1998). Nutritional and functional characteristics of whey proteins in food products. Journal of Dairy Science, 81, 597–608.
Elias, R. J., McClements, D. J., & Decker, E. A. (2005). Antioxidant activity of cysteine, tryptophan, and methionine residues in continuous phase of β-lactoglobulin in oil-in-water emulsions. Journal of Agricultural and Food Chemistry, 53, 10248–10253.
Færgemand, M., Otte, J., & Qvist, K. B. (1998). Cross-linking of whey proteins by enzymatic oxidation. Journal of Agricultural and Food Chemistry, 46, 1326–1333.
Kinsella, J. E., & Whitehead, D. M. (1989). Proteins in whey: Chemical, physical, and functional properties. Advances in Food and Nutrition Research, 33, 343–438.
Li-Chan, E., & Nakai, S. (1991). Importance of hydrophobicity of proteins in food emulsions. In M. El-Nokaly & D. Cornell (Eds.), Microemulsions and emulsions in foods (chapter 15) (pp. 193–212). Washington: American Chemical Society.
Liu, G., & Xiong, Y. L. (2000). Thermal transitions and dynamic gelling properties of oxidatively modified myosin, b-lactoglobulin, soy 7S globulin and their mixtures. Journal of the Science of Food and Agriculture, 80, 1728–1734.
Liu, G., Xiong, Y. L., & Butterfield, D. A. (2000). Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolates. Journal of Food Science, 65, 811–818.
Lund, M. N., Heinonen, M., Baron, C. P., & Estévez, M. (2011). Protein oxidation in muscle foods: A review. Molecular Nutrition & Food Research, 55, 83–95.
Mestdagh, F., Kerkaert, B., Cucu, T., & Meulenaer, B. D. (2011). Interaction between whey proteins and lipids during light-induced oxidation. Food Chemistry, 126, 1190–1197.
Morr, C. V., & Ha, E. Y. (1993). Whey protein concentrates and isolates: Processing and functional properties. Critical Review in Food Science and Nutrition, 33, 431–476.
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.
Pena-Ramos, E. A., Xiong, Y. L., & Arteaga, G. E. (2004). Fractionation and characterization for antioxidant activity of hydrolyzed whey protein. Journal of the Science of Food and Agriculture, 84, 1908–1918.
Sathe, S. K., & Salunkhe, D. K. (1981). Functional properties of the Great Northern Bean (Phaseolus vulgaris L.) proteins: Emulsion, foaming, viscosity and gelation properties. Journal of Food Science, 46, 71–74.
Shahidi, F., Han, X. Q., & Synowiecki, J. (1995). Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chemistry, 53, 285–293.
Smithers, G. W. (2008). Whey and whey proteins—From ‘gutter-to-gold’. International Dairy Journal, 18, 695–704.
Srinivasan, S., & Hultin, H. O. (1997). Chemical, physical, and functional properties of cod proteins modified by a nonenzymic free-radical-generating system. Journal of Agricultural and Food Chemistry, 45, 310–320.
Xiong, Y. L., Blanchard, S. P., Ooizumi, T., & Ma, Y. (2010). Hydroxyl radical and ferryl-generating systems promote gel network formation of myofibrillar protein. Journal of Food Science, 75, C215–C221.
Acknowledgments
This study was supported by the National Natural Science Foundation in China (grant no. 30871818) and the Foundation of Innovative Research Team of Higher Education of Heilongjiang Province (grant no. 2010td11).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Kong, B., Xiong, Y.L., Cui, X. et al. Hydroxyl Radical-Stressed Whey Protein Isolate: Functional and Rheological Properties. Food Bioprocess Technol 6, 169–176 (2013). https://doi.org/10.1007/s11947-011-0674-8
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11947-011-0674-8