Food and Bioprocess Technology

, Volume 5, Issue 6, pp 2342–2352 | Cite as

Comparisons on the Functional Properties and Antioxidant Activity of Spray-Dried and Freeze-Dried Egg White Protein Hydrolysate

  • Chen Chen
  • Yu-Jie Chi
  • Wei Xu
Original Paper


Freeze-dried and spray-dried egg white protein hydrolysates (FD-EWPH, SD-EWPH) prepared by papain were evaluated for their proximate composition, color, molecular weight distribution, physical structures, functional properties, and antioxidant activity. FD-EWPH and SD-EWPH had similar proximate composition and molecular weight distribution, but they had different color and physical structures. There was no significant difference (P > 0.05) in solubility among egg white protein hydrolysate (EWPH) before drying (UD-EWPH), FD-EWPH, and SD-EWPH. The foaming properties of EWPH were improved by freeze-drying but reduced by spray-drying (P < 0.05). Freeze-drying did not influence the emulsifying properties of EWPH while spray-drying had harmful effects on it. In the antioxidant test, no significant differences (P > 0.05) in 1,1-diphenyl-2-picryl-hydrazyl radical-scavenging activity, reducing power, and lipid peroxidation inhibition was found among UD-EWPH, FD-EWPH, and SD-EWPH. The results indicated that spray-drying might be suitable to dry antioxidant hydrolysates for its simple, cost-effective, and time-saving process. Moreover, further modeling study of optimized spray-drying processing parameters is needed in order to minimize the emulsifying and foaming property damage.


Egg white protein hydrolysate Freeze-drying Spray-drying Antioxidant Functional properties 



The authors gratefully acknowledge the financial support provided by the earmarked fund for Modern Agro-industry Technology Research System of China (No.nycytx-41-g23). The authors especially thank anonymous reviewers for valuable and critical comments, which greatly improved the quality of the manuscript.


  1. Adler-Nissen, J. (1986). Enzymic hydrolysis of food proteins, vols. 9–56 (pp. 110–169). Barking: Elsevier.Google Scholar
  2. Anandharamakrishnan, C., Rielly, C. D., & Stapley, A. G. F. (2008). Loss of solubility of α-lactalbumin and β-lactoglobulin during the spray drying of whey proteins. LWT Food Science and Technology, 41, 270–277.CrossRefGoogle Scholar
  3. AOAC (2000). Official methods of analysis (17th ed.). Gaithersberg, MD: Association of Official Analytical Chemists.Google Scholar
  4. Belitz, H.-D., Grosch, W., & Schieberle, P. (2009). Food Chemistry (4th revised and extended ed.) (p. 62). Verlag Berlin Heidelberg: Springer.Google Scholar
  5. Cepeda, E., Villaran, M. C., & Aranguiz, N. (1998). Functional properties of Faba Bean (Vicia faba) protein flour dried by spray drying and freeze drying. Journal of Food Engineering, 36, 303–310.CrossRefGoogle Scholar
  6. Chen, H. M., Muramoto, K., Yamaguchi, F., Fujimoto, K., & Nokihara, K. (1998). Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. Journal of Agricultural and Food Chemistry, 46, 49–53.CrossRefGoogle Scholar
  7. Dávalos, A., Miguel, M., Bartolomé, B., & López-Fandiño, R. (2004). Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis. Journal of Food Protection, 67, 1939–1944.Google Scholar
  8. Denavi, G., Tapia-Blácido, D. R., Añón, M. C., Sobral, P. J. A., Mauri, A. N., & Menegalli, F. C. (2009). Effects of drying conditions on some physical properties of soy protein films. Journal of Food Engineering, 90, 341–349.CrossRefGoogle Scholar
  9. Dos Santos, S. D., Martins, V. G., Salas-Mellado, M., & Prentice, C. (2010). Evaluation of functional properties in protein hydrolysates from Bluewing Searobin (Prionotus punctatus) obtained with different microbial enzymes. Food and Bioprocess Technology. doi: 10.1007/s11947-009-0301-0.Google Scholar
  10. Giménez, B., Alemán, A., Montero, P., & Gómez-Guillén, M. C. (2009). Antioxidant and functional properties of gelatin hydrolysates obtained from skin of sole and squid. Food Chemistry, 114, 976–983.CrossRefGoogle Scholar
  11. Guo, H., Kouzuma, Y., & Yonekura, M. (2009). Structures and properties of antioxidative peptides derived from royal jelly protein. Food Chemistry, 113, 238–245.CrossRefGoogle Scholar
  12. Haque, Md K., & Roos, Y. H. (2006). Differences in the physical state and thermal behavior of spray-dried and freeze-dried lactose and lactose/protein mixtures. Innovative Food Science & Emerging Technologies, 7, 62–73.CrossRefGoogle Scholar
  13. Her, J.-Y., Song, C.-S., Lee, S. J., & Lee, K.-G. (2010). Preparation of kanamycin powder by an optimized spray freeze-drying method. Powder Technology, 199, 159–164.CrossRefGoogle Scholar
  14. Kamrul, H. Md, & Roos, Y. H. (2006). Differences in the physical state and thermal behavior of spray-dried and freeze-dried lactose and lactose/protein mixtures. Innovative Food Science & Emerging Technologies, 7, 62–73.CrossRefGoogle Scholar
  15. Kim, S.-Y., Je, J.-Y., & Kim, S.-K. (2007). Purification and characterization of antioxidant peptide from hoki (Johnius belengerii) frame protein by gastrointestinal digestion. The Journal of Nutritional Biochemistry, 18, 31–38.CrossRefGoogle Scholar
  16. Klompong, V., Benjakul, S., Kantachote, D., & Shahidi, F. (2007). Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chemistry, 102, 1317–1327.CrossRefGoogle Scholar
  17. 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.CrossRefGoogle Scholar
  18. Kuropatwa, M., Tolkach, A., & Kulozik, U. (2009). Impact of pH on the interactions between whey and egg white proteins as assessed by the foamability of their mixtures. Food Hydrocolloids, 23, 2174–2181.CrossRefGoogle Scholar
  19. Lechevalier, V., Jeante, R., Arhaliass, A., Legrand, J., & Nau, F. (2007). Egg white drying: Influence of industrial processing steps on protein structure and functionalities. Journal of Food Engineering, 83, 404–413.CrossRefGoogle Scholar
  20. Lee, W. C., & Chen, T. C. (2002). Functional characteristics of egg white solids obtained from papain treated albumen. Journal of Food Engineering, 51, 263–266.CrossRefGoogle Scholar
  21. Li, Y. H., Jiang, B., Zhang, T., Mu, W. M., & Liu, J. (2008). Antioxidant and free radical-scavenging activities of chickpea protein hydrolysate (CPH). Food Chemistry, 106, 444–450.CrossRefGoogle Scholar
  22. Linarès, E., Larré, C., & Popineau, Y. (2001). Freeze- or spray-dried gluten hydrolysates. 1. Biochemical and emulsifying properties as a function of drying process. Journal of Food Engineering, 48, 127–135.CrossRefGoogle Scholar
  23. Liu, J. B., Yu, Z. P., Zhao, W. Z., Lin, S. Y., Wang, E. L., Zhang, Y., et al. (2010a). Isolation and identification of angiotensin-converting enzyme inhibitory peptides from egg white protein hydrolysates. Food Chemistry, 122(4), 1159–1163.CrossRefGoogle Scholar
  24. Liu, Q., Kong, B., Xiong, Y. L., & Xia, X. (2010b). Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis. Food Chemistry, 118, 403–410.CrossRefGoogle Scholar
  25. Ma, Y., Cai, C., Wang, J., & Sun, D.-W. (2006). Enzymatic hydrolysis of corn starch for producing fat mimetics. Journal of Food Engineering, 73, 297–303.CrossRefGoogle Scholar
  26. Mendis, E., Rajapakse, N., & Kim, S. K. (2005). Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. Journal of Agricultural and Food Chemistry, 53, 581–587.CrossRefGoogle Scholar
  27. Miguel, M., Recio, I., Gomez-Ruiz, J. A., Ramos, M., & López-Fandiño, R. (2004). Angiotensin I-converting enzyme inhibitory activity of peptides derived from egg white proteins by enzymatic hydrolysis. Journal of Food Protection, 67, 1914–1920.Google Scholar
  28. Morr, C. V. (1985). Composition, physicochemical and functional properties of reference whey protein concentrates. Journal of Food Science, 50, 1406–1411.CrossRefGoogle Scholar
  29. Moure, A., Domínguez, H., & Parajó, J. C. (2006). Antioxidant properties of ultrafiltration-recovered soy protein fractions from industrial effluents and their hydrolysates. Process Biochemistry, 41, 447–456.CrossRefGoogle Scholar
  30. Nakajima, K., Yoshie-Stark, Y., & Ogushi, M. (2009). Comparison of ACE inhibitory and DPPH radical scavenging activities of fish muscle hydrolysates. Food Chemistry, 114, 844–851.CrossRefGoogle Scholar
  31. Ovissipour, M., Safari, R., Motamedzadegan, A., & Shabanpour, B. (2009). Chemical and biochemical hydrolysis of Persian sturgeon (Acipenser persicus) visceral protein. Food and Bioprocess Technology. doi: 10.1007/s11947-009-0284-x.Google Scholar
  32. Pan, M., Jiang, T. S., & Pan, J. L. (2009). Antioxidant activities of rapeseed protein hydrolysates. Food and Bioprocess Technology. doi: 10.1007/s11947-009-0206-y.Google Scholar
  33. 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.CrossRefGoogle Scholar
  34. Pellegrini, A., Hulsmeier, A. J., Hunziker, P., & Thomas, U. (2004). Proteolytic fragments of ovalbumin display antimicrobial activity. Biochimica et Biophysica Acta, 1672, 76–85.CrossRefGoogle Scholar
  35. Qian, Z.-J., Jung, W.-K., & Kim, S.-K. (2008). Free radical scavenging activity of a novel antioxidative peptide purified from hydrolysate of bullfrog skin, Rana catesbeiana Shaw. Bioresource Technology, 99, 1690–1698.CrossRefGoogle Scholar
  36. Ranathunga, S., Rajapakse, N., & Kim, S.-K. (2006). Purification and characterization of antioxidative peptide derived from muscle of conger eel (Conger myriaster). European Food Research and Technology, 222, 310–315.CrossRefGoogle Scholar
  37. Rumbo, M., Chirdo, F. G., Fossati, C. A., & Anon, M. C. (1996). Analysis of structural properties and immunochemical reactivity of heat-treated ovalbumin. Journal of Agricultural and Food Chemistry, 44, 3793–3798.CrossRefGoogle Scholar
  38. Shahidi, F., Xiao-Quing, H., & Synowiecki, J. (1995). Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chemistry, 53, 285–293.CrossRefGoogle Scholar
  39. Shahidi, F., Liyana-Pathirana, C. M., & Wall, D. S. (2006). Antioxidant activity of white and black sesame seeds and their hull fractions. Food Chemistry, 99, 478–483.CrossRefGoogle Scholar
  40. Sun, M. J., Chi, Y. J., & Zhang, M. J. (2008). Technology for improving foaming properties of egg albumen powders. Transactions of the CSAE, 24(11), 274–278 (in china).Google Scholar
  41. Tang, S., Hettiarachchy, N. S., Horax, R., & Eswaranandam, S. (2003). Physicochemical properties and functionality of rice bran protein hydrolyzate prepared from heat-stabilized defatted rice bran with the aid of enzymes. Journal of Food Science, 68, 152–157.CrossRefGoogle Scholar
  42. Van der Plancken, I., Van Loey, A., & Hendrickx, M. E. (2007). Foaming properties of egg white proteins affected by heat or high pressure treatment. Journal of Food Engineering, 78, 1410–1426.CrossRefGoogle Scholar
  43. Waniska, R. D. & Kinsella, J. E. (1979). Foaming properties of proteins: Evaluation of a column aeration apparatus using ovalbumin. Journal of Food Science, 44, 1398–1411.CrossRefGoogle Scholar
  44. 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.CrossRefGoogle Scholar
  45. Xie, Z., Huang, J., Xu, X., & Jin, Z. (2008). Antioxidant activity of peptides isolated from alfalfa leaf protein hydrolysate. Food Chemistry, 111, 370–376.CrossRefGoogle Scholar
  46. Yang, B., Yang, H., Li, J., Li, Z., & Jiang, Y. (2011). Amino acid composition, molecular weight distribution and antioxidant activity of protein hydrolysates of soy sauce lees. Food Chemistry, 124, 551–555.CrossRefGoogle Scholar
  47. Yen, G. C., & Chen, H. Y. (1995). Antioxidant activity of various tea extract in relation to their antimutagenicity. Journal of Agricultural and Food Chemistry, 43, 27–32.CrossRefGoogle Scholar
  48. Yu, B., & Chi, Y. J. (2009). Effect of glycosylation on molecular characteristics and emulsifying properties of ovalbumin. Scientia Agricultura Sinica, 42(7), 2499–2504 (in china).Google Scholar
  49. Zhang, R. D., Chi, Y. J., Chen, C., & Ruan, C. Q. (2010). Study on the antioxidant and angiotensin-I converting enzyme inhibitory activities of proteinase hydrolysates from egg white. Acta Nutrimenta Sinica, 32(4), 345–349 (in China).Google Scholar
  50. Zhu, K. X., Zhou, H. M., & Qian, H. F. (2006). Antioxidant and free radical-scavenging activities of wheat germ protein hydrolysates (WGPH) prepared with alcalase. Process Biochemistry, 41, 1296–1302.CrossRefGoogle Scholar

Copyright information

© Springer Science + Business Media, LLC 2011

Authors and Affiliations

  1. 1.College of Food ScienceNortheast Agricultural UniversityHarbinPeople’s Republic of China

Personalised recommendations