Comparisons on the Functional Properties and Antioxidant Activity of Spray-Dried and Freeze-Dried Egg White Protein Hydrolysate
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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.
KeywordsEgg 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.
- Adler-Nissen, J. (1986). Enzymic hydrolysis of food proteins, vols. 9–56 (pp. 110–169). Barking: Elsevier.Google Scholar
- AOAC (2000). Official methods of analysis (17th ed.). Gaithersberg, MD: Association of Official Analytical Chemists.Google Scholar
- Belitz, H.-D., Grosch, W., & Schieberle, P. (2009). Food Chemistry (4th revised and extended ed.) (p. 62). Verlag Berlin Heidelberg: Springer.Google Scholar
- 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
- 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
- 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
- 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
- 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
- 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
- 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