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測(cè)量應(yīng)用案例-20190606
閱讀：149 發(fā)布時(shí)間：2019-6-17
作者： Farhad Alavia, Zahra Emam-Djomeha,b,d, Shima Momena, Mehdi Mohammadiana, Maryam Salamia, Ali Akbar Moosavi-Movahedic,d
aDepartment of Food Science, Engineering and Technology, College of Agriculture & Natural Resources, University of Tehran, Karaj Campus, Karaj, Iran
bTransfer Phenomena Laboratory (TPL), Controlled Release Center, Department of Food Science, Engineering and Technology, College of Agriculture & Natural Resources, University of Tehran, Karaj Campus, Karaj, Iran
cInstitute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
dCenter of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran
摘要：This study investigated the impact of free radical-induced aggregation by a redox pair (ascorbic acid + H2O2) on physicochemical characteristics, structure, and rheology as well as the emulsifying and foaming capacity of egg white protein (EWP). In general, this treatment led to oxidize the free SH groups, a little change in secondary structure, increasing surface hydrophobic (H0) and ζ-potential as well induce aggregation of egg white protein through disulfide cross-linking. The pH at which the oxidative aggregation reaction was performed had a significant effect on the functionality of the EWP. The EWP aggregated at pH 11 had a very high apparent viscosity, which justified by its greater H0, higher aggregation yield and larger aggregates with high effective volume, as confirmed by SDS-PAGE and AFM. Furthermore, emulsions prepared by aggregated EWP samples, particularly the EWP aggregated at pH 11, showed higher stability against droplet flocculation and phase separation during storage for 30 days at various pH (4–7) and salt concentration (0–200?mM) as compared to emulsions made with native EWP, presumably due to create a more viscoelastic film with promoted steric hindrance on oil droplets. Moreover, a dramatically enhanced foam stability was obtained by the EWP aggregated at pH 11. This study suggested that radical induced aggregation has a potential to improve the interface-related properties of egg white protein.