Mechanism of ultrasound and tea polyphenol assisted ultrasound modification of egg white protein gel

被引:94
作者
Xue, Hui [1 ]
Tu, Yonggang [3 ]
Zhang, Guowen [2 ]
Xin, Xiaojuan [1 ]
Hu, Hui [1 ]
Qiu, Wei [1 ]
Ruan, Dandan [4 ]
Zhao, Yan [3 ]
机构
[1] Nanchang Univ, Engn Res Ctr Biomass Convers, Minist Educ, Nanchang 330047, Jiangxi, Peoples R China
[2] Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China
[3] Jiangxi Agr Univ, Jiangxi Key Lab Nat Prod & Funct Food, Nanchang 330045, Jiangxi, Peoples R China
[4] Hubei Shendan Hlth Food Co LTD, Xiaogan 430000, Peoples R China
基金
中国国家自然科学基金;
关键词
Ultrasound; Egg white; Tea polyphenols; Modify; Gelation;
D O I
10.1016/j.ultsonch.2021.105857
中图分类号
O42 [声学];
学科分类号
070206 ; 082403 ;
摘要
In order to improve the characteristics of egg white protein gel and the stability of egg white protein gel products. In this work, the changes of the texture, physicochemical properties, secondary structure and microstructure of ultrasound modified egg white protein gel (UEP) and tea polyphenols (TP) assisted ultrasound modification of egg white protein gel (TUEP) with different ultrasonic power (0-360 W) were studied. With the increase of ultrasonic power, soluble protein, surface hydrophobicity and disulfide bonds of TUEP and UEP showed an increasing trend. In particular, with the increase of ultrasonic power, the content of intramolecular beta-sheets and alpha-helices of TUEP showed an increasing trend, and significantly improved the relaxation time and microstructure, thus enhancing TUEP gel stability. In addition, the hardness and water holding capacity (WHC) of TUEP and UEP can be increased by ultrasonic treatment, and when the ultrasonic power reached 120 W, the hardness and WHC reached the maximum. The hardness and WHC of TUEP were significantly better than that of UEP. SDSPAGE results showed that the peptide chain of protein without being broken under ultrasonic treatment. Ultrasonic treatment can improve the gel strength of egg white protein by promoting the cross-linking of proteins to form a dense gel structure, and egg white protein gel form more disulfide bonds and a more stable gel conformation under TP assisted ultrasound. In conclusion, ultrasound and TP assisted ultrasound modification of egg white protein gel is a reliable technique, which can improve the value of egg white protein in food processing.
引用
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页数:10
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