Effects of ethanol treatment on the physicochemical properties, microstructure and protein structures of egg yolk gels

被引:30
作者
Xin, Xiaojuan [1 ]
Zhang, Guowen [2 ]
Xue, Hui [1 ]
Qiu, Wei [1 ]
Hu, Hui [1 ]
Tu, Yonggang [3 ,4 ]
Zhao, Yan [3 ,4 ]
机构
[1] Nanchang Univ, Engn Res Ctr Biomass Convers, Minist Educ, Nanchang 330047, Peoples R China
[2] Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Peoples R China
[3] Jiangxi Agr Univ, Jiangxi Key Lab Nat Prod & Funct Food, Nanchang 330045, Peoples R China
[4] Jiangxi Agr Univ, Agr Prod Proc & Qual Control Engn Lab Jiangxi, Nanchang 330045, Peoples R China
关键词
Egg yolk gels; Ethanol treatment; Protein unfolding; Protein aggregation; INTERMOLECULAR FORCE; CHEMICAL-COMPOSITION; BETA-LACTOGLOBULIN; GELATION; WATER; FAT;
D O I
10.1016/j.foodchem.2022.135041
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The aim of this study was to investigate the effect of ethanol treatment on the properties of egg yolk gels (EYG). The hardness of EYG showed an increasing trend, and the changes in free sulfhydryl groups manifested that ethanol treatment facilitated the formation of disulfide bonds. Environment scanning electron microscopy revealed that the degree of protein aggregation increased. Low-field nuclear magnetic resonance results indicated that ethanol treatment promoted the conversion of immobile water or lipids to free water or lipids. Moreover, the increase in the absolute of zeta potential was accompanied by the decrease in surface hydrophobicity, and the secondary structure of native egg yolk (EY) proteins underwent changes with ethanol treatment. Overall, these results demonstrated that ethanol treatment induced the structural unfolding and aggregation of EY proteins, and facilitated the better stability of the gel structures. The impact of the ethanol on the EYG increased with the concentration.
引用
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页数:10
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共 45 条
[1]   Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes [J].
Alizadeh-Pasdar, N ;
Li-Chan, ECY .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2000, 48 (02) :328-334
[2]   Egg yolk: structures, functionalities and processes [J].
Anton, Marc .
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 2013, 93 (12) :2871-2880
[3]   STRUCTURE OF YOLK OF HENS EGG AS STUDIED BY ELECTRON MICROSCOPY .1. YOLK OF UNINCUBATED EGG [J].
BELLAIRS, R .
JOURNAL OF BIOPHYSICAL AND BIOCHEMICAL CYTOLOGY, 1961, 11 (01) :207-&
[4]   DETERMINATION OF SH-GROUPS AND SS-GROUPS IN SOME FOOD PROTEINS USING ELLMANS REAGENT [J].
BEVERIDGE, T ;
TOMA, SJ ;
NAKAI, S .
JOURNAL OF FOOD SCIENCE, 1974, 39 (01) :49-51
[5]   Food protein-based materials as nutraceutical delivery systems [J].
Chen, LY ;
Remondetto, GE ;
Subirade, M .
TRENDS IN FOOD SCIENCE & TECHNOLOGY, 2006, 17 (05) :272-283
[6]   Change of the structure and the digestibility of myofibrillar proteins in Nanjing dry-cured duck during processing [J].
Du, Xiaojing ;
Sun, Yangying ;
Pan, Daodong ;
Wang, Ying ;
Ou, Changrong ;
Cao, Jinxuan .
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 2018, 98 (08) :3140-3147
[7]   Ethanol induced changes in structural, morphological, and functional properties of whey proteins isolates: Influence of ethanol concentration [J].
Feng, Yangyang ;
Ma, Xiaoli ;
Kong, Baohua ;
Chen, Qian ;
Liu, Qian .
FOOD HYDROCOLLOIDS, 2021, 111
[8]   Influence of bio-active terpenes on the characteristics and functional properties of egg yolk [J].
Gouda, Mostafa ;
Zu, Linlin ;
Ma, Sumin ;
Sheng, Long ;
Ma, Meihu .
FOOD HYDROCOLLOIDS, 2018, 80 :222-230
[9]   Alcohol-induced denaturation of β-lactoglobulin:: A close correlation to the alcohol-induced α-helix formation of melittin [J].
Hirota-Nakaoka, N ;
Goto, Y .
BIOORGANIC & MEDICINAL CHEMISTRY, 1999, 7 (01) :67-73
[10]   Kappa-carrageenan enhances the gelation and structural changes of egg yolk via electrostatic interactions with yolk protein [J].
Huang, Min ;
Mao, Yuzhu ;
Li, Hongliang ;
Yang, Hongshun .
FOOD CHEMISTRY, 2021, 360