Emulsifying stability of enzymatically hydrolyzed egg yolk granules and structural analysis

2020 ◽  
Vol 101 ◽  
pp. 105521 ◽  
Author(s):  
Qin Li ◽  
Shitao Tang ◽  
Fayez Khalaf Mourad ◽  
Wenjie Zou ◽  
Lizhi Lu ◽  
...  
2018 ◽  
Vol 268 ◽  
pp. 369-377 ◽  
Author(s):  
Meram Chalamaiah ◽  
Yussef Esparza ◽  
Hui Hong ◽  
Feral Temelli ◽  
Jianping Wu

Foods ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 2238
Author(s):  
Xin Li ◽  
Yue-Meng Wang ◽  
Cheng-Feng Sun ◽  
Jian-Hao Lv ◽  
Yan-Jun Yang

As an excellent foaming agent, egg white protein (EWP) is always contaminated by egg yolk in the industrial processing, therefore, decreasing its foaming properties. The aim of this study was to simulate the industrial EWP (egg white protein with 0.5% w/w of egg yolk) and characterize their foaming and structural properties when hydrolyzed by two types of esterase (lipase and phospholipase A2). Results showed that egg yolk plasma might have been the main fraction, which led to the poor foaming properties of the contaminated egg white protein compared with egg yolk granules. After hydrolyzation, both foamability and foam stability of investigated systems thereof (egg white protein with egg yolk, egg white protein with egg yolk plasma, and egg white protein with egg yolk granules) increased significantly compared with unhydrolyzed ones. However, phospholipids A2 (PLP) seemed to be more effective on increasing their foaming properties as compared to those systems hydrolyzed by lipase (LP). The schematic diagrams of yolk fractions were proposed to explain the aggregation and dispersed behavior exposed in their changes of structures after hydrolysis, suggesting the aggregated effects of LP on yolk plasma and destructive effects of PLP on yolk granules, which may directly influence their foaming properties.


1992 ◽  
Vol 57 (6) ◽  
pp. 1323-1326 ◽  
Author(s):  
D. CAUSERET ◽  
E. MATRINGE ◽  
D. LORIENT
Keyword(s):  
Egg Yolk ◽  

1961 ◽  
Vol 39 (8) ◽  
pp. 1295-1307 ◽  
Author(s):  
R. W. Burley ◽  
W. H. Cook

The yolk granules from hen's egg represent on a dry basis 23% of the yolk solids, and they contain about 90% of the protein phosphorus, 95% of the iron, and nearly 70% of the calcium in yolk. Ultracentrifugal and other analyses on solutions of the granules show that they are 70% α- and β-lipovitellin in an approximate ratio of 1:1.8, 16% phosvitin, and 12% low-density lipoprotein. The properties and composition of the two lipovitellins isolated from the granules are the same as those isolated from solutions of whole yolk. Further purification reduces the protein phosphorus in α-lipovitellin to 0.50% and in β-lipovitellin to 0.27%, and this confirms that α-vitellin has a higher phosphorus content. Experiments at low temperature suggest that phosvitin exists in the granules as a high molecular weight complex.


2021 ◽  
pp. 131077
Author(s):  
Teng Li ◽  
Huanhuan Su ◽  
Jiaqian Zhu ◽  
Yuying Fu
Keyword(s):  
Egg Yolk ◽  

1964 ◽  
Vol 42 (8) ◽  
pp. 1203-1215 ◽  
Author(s):  
M. W. Radomski ◽  
W. H. Cook

The two components of lipovitellin and the three major components of yolk granules, phosvitin, α- and β-lipovitellin, have been separated by gradient elution chromatography on TEAE-cellulose. A 0.2 M phosphate buffer (pH 6.8) had the necessary ionic strength to dissolve these proteins and when applied in this solvent all components except β-lipovitellin were retained by the column. A linear gradient of ionic strength (limit buffer 0.2 M phosphate plus 0.5 M NaCl) was used to remove the other components. Recovery was essentially complete and the composition and properties of the individual components were similar to those obtained by previous chromatographic methods that gave only partial recovery. An additional component eluted after α-lipovitellin and before phosvitin, previously observed in Dowex-1 separations, was also observed by the present method. The composition, sedimentation behavior, and absorption spectra of this component indicate that it is a soluble complex of phosvitin and lipovitellin. When granules are dissolved in alkaline solvents (pH 9.4) of low ionic strength (0.05), phosvitin is not evident as a separate component during ultracentrifugation, but appears as the ionic strength is increased.


2019 ◽  
Vol 100 (4) ◽  
pp. 1470-1478 ◽  
Author(s):  
Anheng Wang ◽  
Zhigang Xiao ◽  
Jingjing Wang ◽  
Guijie Li ◽  
Lijuan Wang

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