Mechanism of differences in characteristics of thick/thin egg whites during storage: Physicochemical, functional and molecular structure characteristics analysis

Huang, Qun; Liu, Lan; Wu, Yongxiang; Huang, Xiang; Wang, Guoze; Song, Hongbo; Geng, Fang; Luo, Peng

doi:10.1016/j.foodchem.2021.130828

Cited by 41 publications

(22 citation statements)

References 35 publications

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“…Generally, the EAI of modified EM proteins in Group 3 and Group 4 was better than that of Control and Group 1. This suggested that higher EAI, induced by freshness deteriorations of EM samples, which were subjected to refrigeration storage for 20–30 days after defrosting treatment, might be associated with more partial structural expansion of EW protein, exposure of hydrophobic groups and electrostatic interactions at the oil/water interface (Huang et al ., 2022). ESI refers protein capacity and oil to form a strong oil and water emulsion.…”

Section: Resultsmentioning

confidence: 99%

Effect of refrigeration storage on functional properties and structure of egg white after defrosting treatments

Dai¹,

Xia²,

Huang

et al. 2022

Int J of Food Sci Tech

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The changes in refrigeration storage after defrosting treatments on functional properties and structure of egg white (EW) were investigated in this study. The foaming properties and surface hydrophobicity decreased significantly (P < 0.05), whereas the free thiol content of EW increased during prolonged refrigeration storage after defrosting treatments. The values of emulsifying activity index were slightly higher in EM subjected to refrigeration storage for 20-30 days after defrosting treatments (P < 0.05). The texture profiles showed that the cooked EW gel subjected to refrigeration storage for 20 days after defrosting treatments, reached the minimum hardness, springiness and gumminess values vs. that of Control and Group 1. Additionally, scanning electron microscope (SEM) reflected that more and larger protein aggregates as well as irregular structure in EM during prolonged refrigeration storage after defrosting treatments. The increase in free sulfhydryl group and decrease in surface hydrophobicity tended to cause protein oxidation, aggregation and degradation, leading to deterioration of functional properties in EW following refrigeration storage after defrosting treatments. The results of this study indicate that it is important to use the EW of Control and Group 1 without any detrimental effects on functional and morphology properties in food processing industry.

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Section: Resultsmentioning

confidence: 99%

Effect of refrigeration storage on functional properties and structure of egg white after defrosting treatments

Dai¹,

Xia²,

Huang

et al. 2022

Int J of Food Sci Tech

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“…Therefore, the structure of EWP compound could be characterized by FT‐IR. A broad absorption feature peak appeared near 3320 cm −1 (Figure 6), corresponding to the amide A band, which was caused by N‐H or O‐H stretching vibrations (Huang, Huang, et al., 2021). As the glycosylation reaction progressed, the intensity of optical transmittance (opposite of absorbance) showed a downward trend followed by an upward trend, with the lowest optical transmittance corresponding to BCE‐150.…”

Section: Resultsmentioning

confidence: 99%

“…The determination of surface hydrophobicity was slightly modified according to the method of Huang, Liu, et al. (2021). To 1 ml of the sample with protein concentration of 1 mg/ml, 200 µl of bromophenol blue solution (BPB, 1 mg/ml) was added and mixed well.…”

Section: Methodsmentioning

confidence: 99%

“…The lyophilized powder samples were weighed and dissolved in phosphate buffer solution until protein concentration was 5 mg/ml. BCE and blank sample solutions were centrifuged at 10,000 r/min and 4℃ for 15 min, and protein concentration was determined by the biuret method (Huang, Huang, et al., 2021). Solubility was expressed as the percentage of protein content in the supernatant after centrifugation to the protein content in the solution before centrifugation.…”

Section: Methodsmentioning

confidence: 99%

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Effect of ball milling‐assisted glycosylation modification on the structure and foaming property of egg white protein

Liu

Qia

et al. 2022

Journal of Food Science

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The effect of different glycosylation degrees on molecular structure and foaming property of egg white protein (EWP) was investigated using ball milling-assisted glycosylation. The results showed the foaming ability (FA) and foam stability (FS) of EWP improved when the degree of glycosylation was increased. In particular, FA of ball milling-assisted glycosylation of EWP enhanced by 39.9% and 28.8%, and the FS increased by 28.7% and 24.0% compared with EWP and ball milling egg white protein (BE) at 150 min of reaction.Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis could reflect the grafting degree of EWP and glucose molecules from the side. When EWP was fully grafted with glucose, endogenous fluorescence and free sulfhydryl groups indicated that tertiary structure of EWP was depolymerized, and Fourier transform infrared spectroscopy showed the secondary structure tended to change from order to disorder. The results of this study indicated that ball milling-assisted glycosylation modification was a practical method to improve the foaming property of EWP.

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“…Prepared samples were diluted to 0.2 mg/mL with water of the corresponding pH value. The ζ-potential and mean particle size of each group of samples were measured by a nanoparticle sizer (ZS90; Malvern Zetasizer Nano, Malvern, UK) ( Huang et al, 2022 ; Xiong et al, 2021 ). The measurement temperature was 25 °C and the parameters were set according to the instrument's manual.…”

Section: Methodsmentioning

confidence: 99%

Ultrasound-assisted pH-shifting remodels egg-yolk low-density lipoprotein to enable construction of a stable aqueous solution of vitamin D3

Wang²,

Wang³

et al. 2022

Current Research in Food Science

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Mechanism of differences in characteristics of thick/thin egg whites during storage: Physicochemical, functional and molecular structure characteristics analysis

Cited by 41 publications

References 35 publications

Effect of refrigeration storage on functional properties and structure of egg white after defrosting treatments

Effect of refrigeration storage on functional properties and structure of egg white after defrosting treatments

Effect of ball milling‐assisted glycosylation modification on the structure and foaming property of egg white protein

Ultrasound-assisted pH-shifting remodels egg-yolk low-density lipoprotein to enable construction of a stable aqueous solution of vitamin D3

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