Functional properties of ovalbumin glycosylated with carboxymethyl cellulose of different substitution degree

An, Yaping; Cui, Bing; Wang, Yuntao; Jin, Weiping; Geng, Xiaopeng; Yan, Xiangxing; Li, Bin

doi:10.1016/j.foodhyd.2014.01.028

Cited by 64 publications

(38 citation statements)

References 43 publications

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“…[3] It is an important food ingredient, which is frequently used as a surfactant protein in the food industry to improve and maintain the quality (texture and volume) of aerated food. [4] Much research has been conducted in order to improve the functional properties of OVA, [5] including phosphorylation, [6,7] glycosylation, [8][9][10] enzymatic modification, [11] and high pressure. [5] Compared to other modification methods, glycosylation is an effective method to improve the food-use functional properties of OVA.…”

Section: Introductionmentioning

confidence: 99%

Enzymolysis and glycosylation synergistic modified ovalbumin: functional and structural characteristics

Liu

Prakash

et al. 2018

International Journal of Food Properties

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The functional and structural properties of enzymatic hydrolysis and glycosylation synergistic modified ovalbumin (OVA) were investigated. The results showed that hydrolysis and glycosylation had synergetic effects on emulsifying and foaming properties, water and oil-binding capacity of OVA. And hydrolysis and glycosylation also could improve gel strength and thermal properties of OVA. Polyacrylamide gel electrophoresis analysis implied that the formation of 20.1 kDa~29 kDa Maillard reaction products (MRPs). UV absorption and Fourier Transform Infrared spectroscopy analyses confirmed that enzymatic hydrolysis and glycosylation could change the secondary structure of OVA. Moreover, hydrolysis and glycosylation could produce OVA with compact and orderly network structure.

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Section: Introductionmentioning

confidence: 99%

Enzymolysis and glycosylation synergistic modified ovalbumin: functional and structural characteristics

Liu

Prakash

et al. 2018

International Journal of Food Properties

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“…Although the denaturation temperature at the second peak remained consistent, the increased enthalpy suggested a higher content of ovalbumin in the GML feed-supplemented groups, especially the 450 mg kg −1 GML group which showed a significant increase in enthalpy. Ovalbumin has a high amount of sulfur-containing amino acids, including 15 methionine residues with one disulfide bond and four sulfhydryl groups 26 and ovalbumin, as the main constituent of EWP, strongly affects egg white gelation behavior, foaming properties and emulsion stability. wileyonlinelibrary.com/jsfa The gelation of egg white is a complex process, involving protein denaturation, aggregation and the formation of a gel network.…”

Section: Discussionmentioning

confidence: 99%

Dietary glycerol monolaurate supplementation for the modification of functional properties of egg white protein

et al. 2019

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BACKGROUND Understanding the interactions between feed additives and the functional properties of egg white protein (EWP) may offer novel insights into the effects of feed additives on laying hens and may provide an alternative for modification of the functional properties of EWP by using laying hens as bioreactors. Glycerol monolaurate (GML) is widely used in the food industry as an effective antibacterial emulsifier. In this work, the effects of three doses of dietary GML supplementation (150, 300, and 450 mg kg−1 hen) on the functional properties of EWP were investigated. RESULTS The hardness of EWP gels was significantly improved by 300 and 450 mg kg−1 GML supplementation. Foaming capacity (FC) and foaming stability (FS) were increased after GML treatment; 450 mg kg−1 GML supplementation showed the most significant improvements, with 44.82% in FC and 23.39% in FS. Stabilization of EWP‐oil emulsions was also improved, supported by a slowed creaming process and the formation of smaller oil droplets. The heat denaturation temperature and rheological properties were also modified by dietary GML supplementation, implying improved thermal stability. CONCLUSION Our study demonstrated that GML supplementation has the potential to modify the functional properties of EWP, broadening the application of GML and providing a new perspective for evaluation of the efficacy of feed additives. © 2019 Society of Chemical Industry

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“…It was then centrifuged at 4000 ×g for 10 min at 25 °C. After centrifugation, the weight of the gel was measured again, and the WHC was calculated by the rate (%) of gel weight before and after centrifugation (An et al, ; Bao et al, ). Five replicates were performed for each gel sample.…”

Section: Methodsmentioning

confidence: 99%

“…Ovalbumin (OVA) is widely applied in the food industry, and it is one of the representative proteins that are used as a model in food research. The well‐known molecular structure and ease of acquisition make OVA an ideal reference for studying the properties of other food proteins (An et al, ; Liu et al, ). The effect of different treatments and modifications of OVA is also a hotspot of study because the results could provide important information on the understanding of the structure and property changes of food proteins during food processing and preservation.…”

Section: Introductionmentioning

confidence: 99%

“…It has been demonstrated that phosphorylation could increase the surface charges and intermolecular repulsion, thereby improving the emulsifying ability and stability (Xiong & Ma, ; Xiong, Zhang, & Ma, ). The conjugation of OVA with CMC significantly increased the emulsifying capacity and foam stability, but the foaming ability decreased (An et al, ).…”

Section: Introductionmentioning

confidence: 99%

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Effect of hydroxyl radical-induced oxidation on the structure and heat-induced gel properties of ovalbumin

Geng

Huang

et al. 2018

J Food Process Preserv

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The present study is aimed to investigate the effect of hydroxyl radical‐induced oxidation on the structure and gel properties of chicken ovalbumin. With the increase in oxidation time and H2O2 dose, the carbonyl content in ovalbumin increased, while the free sulfhydryl content decreased. The effect of oxidation on the structure of ovalbumin was examined, and the results indicated that the disorder level increased. Oxidation of ovalbumin lowered the solubility, and the viscosity of the solution decreased significantly. Oxidation weakened the water holding capacity and gel hardness, as well as resulting in significant changes in the microstructure of ovalbumin gels. Hydroxyl radical‐induced oxidation caused destabilization of the ovalbumin structure, thereby affecting the heat‐induced gel properties. Practical applications The present study demonstrated the effect of hydroxyl radical‐induced oxidation on chicken OVA, concluding that the oxidation might be one of the primary reasons for the degradation of its gel properties. Consequently, avoiding protein oxidation during storage and processing would help maintain the functional properties of the chicken egg white. Therefore, this study provides important information for the research and application of ovalbumin.

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Functional properties of ovalbumin glycosylated with carboxymethyl cellulose of different substitution degree

Cited by 64 publications

References 43 publications

Enzymolysis and glycosylation synergistic modified ovalbumin: functional and structural characteristics

Enzymolysis and glycosylation synergistic modified ovalbumin: functional and structural characteristics

Dietary glycerol monolaurate supplementation for the modification of functional properties of egg white protein

Effect of hydroxyl radical-induced oxidation on the structure and heat-induced gel properties of ovalbumin

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