Enhancement of emulsification properties by modulation of egg white protein fibril structure with different heating times

Dong, Wanyi; Zhang, Xinyue; Ding, Lixian; Liu, Cong; Ai, Minhui; Jin, Yongguo; Isobe, Kazuhiro; Handa, Akihiro; Cai, Zhaoxia

doi:10.1016/j.foodhyd.2022.108203

Cited by 31 publications

(9 citation statements)

References 45 publications

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“…The above study showed that different heating methods and time affected the conformation of protein in samples. It was proved that the structure changes could influence the efficacy of evolving oil droplets due to the different of morphology and surface groups, thus, the functional properties of protein might be affected (Dong et al, 2023). The emulsion capacity (EC) reflected the adsorption capacity of protein at the water–oil interface, and the emulsion stability (ES) indicated the retention ability of protein at the oil–water interface after emulsion (Dong et al, 2023).…”

Section: Resultsmentioning

confidence: 99%

Impact of steaming and roasting heat‐treatment on physico‐chemical and functional properties of walnut kernel

Zhao,

Ren,

Liu

et al. 2023

J Americ Oil Chem Soc

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In this study, the effect of steaming and roasting treatment on the physicochemical and functional properties of walnut kernel at 95°C for different time (15, 20, and 30 min) was investigated. Steaming and roasting treatments significantly increased the enthalpy change for protein denaturation, in‐vitro digestibility, viscosity, storage modulus (G′) and loss modulus (G″) (p < 0.05), the order from high to low was steaming (7.11–8.69 J g−1; the gastric and intestinal digestion: 1.21%–17.83% and 1.51%–27.31%, respectively; 134.04–450.49 Pa s; 214.28–1047.14 and 61.72–196.09 Pa) > roasting (6.24–7.07 J g−1; the gastric and intestinal digestion: 1.26–15.42% and 1.21–22.37% a, respectively; 16.92–86.07 Pa s; 6.58–209.85 and 3.08–67.14) > untreated (4.53 J g−1; the gastric and intestinal digestion: 0.24%–4.18% and 1.00–7.58%, respectively; 17.06 Pa s; 5.78 and 1.79 Pa). All samples contained the essential amino acids, the amino acid score of samples by steaming was the highest. In addition, the protein of walnut kernel after heating treatment contained more α‐helix and random coil structures compared to the untreated sample, while β‐sheet and β‐turns structures decreased. Moreover, the thermal treatment could cause the changes of the water/oil holding capacity, foaming and emulsifying properties of walnut kernel flour. When there were differences between the results of steaming and roasting samples, it was concluded that the water played an important role in steaming. These results suggested that the thermal treatment as an effective approach could improve the physico‐chemical, structural and functional properties of walnut kernel and be potentially applied in the food processing.

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Section: Resultsmentioning

confidence: 99%

Impact of steaming and roasting heat‐treatment on physico‐chemical and functional properties of walnut kernel

Zhao,

Ren,

Liu

et al. 2023

J Americ Oil Chem Soc

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“…The upsurge in creaming index (CI) further confirmed that the emulsification of the EWP-stabilized emulsion intensified with the extension of time (Figure 5c). This primarily originated from the comparatively feeble interfacial attributes of egg white proteins, rendering them less proficient at upholding extended stability after their adsorption at the oil-water interface [5]. After storage of 30 days, the covalent complex stabilized emulsion exhibited good storage stability.…”

Section: Emulsion Stabilitymentioning

confidence: 99%

“…Egg white proteins, in their unique globular conformation, jointly have both hydrophilic and hydrophobic sites on their surfaces, which potentially facilitate their rapid adsorption at the oil-water interface and inhibit droplet aggregation through the formation of an interfacial film, accompanied by the initiation of electrostatic interactions and steric repulsion [4]. However, the majority of the hydrophobic groups within egg white proteins remain internal to the molecule, resulting in limited surface hydrophobicity and poor emulsification properties, and this constraint curtails the application of egg white proteins in the emulsification systems [5]. Meanwhile, the constrained interfacial stability of egg white proteins at the oil-water interface poses a critical challenge in the development of egg white protein-based emulsion products.…”

Section: Introductionmentioning

confidence: 99%

Egg White Protein–Proanthocyanin Complexes Stabilized Emulsions: Investigation of Physical Stability, Digestion Kinetics, and Free Fatty Acid Release Dynamics

Zhang,

Li,

Yang

et al. 2024

Molecules

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Egg white proteins pose notable limitations in emulsion applications due to their inadequate wettability and interfacial instability. Polyphenol-driven alterations in proteins serve as an effective strategy for optimizing their properties. Herein, covalent and non-covalent complexes of egg white proteins-proanthocyanins were synthesized. The analysis of structural alterations, amino acid side chains and wettability was performed. The superior wettability (80.00° ± 2.23°) and rigid structure (2.95 GPa) of covalent complexes established favorable conditions for their utilization in emulsions. Furthermore, stability evaluation, digestion kinetics, free fatty acid (FFA) release kinetics, and correlation analysis were explored to unravel the impact of covalent and non-covalent modification on emulsion stability, dynamic digestion process, and interlinkages. Emulsion stabilized by covalent complex exhibited exceptional stabilization properties, and FFA release kinetics followed both first-order and Korsmeyer–Peppas models. This study offers valuable insights into the application of complexes of proteins-polyphenols in emulsion systems and introduces an innovative approach for analyzing the dynamics of the emulsion digestion process.

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“…Furthermore, Li and Li [ 17 ] revealed a positive correlation between WHC and gel strength in EW gels, attributed to the presence of a compact gel network. The acid/heat-induced aggregation of EW proteins exposes more hydrophobic and charged groups on the surface of fibrillar protein aggregates, thereby enhancing interfacial adsorption activity [ 18 ]. These interconnected properties and intermolecular interactions collectively contribute to shaping the overall functionality of EW gels.…”

Section: Gelation Of Ew Proteinsmentioning

confidence: 99%

Chicken Egg White Gels: Fabrication, Modification, and Applications in Foods and Oral Nutraceutical Delivery

Li,

Wang,

Chang

et al. 2024

Foods

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Chicken egg white (EW) proteins possess various useful techno-functionalities, including foaming, gelling or coagulating, and emulsifying. The gelling property is one of the most important functionalities of EW proteins, affecting their versatile applications in the food and pharmaceutical industries. However, it is challenging to develop high-quality gelled foods and innovative nutraceutical supplements using native EW and its proteins. This review describes the gelling properties of EW proteins. It discusses the development and action mechanism of the physical, chemical, and biological methods and exogenous substances used in the modification of EW gels. Two main applications of EW gels, i.e., gelling agents in foods and gel-type carriers for nutraceutical delivery, are systematically summarized and discussed. In addition, the research and technological gaps between modified EW gels and their applications are highlighted. By reviewing the new modification strategies and application trends of EW gels, this paper provides insights into the development of EW gel-derived products with new and functional features.

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Enhancement of emulsification properties by modulation of egg white protein fibril structure with different heating times

Cited by 31 publications

References 45 publications

Impact of steaming and roasting heat‐treatment on physico‐chemical and functional properties of walnut kernel

Impact of steaming and roasting heat‐treatment on physico‐chemical and functional properties of walnut kernel

Egg White Protein–Proanthocyanin Complexes Stabilized Emulsions: Investigation of Physical Stability, Digestion Kinetics, and Free Fatty Acid Release Dynamics

Chicken Egg White Gels: Fabrication, Modification, and Applications in Foods and Oral Nutraceutical Delivery

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