Special Issue "Eggs and Their Derivatives: Physicochemical, Nutritional and Technological Properties"

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Quality and Safety".

Deadline for manuscript submissions: 23 January 2024 | Viewed by 1289

Special Issue Editor

College of Food Science and Technology, Huazhong Agricultural University, Wuhan, China
Interests: egg processing technology; traditional and novel egg products; egg by-products; large-scale extraction of egg functional components; egg nutrition and function; control of egg quality

Special Issue Information

Dear Colleagues,

Eggs with abundant proteins, unsaturated fatty acids, vitamins, minerals, etc., have become an important food in our daily diet. Based on the consumer demand and different applications, eggs have been processed into a variety of egg products, including traditional egg products (e.g., salted egg, preserved egg), appropriative egg products (e.g., egg white and yolk powder, liquid egg), leisure egg products (e.g., dried egg, marinated egg, vinegar egg, egg sausage), and egg-derived functional components (ovalbumin, ovotransferrin, lysozyme, IgY, phosvitin, lecithin). The processing methods, physiochemical and nutritional properties of egg products need to be investigated to improve the quality of products and promote their consumption. Some novel processing techniques and strategies are expectantly introduced to increase the processing efficiency of egg products. Egg by-products (e.g., egg shell, shell membrane) are encouraged to be processed into high-value-added products (e.g., shell-derived organic calcium, shell membrane derived hydrolysates). The relevant research work will promote the rapid and efficient development of the egg processing industry.

Prof. Dr. Yongguo Jin
Guest Editor

Manuscript Submission Information

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  • fried egg
  • boiled egg
  • salted egg
  • marinated egg
  • preserved egg
  • soft-boiled egg
  • hot spring egg
  • edible raw egg
  • fermented egg
  • vinegar egg
  • egg sausage
  • dried egg
  • egg powder
  • liquid egg
  • egg white
  • egg yolk
  • egg shell
  • shell membrane
  • processing
  • preservation
  • nutrition

Published Papers (1 paper)

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Providing New Insights on the Molecular Properties and Thermal Stability of Ovotransferrin and Lactoferrin
Foods 2023, 12(3), 532; https://doi.org/10.3390/foods12030532 - 25 Jan 2023
Cited by 1 | Viewed by 1053
Ovotransferrin (OVT) is a multi-functional protein showing over 50% homology with Bovine lactoferrin (BLF) and human lactoferrin (HLF), which have the potential to be a substitute for lactoferrin (LF) due to the limited production of LF. To explore the substitutability of OVT, the [...] Read more.
Ovotransferrin (OVT) is a multi-functional protein showing over 50% homology with Bovine lactoferrin (BLF) and human lactoferrin (HLF), which have the potential to be a substitute for lactoferrin (LF) due to the limited production of LF. To explore the substitutability of OVT, the molecular properties and thermal stability of OVT, BLF and HLF were characterized because these properties will affect the processing quality and biological activities of protein products when exposed to different processing conditions (e.g., temperature, pH, ion strength). The results showed that although obviously different isoelectric point (5.31, 9.12 and 8.75 for OVT, BLF and HLF, respectively), particle size distribution and hydrophobicity were found, they exhibited good dispersity because of high potential value. They showed an endothermic peak at 80.64 °C, 65.71 °C and 90.01 °C, respectively, and the denaturation temperature varied at different pH and ionic strength. OVT and BLF were more susceptible to heating at pH 5.0 as reflected by the decline of denaturation temperature (21.78 °C shift for OVT and 5.81 °C shift for BLF), while HLF could remain stable. Compared with BLF, OVT showed higher secondary structure stability at pH 7.0 and 9.0 with heating. For example, the α-helix content of OVT changed from 20.35% to 15.4% at pH 7.0 after heating, while that of BLF changed from 20.05% to 6.65%. The increase on fluorescence intensity and redshifts on the maximum wavelength after heating indicated the changes of tertiary structure of them. The turbidity measurements showed that the thermal aggregation degree of OVT was lower than BLF and HLF at pH 7.0 (30.98%, 59.53% and 35.66%, respectively) and pH 9.0 (4.83%, 12.80% and 39.87%, respectively). This work demonstrated the similar molecular properties and comparable thermal stability of OVT to BLF and HLF, which can offer a useful reference for the substitute of LF by OVT. Full article
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