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Stability of hen egg-white lysozyme during embryonic development
Yukiko Muroi1,2, Izumi Aburaya1, Yuki Kiyokawa2
1Faculty of Food and Nutrition, Kyushu Nutrition and Welfare University, Kokura-Kitaku, Kitakyushu, Japan.
Bioscience, Biotechnology, and Biochemistry
|August 10, 2022
Summary
Egg white proteins like lysozyme remain active during embryonic development, despite a decrease in overall egg white mass and activity. Lysozyme undergoes minor structural changes while retaining key functions.
Area of Science:
- Biochemistry
- Molecular Biology
- Developmental Biology
Background:
- Egg white proteins are crucial for embryonic development.
- Ovalbumin stability during embryogenesis was previously noted.
- Understanding lysozyme's fate in fertile eggs is important.
Purpose of the Study:
- To investigate the maintenance and changes in egg-white proteins, specifically lysozyme, during avian embryogenesis.
- To assess the functional and conformational stability of purified lysozyme throughout incubation.
Main Methods:
- Quantification of egg white mass and protein content over incubation days.
- Measurement of total bacteriolytic activity.
- Purification of lysozyme from egg white at different incubation stages.
- Enzymatic assays (Km, Vmax), thermal denaturation, and hydrophobicity measurements of purified lysozyme.
Main Results:
- Egg white mass and gross protein content decreased during incubation.
- Total bacteriolytic activity declined, correlating with protein content.
- Purified lysozyme retained enzymatic and bacteriolytic activity against Micrococcus lysodeikticus and inhibitory effects on Staphylococcus aureus.
- Lysozyme exhibited altered kinetic parameters (Km, Vmax), a slight decrease in denaturation temperature, and increased surface hydrophobicity as embryogenesis progressed.
Conclusions:
- Egg-white lysozyme maintains its essential enzymatic and antibacterial functions throughout avian embryogenesis.
- Despite functional retention, lysozyme undergoes subtle conformational alterations, including changes in enzyme kinetics and stability, during development.
