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Published on: January 27, 2021
A new method of separating ovomucin from egg white
1Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta, Canada T6G 2P5.
Journal of Agricultural and Food Chemistry
|April 8, 2009
Summary
A new two-step method effectively purifies ovomucin, a key egg white glycoprotein. This process optimizes salt concentrations to remove contaminants like ovalbumin and lysozyme, achieving over 90% purity for potential scale-up.
Area of Science:
- Food Science
- Biochemistry
- Protein Chemistry
Background:
- Ovomucin is crucial for egg white viscosity but difficult to purify.
- Contaminants like ovalbumin and lysozyme hinder pure ovomucin preparation.
Purpose of the Study:
- To investigate salt concentration effects on ovomucin extractability.
- To develop a simple, scalable method for high-purity ovomucin production.
Main Methods:
- Assessing ovomucin extract composition across various salt concentrations (NaCl).
- Developing a two-step purification protocol involving sequential salt treatments.
- Utilizing pH 6.0 and specific NaCl concentrations (100 mM, then 500 mM).
Main Results:
- Salt concentration significantly impacts contaminant profiles: lysozyme dominates at low (<100 mM) and ovalbumin at high (≥200 mM) concentrations.
- The developed two-step method achieved >90% ovomucin purity.
- Yield was 400.2 mg/100 g egg white.
Conclusions:
- Salt concentration is a critical factor in ovomucin purification strategy.
- The novel two-step method offers a simple, eco-friendly, and scalable approach for producing purified ovomucin.
- This method effectively removes major contaminants, paving the way for industrial applications.
