The supramolecular organization of ovomucin—Biophysical and morphological studies
Open accessAbstract
Ovomucin participates in the ovomucin-gel-forming properties because of its shape and its ability to interact in a specific spatial organization. Purified from chicken egg-white by exclusion chromatography with Sephacryl S-300 and Sepharose CL-2B and analysed by light-scattering, it exhibited an Mr of about 40 x 10(6). This large Mr can be explained by the aggregation of polymers that can be degraded into 3 x 10(6)-Mr fragments by reduction with dithiothreitol. The values for hydrodynamic parameters such as Mr, radius of gyration, hydrodynamic radius, mass per unit length and combinations of them suggested that ovomucin is a linear and highly flexible molecule conferring upon it a random-coil-like structure in 0.2 M-NaCl solution. Analysis of the ovomucin molecules by electron microscopy revealed its linear character but also indicated a lower Mr than that obtained in the light-scattering experiments. By temperature-induced non-specific aggregation of an ovomucin solution containing other globular egg proteins, an attempt was made to find out what conditions are required for gel formation and to examine the quality of aggregation that is obtained under these conditions. Results show that the viscosity of the solution did not increase after heat treatment. Apparently, in the ovomucin gel, specific spatial organization of the ovomucin molecules is required for hydrogel formation.
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Homogenization and sonication improved the solubility of ovomucin to a certain degree by either cleaving the disulfide bonds or releasing the attached carbohydrate from the main protein chain.
“Homogenization and sonication improved the solubility of ovomucin (Rabouille et al., 1990) to a certain degree by either cleaving the disulfide bonds or releasing the attached carbohydrate from the main protein chain (Omana et al., 2010).”
From Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents—A review (2013) · cites this paper as Rabouille et al., 1990
Rabouille et al. (1990) used a 10× dilution method to separate ovomucin, but a 10-fold increase in volume causes an important practical issue for scaled-up production.
“Rabouille et al. (1990) used a 10× dilution method to separate ovomucin, but a 10-fold increase in volume causes an important practical issue for scaled-up production.”
From Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents—A review (2013) · cites this paper as Rabouille et al., 1990
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- Authors
- Rabouille, C., Aon, M. A., Muller, G., Cartaud, J., & Thomas, D.
- Affiliations
- Université de Technologie de Compiègne (FR)
- Laboratoire des Polyméres, Biopolyméres et Membranes, U.A. 500 du C.N.R.S., Faculté de Sciences de Rouen, B.P. 116, 76130 Mont St. Aignan, France
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Rabouille, C
- Thomas, D
- ORCID
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1990-03-15
- Volume
- 266
- Issue
- 3
- Pages
- 697-706
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1131196
- OpenAlex
- W60932085
- Cited by
- 22
- References
- 36
- Citations by year
- 2023: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2016: 1 · 2015: 3 · 2014: 3 · 2013: 1 · 2012: 1
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Keywords
- ovomucin, supramolecular organization, egg white proteins, gelation, hydrogels, molecular weight, radius of gyration, hydrodynamic radius, random coil, protein aggregation, heat-induced aggregation, viscosity, chicken egg white
- MeSH terms
- Animals, Chickens, Egg Proteins, Electrophoresis, Agar Gel, Molecular Weight, Ovomucin, Viscosity
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