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An In Ovo Model for Testing Insulin-mimetic Compounds
Published on: April 23, 2018
Egg white ovalbumin digestion mimicking physiological conditions
Gustavo Martos1, Patricia Contreras, Elena Molina
1Instituto de Fermentaciones Industriales, CSIC C/ Juan de la Cierva 3, Madrid, Spain.
Journal of Agricultural and Food Chemistry
|March 30, 2010
Summary
Ovalbumin (OVA) digestion in simulated gastric and duodenal conditions shows resistance to pepsin but increased degradation with bile salts and phosphatidylcholine. Allergenicity decreased after duodenal digestion.
Area of Science:
- Food Science
- Biochemistry
- Allergenicity Research
Background:
- Ovalbumin (OVA) is a major allergen in egg white.
- Understanding its gastrointestinal digestion is crucial for managing food allergies.
Purpose of the Study:
- To investigate the in vitro digestion of ovalbumin (OVA) under simulated gastric and duodenal conditions.
- To assess the impact of pH, protease concentration, and surfactants (phosphatidylcholine and bile salts) on OVA digestion and allergenicity.
Main Methods:
- Simulated in vitro digestion in two steps (gastric and duodenal).
- Analysis of OVA proteolysis using varying pH, protease concentrations, phosphatidylcholine (PC), and bile salts (BS).
- Assessment of retained immunoreactivity using IgE from allergic patients' sera.
Main Results:
- OVA demonstrated high resistance to pepsin in simulated gastric conditions.
- Bile salts and phosphatidylcholine significantly enhanced OVA proteolysis by pancreatic enzymes in simulated duodenal conditions.
- In vitro gastric digestion retained OVA immunoreactivity, while duodenal digestion considerably decreased it.
Conclusions:
- OVA's resistance to gastric digestion is overcome by duodenal surfactants, increasing its susceptibility to proteolysis.
- Digestion significantly reduces OVA's allergenic potential, particularly under duodenal conditions.
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