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Opioid peptides encrypted in intact milk protein sequences
1Bundesanstalt für Milchforschung, Institut für Chemie und Physik, Kiel, Germany. meisel@bafm.de
The British Journal of Nutrition
|March 10, 2001
Summary
Enzymatic digestion can activate opioid peptides from milk proteins, influencing bodily regulatory processes. These peptides interact with intestinal receptors or are absorbed to reach systemic opioid receptors.
Area of Science:
- Biochemistry
- Food Science
- Pharmacology
Background:
- Milk proteins contain precursor sequences for opioid peptides.
- These peptides are typically inactive within the intact protein structure.
Purpose of the Study:
- To investigate the release and activation of opioid peptides from milk proteins.
- To understand the potential physiological roles of these activated peptides.
Main Methods:
- Enzymatic proteolysis simulating gastrointestinal digestion.
- Analysis of peptide release and activation during food processing.
Main Results:
- Opioid agonistic and antagonistic peptides can be released and activated by enzymatic proteolysis.
- Activated opioid peptides have the potential to modulate various regulatory processes.
Conclusions:
- Enzymatic digestion activates opioid peptides from milk proteins.
- These peptides can interact with intestinal opioid receptors or be absorbed to affect endogenous opioid receptors.