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Chemical characterization of bioactive peptides from in vivo digests of casein

Published online by Cambridge University Press:  01 June 2009

Hans Meisel  and
Herman Frister
Hans Meisel
Affiliation:
Institut für Chemie und Physik, Bundesandstalt für Milchforschung, 2300 Kiel, F.R.G.
Herman Frister
Affiliation:
Institut für Chemie und Physik, Bundesandstalt für Milchforschung, 2300 Kiel, F.R.G.
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Summary

The in vivo formation of biologically active caseinopeptides was studied. It was proved that bioactive peptides were released in the small intestine of minipigs in the course of luminal digestion of diets containing bovine casein. An opioid peptide and a phosphopeptide were isolated from jejunal chyme and were chemically characterized. The opioid peptide has been identified as a fragment of β-casein (60–70). This peptide, named β-casomorphin-ll, displayed substantial opioid activity in an opiate receptor-binding assay. The caseinophosphopeptide has been shown to be a fragment of αs1-casein (66–74). Casein-derived phosphopeptides exhibit a potent ability to form soluble complexes with Ca and trace elements. Evidence exists that casomorphins and caseinophosphopeptides participate in the regulation of nutrient entry.

Type
Original Articles
Information
Journal of Dairy Research , Volume 56 , Issue 3: Special Issue: Proceedings of the Hannah Research Institute Casein Conference , May 1989 , pp. 343 - 349
Copyright
Copyright © Proprietors of Journal of Dairy Research 1989

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References

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