Tryptic hydrolysis of bovine αS2-casein: identification and release kinetics of peptides

Bovine α S2-casein was purified by anionic exchange and hydrophobic interaction chromatographies. The purified α S2-casein was hydrolysed with trypsin; the resulting peptides were identified by amino acids composition and on line reversed-phase high performance liquid chromatography coupled with ele...

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Bibliographic Details
Published in:International dairy journal 2003, Vol.13 (1), p.15-27
Main Authors: Tauzin, J., Miclo, L., Roth, S., Mollé, D., Gaillard, J.-L.
Format: Article
Language:English
Subjects:
alphaS2-casein
amino acid composition
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Biological and medical sciences
Bovine αS2-casein
cattle
Food industries
Fundamental and applied biological sciences. Psychology
hydrolysis
hydrophobic bonding
Mass spectrometry
Milk and cheese industries. Ice creams
Peptide kinetics
peptides
reversed-phase high performance liquid chromatography
Trypsin
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Summary:Bovine α S2-casein was purified by anionic exchange and hydrophobic interaction chromatographies. The purified α S2-casein was hydrolysed with trypsin; the resulting peptides were identified by amino acids composition and on line reversed-phase high performance liquid chromatography coupled with electrospray mass spectrometry. A study on the kinetics of peptide release enabled discrimination between different protein areas according to their surface-accessibility. Data from the kinetic study were reconciled with secondary structure predictions and a hypothetical model of the structural organisation of purified bovine α S2-casein in solution was proposed.
ISSN:0958-6946
1879-0143
DOI:10.1016/S0958-6946(02)00127-9