Susceptibility of equine κ- and β-caseins to hydrolysis by chymosin

Equine whole casein was hydrolysed by chymosin and some peptides generated were characterised by microsequencing after reversed-phase high performance liquid chromatography or sodium dodecyl sulphate polyacrylamide gel electrophoresis. β-Casein was readily hydrolysed into amino- and carboxy-terminal...

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Bibliographic Details
Published in:International dairy journal 2001, Vol.11 (11), p.885-893
Main Authors: Egito, A.S., Girardet, J.-M., Miclo, L., Mollé, D., Humbert, G., Gaillard, J.-L.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Chymosin
Equine casein
Equine milk
Fundamental and applied biological sciences. Psychology
Glycomacropeptide
Miscellaneous
Proteins
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Summary:Equine whole casein was hydrolysed by chymosin and some peptides generated were characterised by microsequencing after reversed-phase high performance liquid chromatography or sodium dodecyl sulphate polyacrylamide gel electrophoresis. β-Casein was readily hydrolysed into amino- and carboxy-terminal fragments after cleavage of the Leu 190–Tyr 191 bond. These two fragments seemed to be resistant to further chymosin hydrolysis on incubation for up to 24 h. Equine κ-casein was purified by affinity chromatography on immobilised wheat germ agglutinin. O-Glycosylated κ-casein was found to represent less than 6.8% of the equine casein components. Equine κ-casein was also hydrolysed and para- κ-casein and glycomacropeptide were generated after cleavage of the Phe 97–Ile 98 bond.
ISSN:0958-6946
1879-0143
DOI:10.1016/S0958-6946(01)00123-6