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Ion-exchange fast protein liquid chromatography: optimization of the purification of caseins using a non-denaturing detergent

Published online by Cambridge University Press:  01 June 2009

Maryse St-Martin  and
Paul Paquin
Maryse St-Martin
Affiliation:
Groupe de Recherche STELA, Département de Sciences et Technologie des Aliments, Facilité des Sciences de l'Agriculture et de l'Alimentation Université Laval, Ste-Foy, Québec, G1K 7P4, Canada
Paul Paquin
Affiliation:
Groupe de Recherche STELA, Département de Sciences et Technologie des Aliments, Facilité des Sciences de l'Agriculture et de l'Alimentation Université Laval, Ste-Foy, Québec, G1K 7P4, Canada
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Summary

The separation of bovine milk proteins by fast protein liquid chromatography has been studied by ion-exchange chromatography on Mono S and Mono Q columns. The use of a non-ionic detergent, octyl-glucoside, made possible the separation of the four major casein components (αs1, αs2, β and κ) as well as minor caseins on the Mono S column using urea-containing buffers at pH 3·5. There was, however, considerable overlap between the αs1 and αs2-casein peaks. A good resolution was obtained with a low concentration of urea (3·5 M) and detergent (0·1%). These conditions allowed the separation of casein components in their native state in less than 50 min. The purity of isolated κ-casein was further improved by a second separation on a Mono Q column.

Type
Original Articles
Information
Journal of Dairy Research , Volume 57 , Issue 1 , February 1990 , pp. 63 - 68
Copyright
Copyright © Proprietors of Journal of Dairy Research 1990

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References

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