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Water-soluble peptides in Cheddar cheese: isolation and identification of peptides in the diafiltration retentate of the water-soluble fraction

Published online by Cambridge University Press:  01 June 2009

Tanoj K. Singh ,
Patrick F. Fox  and
Áine Healy
Tanoj K. Singh*
Affiliation:
Department of Food Chemistry, University College, Cork, Irish Republic National Food Biotechnology Centre, University College, Cork, Irish Republic
Patrick F. Fox
Affiliation:
Department of Food Chemistry, University College, Cork, Irish Republic National Food Biotechnology Centre, University College, Cork, Irish Republic
Áine Healy
Affiliation:
National Food Biotechnology Centre, University College, Cork, Irish Republic
*
‡For correspondence.
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Summary

The water-soluble extract of Cheddar cheese was fractionated by diafiltration using 10 kDa cut-off membranes. Peptides were isolated from the diafiltrate retentate by chromatography on DEAE-cellulose with a linear NaCl gradient in 50 mM-Tris-HCl, pH 8·6, and reversed-phase HPLC or electroblotting from urea-PAGE gels. Peptides were identified by determining N-terminal amino acid sequences and mass spectrometry. Most (45) of the total 51 peptides identified in the diafiltrate retentate originated from β-casein, especially from a short region in the N-terminal half of the molecule. Only six peptides originated from αs1-casein; β-lactoglobulin was also identified in the retentate. The origin of most of these peptides could be explained on the basis of known specificities of lactococcal cell envelope proteinases.

Type
Original Articles
Information
Journal of Dairy Research , Volume 62 , Issue 4 , November 1995 , pp. 629 - 640
Copyright
Copyright © Proprietors of Journal of Dairy Research 1995

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