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Journal of Dairy Science Vol. 81 No. 12 3109-3116
© 1998 by American Dairy Science Association ®
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Isolation and Identification of Some Major Water-soluble Peptides in Feta Cheese

Alexandra Michaelidou 1, Efstathios Alichanidis 1, Hennig Urlaub 2, Anna Polychroniadou 3, and Gregory K. Zerfiridis 1

1 Laboratory of Dairy Technology, D-14195 Berlin (Dahlem), Germany
2 Max-Plank-Institut für Molekulare Genetic, D-14195 Berlin (Dahlem), Germany
3 Laboratory of Food Chemistry and Biochemistry, Aristotle University of Thessaloniki, GR-54006 Thessaloniki, Greece

Peptides were isolated from the water-soluble fraction of Feta cheese by reversed-phase HPLC in three successive steps. Peptide sequencing was performed by automatic Edman degradation. Most of the peptides originated from a alphas1-casein (CN), especially from the N-terminal half of the molecule. Two peptides originated from the C-terminal domain of ß-CN. Only one peptide, which was rich in histidine, originated from kappa-CN. ß-Lactoglobulin and alpha-lactalbumin were also identified in the water extract of Feta cheese. The origin of most of these peptides could be explained on the basis of known specificities of chymosin and lactococcal cell-wall proteinases.

Key Words: water-soluble peptides • Feta cheese

Submitted on January 28, 1998
Accepted on June 8, 1998




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