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Journal of Dairy Science Vol. 56 No. 1 39-44
© 1973 by American Dairy Science Association ®
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Peptides, Amino Acids and Amines Liberated from ß-Casein by Micrococcal Cell-Free Preparations

V. Moreno1 and F. V. Kosikowski

Department of Food Science, Cornell University, Ithaca, New York 14850

ABSTRACT

Decomposition products derived from the action of cell-free preparations of Micrococcus freudenreichii, Micrococcus caseolyticus, and Micrococcus candidus on {kappa}-casein were studied for their contribution to the mechanism of {kappa}-casein degradation and to flavor development in cheese.

Peptide patterns were similar in each of the three micrococcal cell-free preparations reacting with {kappa}-casein. Variations induced by length of incubation, temperature, and sodium chloride were observed. Peptides from {kappa}-casein degradation by micrococcal cell-free preparations neither stimulated nor inhibited growth of six bacterial species.

Amino acids freed by M. freudenreichii preparations were mosdy lysine, glutamic acid, proline, valine and leucine; similarly, by M. caseolyticus preparations, glutamic acid, proline, leucine and phenylalanine; and by M. candidus preparations, lysine, valine, leucine and phenylalanine. Lysine, methionine, alanine, proline and leucine in the M. freudenreichii mixture; methionine and phenylalanine in the M. caseolyticus reaction mixture; and phenylalanine in the M. candidus mixture were removed preferentially from {kappa}-casein.

The freed amino acids contributed significantly to the complex flavor of the reaction mixtures, imparting sweet, brothy and bitter flavors whereas some peptides produced bitter flavors.

FOOTNOTES

1 Present address: General Foods Corporation, Technical Center, White Plains, New York 10602.






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Copyright © 1973 by the American Dairy Science Association ®.