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Journal of Dairy Science Vol. 81 No. 2 327-337
© 1998 by American Dairy Science Association ®
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Peptide Accumulation and Bitterness in Cheddar Cheese Made Using Single-Strain Lactococcus lactis Starters with Distinct Proteinase Specificities

Jeffery R. Broadbent 1, Marie Strickland 1, Bart C. Weimer 1, Mark E. Johnson 2, and James L. Steele 2

1 Western Center for Dairy Research and Department of Nutrition and Food Sciences, Utah State University, Logan 84322-8700
2 University of Wisconsin, Madison 53706

This study investigated peptide accumulation and bitterness in reduced- and full-fat Cheddar cheeses that were manufactured with single-strain Lactococcus lactis starters that had distinct cell envelope proteinase specificities. Micellar electrokinetic capillary electrophoresis of aqueous cheese extracts detected three large peaks, designated O, P, and Q, that eluted with peptide standards and increased in area during cheese maturation in a pattern that was distinct for each starter. Regression analysis of bitter flavor scores from trained sensory panels and individual OQ peak areas suggested that peaks P and Q had a negative and positive correlation, respectively, to this defect. Then, HPLC, capillary electrophoresis, peptide sequencing, and mass spectrometry were used to identify five peptides from alphaS1-casein (CN), one from ß-CN, and one from alphaS2-CN that accumulated in 6-mo-old cheeses. Most of the peptides derived from alphaS1-CN (f 1–23) accumulated in a manner that corresponded with starter proteinase specificity. All of the peptides identified in the study except alphaS2-CN (f 1–21) eluted in the O-P-Q region of micellar electrokinetic capillary electropherograms. The alphaS1-CN (f 1–16), alphaS1-CN (f 1–17) and ß-CN (f 193-209) eluted in peak O, alphaS1-CN (f 1–13) and alphaS1-CN (f 1–14) eluted in peak P, and alphaS1-CN (f 1–9) eluted in peak Q.

Key Words: Lactococcus lactis • proteinase • cheese proteolysis • bitterness

Submitted on February 18, 1997
Accepted on September 15, 1997




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