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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
S1-casein (CN), one from ß-CN, and one from
S2-CN that accumulated in 6-mo-old cheeses. Most of the peptides derived from
S1-CN (f 123) accumulated in a manner that corresponded with starter proteinase specificity. All of the peptides identified in the study except
S2-CN (f 121) eluted in the O-P-Q region of micellar electrokinetic capillary electropherograms. The
S1-CN (f 116),
S1-CN (f 117) and ß-CN (f 193-209) eluted in peak O,
S1-CN (f 113) and
S1-CN (f 114) eluted in peak P, and
S1-CN (f 19) 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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