Peptide Accumulation and Bitterness in Cheddar Cheese Made Using Single-Strain Lactococcus lactis Starters with Distinct Proteinase Specificities

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

Research output: Contribution to journalArticle

72 Scopus citations

Abstract

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 O-Q 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 αS1-casein (CN), one from β-CN, and one from αS2-CN that accumulated in 6-mo-old cheeses. Most of the peptides derived from αS1-CN (f 1-23) accumulated in a manner that corresponded with starter proteinase specificity. All of the peptides identified in the study except αS2-CN (f 1-21) eluted in the O-P-Q region of micellar electro-kinetic capillary electropherograms. The αS1-CN (f 1-16), αS1-CN (f 1-17) and β-CN (f 193-209) eluted in peak O, αS1-CN (f 1-13) and αS1-CN (f 1-14) eluted in peak P, and αS1-CN (f 1-9) eluted in peak Q.

Original languageEnglish (US)
Pages (from-to)327-337
Number of pages11
JournalJournal of Dairy Science
Volume81
Issue number2
StatePublished - Feb 1998
Externally publishedYes

Keywords

  • Bitterness
  • Cheese proteolysis
  • Lactococcus lactis
  • Proteinase

ASJC Scopus subject areas

  • Animal Science and Zoology
  • Food Science
  • veterinary(all)

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