This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Broadbent, J. R.
Right arrow Articles by Steele, J. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Broadbent, J. R.
Right arrow Articles by Steele, J. L.
Agricola
Right arrow Articles by Broadbent, J. R.
Right arrow Articles by Steele, J. L.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, April 2002, p. 1778-1785, Vol. 68, No. 4
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.4.1778-1785.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Contribution of Lactococcus lactis Cell Envelope Proteinase Specificity to Peptide Accumulation and Bitterness in Reduced-Fat Cheddar Cheese{dagger}

Jeffery R. Broadbent,1* Mary Barnes,1,{ddagger} Charlotte Brennand,1 Marie Strickland,1 Kristen Houck,2 Mark E. Johnson,2 and James L. Steele3

Western Dairy Center and Department of Nutrition and Food Sciences, Utah State University, Logan, Utah 84322-8700,1 Wisconsin Center for Dairy Research,2 Department of Food Science, University of Wisconsin, Madison, Wisconsin 537063

Received 25 July 2001/ Accepted 21 January 2002

Bitterness is a flavor defect in Cheddar cheese that limits consumer acceptance, and specificity of the Lactococcus lactis extracellular proteinase (lactocepin) is widely believed to be a key factor in the development of bitter cheese. To better define the contribution of this enzyme to bitterness, we investigated peptide accumulation and bitterness in 50% reduced-fat Cheddar cheese manufactured with single isogenic strains of Lactococcus lactis as the only starter. Four isogens were developed for the study; one was lactocepin negative, and the others produced a lactocepin with group a, e, or h specificity. Analysis of cheese aqueous extracts by reversed-phase high-pressure liquid chromatography confirmed that accumulation of {alpha}S1-casein (f 1-23)-derived peptides f 1-9, f 1-13, f 1-16, and f 1-17 in cheese was directly influenced by lactocepin specificity. Trained sensory panelists demonstrated that Cheddar cheese made with isogenic starters that produced group a, e, or h lactocepin was significantly more bitter than cheese made with a proteinase-negative isogen and that propensity for bitterness was highest in cells that produced group h lactocepin. These results confirm the role of starter proteinase in bitterness and suggest that the propensity of some industrial strains for production of the bitter flavor defect in cheese could be altered by proteinase gene exchange or gene replacement.


* Corresponding author. Mailing address: Western Dairy Center and Department of Nutrition and Food Sciences, Utah State University, Logan, UT 84322-8700. Phone: (435) 797-2113. Fax: (435) 797-2379. E-mail: broadbnt{at}cc.usu.edu.

{dagger} Approved as Journal Paper no. 7405 by the Utah Agricultural Experiment Station.

{ddagger} Present address: Department of Biology, Southwest Texas State University, San Marcos, TX 78666.


Applied and Environmental Microbiology, April 2002, p. 1778-1785, Vol. 68, No. 4
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.4.1778-1785.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Awad, S., Hassan, A. N., Halaweish, F. (2005). Application of Exopolysaccharide-Producing Cultures in Reduced-Fat Cheddar Cheese: Composition and Proteolysis. J DAIRY SCI 88: 4195-4203 [Abstract] [Full Text]  
  • Miyake, R., Shigeri, Y., Tatsu, Y., Yumoto, N., Umekawa, M., Tsujimoto, Y., Matsui, H., Watanabe, K. (2005). Two Thimet Oligopeptidase-Like Pz Peptidases Produced by a Collagen- Degrading Thermophile, Geobacillus collagenovorans MO-1. J. Bacteriol. 187: 4140-4148 [Abstract] [Full Text]  
  • Sridhar, V. R., Hughes, J. E., Welker, D. L., Broadbent, J. R., Steele, J. L. (2005). Identification of Endopeptidase Genes from the Genomic Sequence of Lactobacillus helveticus CNRZ32 and the Role of These Genes in Hydrolysis of Model Bitter Peptides. Appl. Environ. Microbiol. 71: 3025-3032 [Abstract] [Full Text]  
  • Fallico, V., McSweeney, P. L. H., Horne, J., Pediliggieri, C., Hannon, J. A., Carpino, S., Licitra, G. (2005). Evaluation of Bitterness in Ragusano Cheese. J DAIRY SCI 88: 1288-1300 [Abstract] [Full Text]  
  • Drake, M. (2004). ADSA Foundation Scholar Award: Defining Dairy Flavors. J DAIRY SCI 87: 777-784 [Abstract] [Full Text]  
  • Chen, Y.-S., Christensen, J. E., Broadbent, J. R., Steele, J. L. (2003). Identification and Characterization of Lactobacillus helveticus PepO2, an Endopeptidase with Post-Proline Specificity. Appl. Environ. Microbiol. 69: 1276-1282 [Abstract] [Full Text]  
  • Christensen, J. E., Broadbent, J. R., Steele, J. L. (2003). Hydrolysis of Casein-Derived Peptides {alpha}S1-Casein(f1-9) and {beta}-Casein(f193-209) by Lactobacillus helveticus Peptidase Deletion Mutants Indicates the Presence of a Previously Undetected Endopeptidase. Appl. Environ. Microbiol. 69: 1283-1286 [Abstract] [Full Text]