ArticleApplied and environmental microbiology2002
Contribution of Lactococcus lactis cell envelope proteinase specificity to peptide accumulation and bitterness in reduced-fat Cheddar cheese.
Article in Applied and environmental microbiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 87 citations in OpenAlex.
- The lactococcal ICE-ome encodes a repertoire of exchangeable traits with potential industrial relevance.BMC genomics · 2024Article
- Effects of Protein, Calcium, and pH on Gene Transcription, Cell-Envelope Peptidase Activity ofFoods (Basel, Switzerland) · 2021Article
- Bacteriostatic Potential of Melatonin: Therapeutic Standing and Mechanistic Insights.Frontiers in immunology · 2021Review
- TheFrontiers in microbiology · 2019Article
- Dipeptidase activity and growth of heat-treated commercial dairy starter culture.Applied biochemistry and biotechnology · 2015Article
- Two thimet oligopeptidase-like Pz peptidases produced by a collagen-degrading thermophile, Geobacillus collagenovorans MO-1.Journal of bacteriology · 2005Article
- Identification of endopeptidase genes from the genomic sequence of Lactobacillus helveticus CNRZ32 and the role of these genes in hydrolysis of model bitter peptides.Applied and environmental microbiology · 2005Article
- Identification and characterization of Lactobacillus helveticus PepO2, an endopeptidase with post-proline specificity.Applied and environmental microbiology · 2003Article
- 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.Applied and environmental microbiology · 2003Article
- Next-generation sequencing as an approach to dairy starter selection.Dairy science & technologyReview
- Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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