An application in cheddar cheese manufacture for a strain of Lactococcus lactis producing a novel broad-spectrum bacteriocin, lacticin 3147.

1996 ◽  
Vol 62 (2) ◽  
pp. 612-619 ◽  
Author(s):  
M P Ryan ◽  
M C Rea ◽  
C Hill ◽  
R P Ross
Keyword(s):  
Lactococcus Lactis ◽  
Broad Spectrum ◽  
Cheddar Cheese ◽  
Lacticin 3147

scholarly journals Evaluation of Lacticin 3147 and a Teat Seal Containing This Bacteriocin for Inhibition of Mastitis Pathogens

1998 ◽  
Vol 64 (6) ◽  
pp. 2287-2290 ◽  
Author(s):  
Máire P. Ryan ◽  
William J. Meaney ◽  
R. Paul Ross ◽  
Colin Hill
Keyword(s):  
Antimicrobial Activity ◽  
Lactococcus Lactis ◽  
Broad Spectrum ◽  
Lacticin 3147 ◽  
Mastitis Pathogens ◽  
Teat Seal

ABSTRACT Lacticin 3147 is a broad-spectrum bacteriocin produced byLactococcus lactis subsp. lactis DPC3147 which is bactericidal against a range of mastitis-causing streptococci and staphylococci. In this study, both lacticin 3147 and the lantibiotic nisin were separately incorporated into an intramammary teat seal product. The seal containing lacticin 3147 exhibited excellent antimicrobial activity and might form the basis of an improved treatment for the prevention of mastitis in dry cows.

scholarly journals Impact of Nisin and Nisin-Producing Lactococcus lactis ssp. lactis on Clostridium tyrobutyricum and Bacterial Ecosystem of Cheese Matrices

Foods ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 898
Author(s):  
Hebatoallah Hassan ◽  
Daniel St-Gelais ◽  
Ahmed Gomaa ◽  
Ismail Fliss
Keyword(s):  
Lactococcus Lactis ◽  
Cheddar Cheese ◽  
Economic Loss ◽  
Gas Production ◽  
Clostridium Tyrobutyricum ◽  
Nisin Production ◽  
Genus Clostridium ◽  
Milk Pasteurization ◽  
Cheese Slurry ◽  
Significant Economic Loss

Clostridium tyrobutyricum spores survive milk pasteurization and cause late blowing of cheeses and significant economic loss. The effectiveness of nisin-producing Lactococcus lactis ssp. lactis 32 as a protective strain for control the C. tyrobutyricum growth in Cheddar cheese slurry was compared to that of encapsulated nisin-A. The encapsulated nisin was more effective, with 1.0 log10 reductions of viable spores after one week at 30 °C and 4 °C. Spores were not detected for three weeks at 4 °C in cheese slurry made with 1.3% salt, or during week 2 with 2% salt. Gas production was observed after one week at 30 °C only in the control slurry made with 1.3% salt. In slurry made with the protective strain, the reduction in C. tyrobutyricum count was 0.6 log10 in the second week at 4 °C with both salt concentration. At 4 °C, nisin production started in week 2 and reached 97 µg/g after four weeks. Metabarcoding analysis targeting the sequencing of 16S rRNA revealed that the genus Lactococcus dominated for four weeks at 4 °C. In cheese slurry made with 2% salt, the relative abundance of the genus Clostridium decreased significantly in the presence of nisin or the protective strain. The results indicated that both strategies are able to control the growth of Clostridium development in Cheddar cheese slurries.

scholarly journals Mechanistic Dissection of the Enzyme Complexes Involved in Biosynthesis of Lacticin 3147 and Nisin

2008 ◽  
Vol 74 (21) ◽  
pp. 6591-6597 ◽  
Author(s):  
Anneke Kuipers ◽  
Jenny Meijer-Wierenga ◽  
Rick Rink ◽  
Leon D. Kluskens ◽  
Gert N. Moll
Keyword(s):  
Lactococcus Lactis ◽  
Bifunctional Enzyme ◽  
Bifunctional Enzymes ◽  
Lacticin 3147 ◽  
Two Component ◽  
Modified Peptides ◽  
Enzyme Complexes ◽  
Insight Into ◽  
Design And Production

ABSTRACT The thioether rings in the lantibiotics lacticin 3147 and nisin are posttranslationally introduced by dehydration of serines and threonines, followed by coupling of these dehydrated residues to cysteines. The prepeptides of the two-component lantibiotic lacticin 3147, LtnA1 and LtnA2, are dehydrated and cyclized by two corresponding bifunctional enzymes, LtnM1 and LtnM2, and are subsequently processed and exported via one bifunctional enzyme, LtnT. In the nisin synthetase complex, the enzymes NisB, NisC, NisT, and NisP dehydrate, cyclize, export, and process prenisin, respectively. Here, we demonstrate that the combination of LtnM2 and LtnT can modify, process, and transport peptides entirely different from LtnA2 and that LtnT can process and transport unmodified LtnA2 and unrelated peptides. Furthermore, we demonstrate a higher extent of NisB-mediated dehydration in the absence of thioether rings. Thioether rings apparently inhibited dehydration, which implies alternating actions of NisB and NisC. Furthermore, certain (but not all) NisC-cyclized peptides were exported with higher efficiency as a result of their conformation. Taken together, these data provide further insight into the applicability of Lactococcus lactis strains containing lantibiotic enzymes for the design and production of modified peptides.

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

1998 ◽  
Vol 81 (2) ◽  
pp. 327-337 ◽  
Author(s):  
Jeffery R. Broadbent ◽  
Marie Strickland ◽  
Bart C. Weimer ◽  
Mark E. Johnson ◽  
James L. Steele
Keyword(s):  
Lactococcus Lactis ◽  
Cheddar Cheese ◽  
Single Strain

scholarly journals Overproduction of Wild-Type and Bioengineered Derivatives of the Lantibiotic Lacticin 3147

2006 ◽  
Vol 72 (6) ◽  
pp. 4492-4496 ◽  
Author(s):  
Paul D. Cotter ◽  
Lorraine A. Draper ◽  
Elaine M. Lawton ◽  
Olivia McAuliffe ◽  
Colin Hill ◽  
...  
Keyword(s):  
Broad Spectrum ◽  
Structural Genes ◽  
Wild Type ◽  
Genetic Determinants ◽  
Lacticin 3147 ◽  
Genes Encoding ◽  
High Level ◽  
Derivatives Of

ABSTRACT Lacticin 3147 is a broad-spectrum two-peptide lantibiotic whose genetic determinants are located on two divergent operons on the lactococcal plasmid pMRC01. Here we introduce each of 14 subclones, containing different combinations of lacticin 3147 genes, into MG1363 (pMRC01) and determine that a number of them can facilitate overproduction of the lantibiotic. Based on these studies it is apparent that while the provision of additional copies of genes encoding the biosynthetic/production machinery and the regulator LtnR is a requirement for high-level overproduction, the presence of additional copies of the structural genes (i.e., ltnA1A2) is not.

scholarly journals Enhancement of 2-methylbutanal formation in cheese by using a fluorescently tagged Lacticin 3147 producing Lactococcus lactis strain

2004 ◽  
Vol 93 (3) ◽  
pp. 335-347 ◽  
Author(s):  
Pilar Fernández de Palencia ◽  
Marta de la Plaza ◽  
M.Luz Mohedano ◽  
M.Carmen Martı́nez-Cuesta ◽  
Teresa Requena ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Lacticin 3147 ◽  
Lactis Strain

scholarly journals Contribution of Lactococcus lactis Cell Envelope Proteinase Specificity to Peptide Accumulation and Bitterness in Reduced-Fat Cheddar Cheese

2002 ◽  
Vol 68 (4) ◽  
pp. 1778-1785 ◽  
Author(s):  
Jeffery R. Broadbent ◽  
Mary Barnes ◽  
Charlotte Brennand ◽  
Marie Strickland ◽  
Kristen Houck ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Cell Envelope ◽  
Cheddar Cheese ◽  
Gene Replacement ◽  
Reversed Phase ◽  
Reduced Fat ◽  
Key Factor ◽  
Industrial Strains ◽  
Group A ◽  
Or Gene

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 αS1-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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