Nomenclature Abstract for Lactobacillus sake carnosus (sic) Torriani et al. 1996.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Sarah Wigley ◽  
George M Garrity
Keyword(s):  
Lactobacillus Sake

Sakacin M, a bacteriocin-like substance from Lactobacillus sake 148

1992 ◽  
Vol 16 (3) ◽  
pp. 215-225 ◽  
Author(s):  
Odón J. Sobrino ◽  
Juan M. Rodríguez ◽  
Wagner L. Moreira ◽  
Luis M. Cintas ◽  
María F. Fernández ◽  
...  
Keyword(s):  
Lactobacillus Sake

scholarly journals Production of a Novel Extracellular Polysaccharide by Lactobacillus sake 0-1 and Characterization of the Polysaccharide.

1995 ◽  
Vol 61 (8) ◽  
pp. 2840-2844 ◽  
Author(s):  
D van den Berg ◽  
G W Robijn ◽  
A C Janssen ◽  
M Giuseppin ◽  
R Vreeker ◽  
...  
Keyword(s):  
Extracellular Polysaccharide ◽  
Lactobacillus Sake

scholarly journals Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706

1992 ◽  
Vol 138 (12) ◽  
pp. 2715-2720 ◽  
Author(s):  
A. Holck ◽  
L. Axelsson ◽  
S.-E. Birkeland ◽  
T. Aukrust ◽  
H. Blom
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Lactobacillus Sake ◽  
Sakacin A

Viability Loss of Foodborne Pathogens by Starter Culture Metabolites

1991 ◽  
Vol 54 (11) ◽  
pp. 873-878 ◽  
Author(s):  
ALI M. MOTLAGH ◽  
MONTY C. JOHNSON ◽  
BIBEK RAY
Keyword(s):  
Foodborne Pathogens ◽  
Starter Culture ◽  
Bactericidal Effect ◽  
Bacteriostatic Effect ◽  
Gram Negative ◽  
Gram Positive Bacteria ◽  
Lactobacillus Sake ◽  
Pathogenic Escherichia Coli ◽  
Storage Studies ◽  
Sakacin A

Antibacterial metabolites produced by starter culture bacteria were tested for inhibitory properties against foodborne pathogens capable of growing in foods at refrigeration temperature. Three culture preparations containing the bacteriocins pediocin AcH, nisin, and sakacin A produced by Pediococcus acidilactici H, Lactococcus lactis ssp. lactis DL 16, and Lactobacillus sake 706, respectively, were studied in addition to four commercial preparations: Nisaplin (similar to nisin), Na-lactate, diacetyl and Microgard. All bacteriocin preparations were bactericidal to the Listeria strains tested including nine strains of L. monocytogenes, but not to any of the gram-negative pathogens studied. Some strains of Listeria were lysed by pediocin AcH. Storage studies at 4°C indicated that the bacteriocin preparations did not have bacteriostatic properties against the surviving cells. Diacetyl produced some bactericidal effect against strains of Yersinia enterocolitica, Aeromonas hydrophila, pathogenic Escherichia coli, and Salmonella anatum, but not against Listeria. Lactate had limited bacteriostatic effect against gram-negative pathogens and none against the gram-positive bacteria. Microgard had neither bactericidal nor bacteriostatic action against the bacteria used in this study.

scholarly journals Biochemical and Genetic Characterization of Propionicin T1, a New Bacteriocin from Propionibacterium thoenii

2000 ◽  
Vol 66 (10) ◽  
pp. 4230-4236 ◽  
Author(s):  
Therese Faye ◽  
Thor Langsrud ◽  
Ingolf F. Nes ◽  
Helge Holo
Keyword(s):  
Amino Acids ◽  
Stop Codon ◽  
Sequence Similarity ◽  
Propionibacterium Freudenreichii ◽  
Terminal Part ◽  
Reading Frame ◽  
Lactobacillus Sake ◽  
Propionibacterium Thoenii ◽  
Self Protection

ABSTRACT A collection of propionibacteria was screened for bacteriocin production. A new bacteriocin named propionicin T1 was isolated from two strains of Propionibacterium thoenii. This bacteriocin shows no sequence similarity to other bacteriocins. Propionicin T1 was active against all strains of Propionibacterium acidipropionici, Propionibacterium thoenii, andPropionibacterium jensenii tested and also againstLactobacillus sake NCDO 2714 but showed no activity againstPropionibacterium freudenreichii. The bacteriocin was purified, and the N-terminal part of the peptide was determined with amino acid sequencing. The corresponding gene pctA was sequenced, and this revealed that propionicin T1 is produced as a prebacteriocin of 96 amino acids with a typical sec leader, which is processed to give a mature bacteriocin of 65 amino acids. An open reading frame encoding a protein of 424 amino acids was found 68 nucleotides downstream the stop codon of pctA. The N-terminal part of this putative protein shows strong similarity with the ATP-binding cassette of prokaryotic and eukaryotic ABC transporters, and this protein may be involved in self-protection against propionicin T1. Propionicin T1 is the first bacteriocin from propionibacteria that has been isolated and further characterized at the molecular level.

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