TY  - JOUR
  - Ahern, M,Verschueren, S,van Sinderen, D
  - 2003
  - March
  - Fems Microbiology Letters
  - Isolation and characterisation of a novel bacteriocin produced by Bacillus thuringiensis strain B439
  - Validated
  - ()
  - bacteriocin Bacillus thuringiensis thuricin 439 antimicrobial peptide GRAM-POSITIVE BACTERIA LACTIC-ACID BACTERIA CEREUS LANTIBIOTICS CEREIN-7
  - 220
  - 127
  - 131
  - Bacillus thuringiensis strain B439 produces a bacteriocin-like inhibitory substance in its growth medium. This antimicrobial peptide. referred to as thuricin 439, acts as a bacteriocidal peptide and exhibits an apparent narrow range of inhibitory activity, essentially only affecting growth of Bacillus cereus and B. thuringiensis strains. It remains active over a relatively wide pH and temperature range. showing no loss of activity following heat treatments up to 80degreesC. Purification of thuricin 439 was achieved using several chromatographic steps, which resulted in the identification of two peptides with inhibitory activity. These two peptides were shown to possess identical N-terminal sequences, but different molecular masses. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
  - DOI 10.1016/S0378-1097(03)00086-7
DA  - 2003/03
ER  - 

@article{V43337976,
   = {Ahern,  M and Verschueren,  S and van Sinderen,  D },
   = {2003},
   = {March},
   = {Fems Microbiology Letters},
   = {Isolation and characterisation of a novel bacteriocin produced by Bacillus thuringiensis strain B439},
   = {Validated},
   = {()},
   = {bacteriocin Bacillus thuringiensis thuricin 439 antimicrobial peptide GRAM-POSITIVE BACTERIA LACTIC-ACID BACTERIA CEREUS LANTIBIOTICS CEREIN-7},
   = {220},
  pages = {127--131},
   = {{Bacillus thuringiensis strain B439 produces a bacteriocin-like inhibitory substance in its growth medium. This antimicrobial peptide. referred to as thuricin 439, acts as a bacteriocidal peptide and exhibits an apparent narrow range of inhibitory activity, essentially only affecting growth of Bacillus cereus and B. thuringiensis strains. It remains active over a relatively wide pH and temperature range. showing no loss of activity following heat treatments up to 80degreesC. Purification of thuricin 439 was achieved using several chromatographic steps, which resulted in the identification of two peptides with inhibitory activity. These two peptides were shown to possess identical N-terminal sequences, but different molecular masses. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.}},
   = {DOI 10.1016/S0378-1097(03)00086-7},
  source = {IRIS}
}