Use of the yeast Pichia pastoris as an expression host for secretion of enterocin L50, a leaderless two-peptide (L50A and L50B) bacteriocin from Enterococcus faecium L50.

@article{Basanta2010UseOT,
  title={Use of the yeast Pichia pastoris as an expression host for secretion of enterocin L50, a leaderless two-peptide (L50A and L50B) bacteriocin from Enterococcus faecium L50.},
  author={Antonio Basanta and Beatriz G{\'o}mez-Sala and Jorge S{\'a}nchez and Dzung Bao Diep and Carmen Rosa Herranz and Pablo V. Hernandez and Luis Mar{\'i}a Cintas},
  journal={Applied and environmental microbiology},
  year={2010},
  volume={76 10},
  pages={3314-24}
}
In this work, we report the expression and secretion of the leaderless two-peptide (EntL50A and EntL50B) bacteriocin enterocin L50 from Enterococcus faecium L50 by the methylotrophic yeast Pichia pastoris X-33. The bacteriocin structural genes entL50A and entL50B were fused to the Saccharomyces cerevisiae gene region encoding the mating pheromone alpha-factor 1 secretion signal (MFalpha1(s)) and cloned, separately and together (entL50AB), into the P. pastoris expression and secretion vector… CONTINUE READING
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