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Expert Commentary

Bioengineering

A bacteriocin perspective

Pages 313-319 | Published online: 24 Aug 2012

Figures & data

Figure 1. Insights revealed from alanine scanning mutagenesis of the lacticin 3147 peptides and subsequent bioactivity based analyses. Residues that are apparently intolerant of change, on the basis of the elimination of bioactivity following alanine conversion, are depicted in red and blue in Ltnα and Ltnβ, respectively. Apparently distinct functional domains in Ltnα (i-iv) and Ltnβ (i and ii) are grouped according to oval shapes of different color.

Figure 1. Insights revealed from alanine scanning mutagenesis of the lacticin 3147 peptides and subsequent bioactivity based analyses. Residues that are apparently intolerant of change, on the basis of the elimination of bioactivity following alanine conversion, are depicted in red and blue in Ltnα and Ltnβ, respectively. Apparently distinct functional domains in Ltnα (i-iv) and Ltnβ (i and ii) are grouped according to oval shapes of different color.

Figure 2. Deferred antagonism agar diffusion assay highlighting the enhanced bioactivity of a Nisin K22T producer, relative to a Nisin A producer, against S. agalactiae ATCC13813 (colony size = 10 mm).

Figure 2. Deferred antagonism agar diffusion assay highlighting the enhanced bioactivity of a Nisin K22T producer, relative to a Nisin A producer, against S. agalactiae ATCC13813 (colony size = 10 mm).

Figure 3. Dr Paul Cotter.

Figure 3. Dr Paul Cotter.