Expression, purification and antimicrobial activity of recombinant pediocin PA-1 M31L, a PA-1 derivative with enhanced stability

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Author
Kuniyoshi, Taís Mayumi
O’ Connor, Paula M.
Arbulu, Sara
Mesa-Pereira, Beatriz
Pinheiro de Souza Oliveira, Ricardo
Hill, Collin
Ross, Paul
Cotter, Paul D.
Keyword
Pediocin PA −1
recombinant expression
Date
2019-03-01

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URI
http://hdl.handle.net/11019/2330
Citation
Kuniyoshi TM, O’ Connor PM, Arbulu S, Mesa-Pereira B, Pinheiro de Souza Oliveira R, Hill C, Ross P, Cotter PD. Expression, purification and antimicrobial activity of recombinant pediocin PA-1 M31L, a PA-1 derivative with enhanced stability. Access Microbiology 2019;1(1A); doi https://doi.org/10.1099/acmi.ac2019.po0471.
Abstract
Pediocin, the prototypical class IIa bacteriocin, is an efficient antilisterial molecule. Loss of pediocin PA-1 activity is attributed to methionine oxidation at position 31 and this can be overcome by substituting methionine for leucine (pediocin M31L). The aim of this study was to produce pediocin M31L with enhanced stability by recombinant expression in E. coli cells.
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