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dc.contributor.authorKuniyoshi, Taís Mayumi
dc.contributor.authorO’ Connor, Paula M.
dc.contributor.authorArbulu, Sara
dc.contributor.authorMesa-Pereira, Beatriz
dc.contributor.authorPinheiro de Souza Oliveira, Ricardo
dc.contributor.authorHill, Collin
dc.contributor.authorRoss, Paul
dc.contributor.authorCotter, Paul D.
dc.date.accessioned2020-08-28T14:57:28Z
dc.date.available2020-08-28T14:57:28Z
dc.date.issued2019-03-01
dc.identifier.citationKuniyoshi 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.en_US
dc.identifier.issn2516-8290
dc.identifier.urihttp://hdl.handle.net/11019/2330
dc.descriptionMeeting presentationen_US
dc.description.abstractPediocin, 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.en_US
dc.language.isoenen_US
dc.publisherMicrobiology Societyen_US
dc.relation.ispartofseriesAccess Microbiology;
dc.subjectPediocin PA −1en_US
dc.subjectrecombinant expressionen_US
dc.titleExpression, purification and antimicrobial activity of recombinant pediocin PA-1 M31L, a PA-1 derivative with enhanced stabilityen_US
dc.typeMeetings and Proceedingsen_US
dc.identifier.doihttps://doi.org/10.1099/acmi.ac2019.po0471
dc.source.volume1
dc.source.issue1A
refterms.dateFOA2020-08-28T14:57:28Z


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