P3-77 Purification and Partial Characterization of a Bacteriocin Produced by Leuconostoc mesenteroides A11

Wednesday, July 25, 2012
Exhibit Hall (Rhode Island Convention Center)
Lizziane Winkelstroter, University of Sao Paulo, Ribeirao Preto, Brazil
Fabricio Tulini, University of Sao Paulo, Ribeirao Preto, Brazil
Elaine De Martinis, University of São Paulo, Ribeirão Preto, Brazil
Introduction: Bacteriocins produced by lactic acid bacteria are antimicrobial peptides, ribosomally synthesized, with potential application in the control of spoilage and pathogenic bacteria in foods, especially Listeria monocytogenes. These peptides have low toxicity compared to preservatives currently in use, due to their degradation by gastrointestinal enzymes. However, many bacteriocins have not been fully characterized and are not allowed yet for biopreservation.

Purpose: To purify and partially characterize the bacteriocin produced by L. mesenteroides A11 isolated from chicken breast.

Methods: Previous studies showed L. mesenteroides A11 is bacteriocinogenic and inhibits L. monocytogenes. In this study, the partially purified bacteriocin was obtained from the neutralized filter-sterilized culture supernatant of L. mesenteroides A11 grown in BHI broth at 25 °C for 24 h. For that, purification with Amberlite® XAD-16 resin, followed by solid phase extraction – SPE were employed. Fractions were obtained with a 2-propanol gradient and collected in each step of purification assay. The organic solvent was removed in a rotatory evaporator and the titre of the bacteriocin in the remaining aqueous solution was determined by the critical dilution assay, expressed as arbitrary units per ml (AU/ml), using L. monocytogenes as indicator strain. The final active fraction was concentrated by freeze-drying and partially purified bacteriocin was analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) to estimate molecular weight by means of silver staining and biological revelation of gel.

Results: Bacteriocin titre in initial L. mesenteroides A11 culture supernatant was 3,200 AU/ml. High recovery of bacteriocin was obtained with XAD-SPE since no loss was detected in bacteriocin quantification in fractions collected during purification steps. By SDS-PAGE, molecular weight of L. mesenteroides A11 bacteriocin was estimated as 3.5 to 8.5kDa.

Significance: Purification of antimicrobial peptides from L. mesenteroides A11 provided information that may be useful to design food biopreservation applications.