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. 1991 Mar;57(3):701–706. doi: 10.1128/aem.57.3.701-706.1991

Partial Purification and Characterization of a Bacteriocin Produced by Propionibacterium thoenii†

Wanda J Lyon 1, Bonita A Glatz 1,*
PMCID: PMC182782  PMID: 16348436

Abstract

A partially purified bacteriocin produced by Propionibacterium thoenii designated propionicin PLG-1 was found to be active against closely related species and exhibited a broad spectrum of activity against other microorganisms. Propionicin PLG-1 was found to be heat labile, sensitive to several proteolytic enzymes, and stable at pH 3 to 9. Propionicin PLG-1 was isolated from solid medium, partially purified by ammonium sulfate precipitation, and purified further by gel filtration. Gel filtration experiments revealed that bacteriocin PLG-1 was present as two different protein aggregates with apparent molecular weights of more than 150,000 and approximately 10,000. Resolution of these protein aggregates by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the presence of a protein common to both with an apparent molecular weight of 10,000.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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