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Partial Characterization and Purification of Enterocin K25 Linked to the Plasmid in Enterococcus sp. K25  

Moon, Gi-Seong (Commensals and Microflora, Institute of Food Research, Norwich Research Park)
Kim, Wang-June (Food Safety Research Division, Korea Food Research Institute)
Publication Information
Food Science and Biotechnology / v.14, no.5, 2005 , pp. 581-585 More about this Journal
Abstract
The antimicrobial activity of partially purified enterocin K25, produced by Enterococcus sp. K25, was abolished by proteases such as pepsin and proteinase K. The bacteriocin was resistant to heat treatment at $75^{\circ}C$ for 15 min and lost 75% of its activity at $100^{\circ}C$ for 30 min. Enterocin K25 showed bactericidal mode of action against an indicator strain, Lactobacillus plantarum NCDO 955. Enterocin K25 was purified to 112.6-fold purity via conventional steps of ammonium sulfate precipitation, ion exchange chromatography, and reversed phase high performance liquid chromatography (RP-HPLC). The molecular mass of the purified enterocin K25 was estimated as 4.3 kDa on an electrophoresis gel. Plasmid (${\sim}6.5\;kb$) linkage of production of enterocin K25 was confirmed by plasmid curing.
Keywords
enterocin K25; bacteriocin purification; Enterococcus sp.;
Citations & Related Records
Times Cited By KSCI : 3  (Citation Analysis)
Times Cited By Web Of Science : 1  (Related Records In Web of Science)
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