• Microbiology and Biotechnology Letters
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• v.34 no.3
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• pp.221-227
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• 2006

BSCX1 was an antimicrobial peptide produced by Bacillus subtilis cx1. Attempts were made to determine the location of inducing factor in the bacteriocin-sensitive cell affecting bacteriocin BSCX1 production. Mixed culture of the bacteriocin producer strain B. subtilis cx1 and its sensitive strain B. subtilis ATCC6633, increased production of bacteriocin BSCX1. The result suggested the presence of a bacteriocin inducing factor in the sensitive strain. The inducing factor was localized in the cell debris and intracellular fraction of B. subtilis ATCC6633. Bacteriocin BSCX1 inducing factor was found to be highly stable in the pH range 2.5-9.5, but inactivated within 3h over $50^{\circ}C$, and treatment with proteinase K destroyed its inducing activity, this result suggested that the inducing factor should be a proteinaceous nature.

• Korean Journal of Food Science and Technology
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• v.34 no.2
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• pp.311-318
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• 2002

A new bacteriocin producing lactic acid bacteria having antagonistic activity against Lactobacillus plantarum, was isolated from Kimchi. It was identified as Leuconostoc mesenteroides, and designated as Leuconostoc mesenteroides B7. The bacteriocin from Leuconostoc mesenteroides B7 named as bacteriocin B7 was stable in the pH range $2.5{\sim}9.5$. Bacteriocin B7 was active over a wide temperature range from $4^{\circ}C$ to $120^{\circ}C$. It was inactivated by proteinase K, trypsin, ${\alpha}-chymotrypsin$, and protease treatments indicating its proteinous nature. Tricine-SDS-PAGE of the purified bacteriocin B7 showed the presence of a single band, having a molecular mass of about 3,500 dalton. Mixed culture of the producer and the indicator, Lb. plantarum KFRI 464 or Lb. delbruekii KFRI 347, increased production of bacteriocin B7. This result suggested the presence of bacteriocin inducing factor in the indicator strain. The inducing factor was localized in cell debris and intracellular faction of the indicator cell, Lb. plantarum KFRI 464. Treatment of the inducing factor with proteinase K destroyed inducing activity. This result strongly suggested that the inducing factor is a protein.