• Journal of Life Science
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• v.13 no.5
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• pp.712-717
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• 2003

In order to establish yeast cells that produce leucocin A, a bacteriocin, the 117 bp leucocin A gene with start and stop codons was synthesized and cloned in pAUR123, a yeast vector. Transformed yeast cells showed antibacterial activity against Bacillus subtilis. The leucocin A gene was confirmed by means of PCR methods with plasmid prepared from transformed yeast cells as template and two leucocin A-specific primers. In this results, yeast cells that produce mass amounts of bacteriocin to use as food preservative or antibiotics were established.

• Journal of Life Science
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• v.15 no.6 s.73
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• pp.923-927
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• 2005

ln order to develop yeast cells that produce a bacteriocin on their cell surfaces, the 114 bp Leucocin A gene with stop codon was ligated into pYDl, an yeast vector. The recombinant DNA, pYDl-LeucoA was used to transform yeast (Saccharomyces cerevisiae) cells. Yeast cells harboring pYDl-LeucoA showed antibacterial activity against Bacillus subtilis. To confirm these bacteriocidal yeast cells possess the Leucocin A gone, PCR was performed with plasmid prepared from transformed yeast cells as a template and two Leucocin A-specific primers. In this study, bacteriocidal yeast cells that can be used as an antibiotic or a food preservative were developed.

• KSBB Journal
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• v.19 no.4
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• pp.291-294
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• 2004

The aim of this study was to figure out the antibacterial pattern of leucocin A transformed yeast with culture. Dry cell weight, total secreted protein, and antibacterial activity were increased to 12 hour, after then they showed decrease while protease activity represented the opposite pattern. This implied the production of leucocin A was growth-related. Compared to the result of one hour culture broth, antibacterial activity was about 3.24 fold at 12 hour culture. Maximum growth inhibition rate was 70.57% compared to nontransformed yeast. As the increase of protease in the supernatant, the antibacterial activity was diminished. This study could permit the mass production of bacteriocin to use as antibiotics or food preservatives.

• Journal of Life Science
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• v.15 no.6 s.73
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• pp.847-850
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• 2005

The aim of this study was to increase production of leucocin A, a kind of bacteriocin, in a transformed variety of S. cerevisiae. We investigated optical density, total secreted protein, protease activity, and antibacterial activity for the transformed S. cerevisiae in different carbon sources. The production of leucocin A growth-associated, and antibacterial activity, according to carbon source, was in the order of sucrose, glucose, glycerol, and fructose. Antibacterial activity was $10.6\%$ higher in the presence of sucrose than glucose. This is the first report regarding the effect of carbon sources on the production of leucocin A in transformed S. cerevisiae, as far as we ascertain. Our results could prove useful in the industrial production of natural preservatives.

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.641-641
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• 2005

• Journal of Microbiology and Biotechnology
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• v.7 no.6
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• pp.409-416
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• 1997

Leuconostoc sp. LAB145-3A isolated from kimchi produced a bacteriocin which was active against food pathogens, such as Listeria monocytogenes, Enterococcus faecalis, and E. faecium. Bacteriocin production occurred during the early exponential phase of growth and was stable upto the late stationary phase of growth. Optimum conditions for bacteriocin production were $37^{\circ}C$ with an initial pH of 7.0. The bacteriocin of LAB145-3A was sensitive to proteases, but stable for solvents, pH change and heat treatment. It was stable even at autoclaving temperature for 15 min. The bacteriocin exhibited a bactericidal mode of action against Lactobacillus curvatus LAB170-12. The bacteriocin produced by Leuconostoc sp. LAB145-3A was purified by CM-cellulose cation exchange column chromatography and Sephadex G-50 gel filtration. The purification resulted in an approximate 10,000-fold increase in the specific activity. Approximately 4% of the initial activity was recovered. Purified bacteriocin exhibited a single band on the SDS-PAGE with an apparent molecular weight of 4,400 daltons. This bacteriocin was named leucocin K. Leuconostoc sp. LAB145-3A had two residential plasmids with molecular sizes of 23 kb and 48 kb. A comparison of plasmid profiles between LAB145-3A and its mutants revealed that the 23 kb plasmid (pCA23) was responsible for bacteriocin production and immunity to the bacteriocin in Leuconostoc sp. LAB145-3A.