Two different propionicins produced by Propionibacterium thoenii P-127
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Updated: Aug 25, 2026

Using the Overlay Assay to Qualitatively Measure Bacterial Production of and Sensitivity to Pneumococcal Bacteriocins
Published on: September 30, 2014
Galit Ben-Shushan1, Varda Zakin, Natan Gollop
1Department of Food Science, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet-Dagan 50250, Israel. ngollop@volcani.agri.gov.il
Abstract:
The bacteriocin GBZ-1 was purified from the growth media of Propionibacterium thoenii P-127 and was found to have a molecular weight of 6000Da. P. thoenii P-127 also known as the producer of the bacteriocin PLG-1 (MW 10kDa). Under specific growth conditions, on semi-solid media, P. thoenii P-127 produced both PLG-1 and GBZ-1. The N-terminal of GBZ-1 was microsequenced, the gene was cloned and the DNA sequence was determined and identified. GBZ-1 is highly homologous to a protease-activated antimicrobial peptide (PAMP). In contrast to PAMP, it was purified in its active form and no protease digestion was required for its activation. The survival curve of indicator bacteria Lactobacillus delbrueckii subsp. lactic ATCC 4797 showed two phases. The fast phase of 20min was followed by a slow phase. While bacterial survival was reduced by 2logs during the fast phase, bacterial survival was reduced by additional 3logs up to 200min during the slow phase. GBZ-1 activity was affected by magnesium and its activity was completely abolished at 50mM magnesium chloride. Other divalent cations had no effect on GBZ-1 activity of GBZ-1. To the best of our knowledge this is the first report of a bacterium producing two different bacteriocins under different growth conditions.
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