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Two different propionicins produced by Propionibacterium thoenii P-127
Year:
2003
Source of publication :
peptides ( source)
Authors :
Gollop, Natan
;
.
Zakin, Varda
;
.
Volume :
24
Co-Authors:
Ben-Shushan, G., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet-Dagan 50250, Israel
Zakin, V., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet-Dagan 50250, Israel
Gollop, N., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet-Dagan 50250, Israel
Facilitators :
From page:
1733
To page:
1740
(
Total pages:
8
)
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. © 2003 Elsevier Inc. All rights reserved.
Note:
Related Files :
bacteria
bacteriocin
Bacteriocins
Base Sequence
gene sequence
Molecular Sequence Data
unclassified drug
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More details
DOI :
10.1016/j.peptides.2003.08.018
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
21586
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:45
Scientific Publication
Two different propionicins produced by Propionibacterium thoenii P-127
24
Ben-Shushan, G., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet-Dagan 50250, Israel
Zakin, V., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet-Dagan 50250, Israel
Gollop, N., Department of Food Science, Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet-Dagan 50250, Israel
Two different propionicins produced by Propionibacterium thoenii P-127
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. © 2003 Elsevier Inc. All rights reserved.
Scientific Publication
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