Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2
Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extr...
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| Autor*in: |
Tulini, Fabricio L. [verfasserIn] |
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E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2014transfer abstract |
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8 |
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Enthalten in: Fibroblast growth factor and endothelin-1 receptors mediate the response of human striatal precursor cells to hypoxia - Ambrosini, S. ELSEVIER, 2015, Amsterdam |
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| Übergeordnetes Werk: |
volume:173 ; year:2014 ; day:3 ; month:03 ; pages:81-88 ; extent:8 |
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| DOI / URN: |
10.1016/j.ijfoodmicro.2013.12.019 |
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| 245 | 1 | 0 | |a Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2 |
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| 520 | |a Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. | ||
| 520 | |a Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. | ||
| 700 | 1 | |a Lohans, Christopher T. |4 oth | |
| 700 | 1 | |a Bordon, Karla C.F. |4 oth | |
| 700 | 1 | |a Zheng, Jing |4 oth | |
| 700 | 1 | |a Arantes, Eliane C. |4 oth | |
| 700 | 1 | |a Vederas, John C. |4 oth | |
| 700 | 1 | |a De Martinis, Elaine C.P. |4 oth | |
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10.1016/j.ijfoodmicro.2013.12.019 doi GBVA2014005000016.pica (DE-627)ELV033731209 (ELSEVIER)S0168-1605(13)00596-5 DE-627 ger DE-627 rakwb eng 570 630 640 570 DE-600 630 DE-600 640 DE-600 610 VZ 630 640 VZ 58.34 bkl Tulini, Fabricio L. verfasserin aut Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2 2014transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. Lohans, Christopher T. oth Bordon, Karla C.F. oth Zheng, Jing oth Arantes, Eliane C. oth Vederas, John C. oth De Martinis, Elaine C.P. oth Enthalten in Elsevier Ambrosini, S. ELSEVIER Fibroblast growth factor and endothelin-1 receptors mediate the response of human striatal precursor cells to hypoxia 2015 Amsterdam (DE-627)ELV018407722 volume:173 year:2014 day:3 month:03 pages:81-88 extent:8 https://doi.org/10.1016/j.ijfoodmicro.2013.12.019 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_40 58.34 Lebensmitteltechnologie VZ AR 173 2014 3 0303 81-88 8 045F 570 |
| spelling |
10.1016/j.ijfoodmicro.2013.12.019 doi GBVA2014005000016.pica (DE-627)ELV033731209 (ELSEVIER)S0168-1605(13)00596-5 DE-627 ger DE-627 rakwb eng 570 630 640 570 DE-600 630 DE-600 640 DE-600 610 VZ 630 640 VZ 58.34 bkl Tulini, Fabricio L. verfasserin aut Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2 2014transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. Lohans, Christopher T. oth Bordon, Karla C.F. oth Zheng, Jing oth Arantes, Eliane C. oth Vederas, John C. oth De Martinis, Elaine C.P. oth Enthalten in Elsevier Ambrosini, S. ELSEVIER Fibroblast growth factor and endothelin-1 receptors mediate the response of human striatal precursor cells to hypoxia 2015 Amsterdam (DE-627)ELV018407722 volume:173 year:2014 day:3 month:03 pages:81-88 extent:8 https://doi.org/10.1016/j.ijfoodmicro.2013.12.019 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_40 58.34 Lebensmitteltechnologie VZ AR 173 2014 3 0303 81-88 8 045F 570 |
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10.1016/j.ijfoodmicro.2013.12.019 doi GBVA2014005000016.pica (DE-627)ELV033731209 (ELSEVIER)S0168-1605(13)00596-5 DE-627 ger DE-627 rakwb eng 570 630 640 570 DE-600 630 DE-600 640 DE-600 610 VZ 630 640 VZ 58.34 bkl Tulini, Fabricio L. verfasserin aut Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2 2014transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. Lohans, Christopher T. oth Bordon, Karla C.F. oth Zheng, Jing oth Arantes, Eliane C. oth Vederas, John C. oth De Martinis, Elaine C.P. oth Enthalten in Elsevier Ambrosini, S. ELSEVIER Fibroblast growth factor and endothelin-1 receptors mediate the response of human striatal precursor cells to hypoxia 2015 Amsterdam (DE-627)ELV018407722 volume:173 year:2014 day:3 month:03 pages:81-88 extent:8 https://doi.org/10.1016/j.ijfoodmicro.2013.12.019 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_40 58.34 Lebensmitteltechnologie VZ AR 173 2014 3 0303 81-88 8 045F 570 |
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10.1016/j.ijfoodmicro.2013.12.019 doi GBVA2014005000016.pica (DE-627)ELV033731209 (ELSEVIER)S0168-1605(13)00596-5 DE-627 ger DE-627 rakwb eng 570 630 640 570 DE-600 630 DE-600 640 DE-600 610 VZ 630 640 VZ 58.34 bkl Tulini, Fabricio L. verfasserin aut Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2 2014transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. Lohans, Christopher T. oth Bordon, Karla C.F. oth Zheng, Jing oth Arantes, Eliane C. oth Vederas, John C. oth De Martinis, Elaine C.P. oth Enthalten in Elsevier Ambrosini, S. ELSEVIER Fibroblast growth factor and endothelin-1 receptors mediate the response of human striatal precursor cells to hypoxia 2015 Amsterdam (DE-627)ELV018407722 volume:173 year:2014 day:3 month:03 pages:81-88 extent:8 https://doi.org/10.1016/j.ijfoodmicro.2013.12.019 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_40 58.34 Lebensmitteltechnologie VZ AR 173 2014 3 0303 81-88 8 045F 570 |
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10.1016/j.ijfoodmicro.2013.12.019 doi GBVA2014005000016.pica (DE-627)ELV033731209 (ELSEVIER)S0168-1605(13)00596-5 DE-627 ger DE-627 rakwb eng 570 630 640 570 DE-600 630 DE-600 640 DE-600 610 VZ 630 640 VZ 58.34 bkl Tulini, Fabricio L. verfasserin aut Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2 2014transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. Lohans, Christopher T. oth Bordon, Karla C.F. oth Zheng, Jing oth Arantes, Eliane C. oth Vederas, John C. oth De Martinis, Elaine C.P. oth Enthalten in Elsevier Ambrosini, S. ELSEVIER Fibroblast growth factor and endothelin-1 receptors mediate the response of human striatal precursor cells to hypoxia 2015 Amsterdam (DE-627)ELV018407722 volume:173 year:2014 day:3 month:03 pages:81-88 extent:8 https://doi.org/10.1016/j.ijfoodmicro.2013.12.019 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_40 58.34 Lebensmitteltechnologie VZ AR 173 2014 3 0303 81-88 8 045F 570 |
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Enthalten in Fibroblast growth factor and endothelin-1 receptors mediate the response of human striatal precursor cells to hypoxia Amsterdam volume:173 year:2014 day:3 month:03 pages:81-88 extent:8 |
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Tulini, Fabricio L. @@aut@@ Lohans, Christopher T. @@oth@@ Bordon, Karla C.F. @@oth@@ Zheng, Jing @@oth@@ Arantes, Eliane C. @@oth@@ Vederas, John C. @@oth@@ De Martinis, Elaine C.P. @@oth@@ |
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purification and characterization of antimicrobial peptides from fish isolate carnobacterium maltaromaticum c2: carnobacteriocin x and carnolysins a1 and a2 |
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Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2 |
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Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. |
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Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. |
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Carnobacterium maltaromaticum C2, isolated from Brazilian smoked fish (Surubim, Pseudoplatystoma sp.), was found to exert antimicrobial activity against Listeria monocytogenes, an important foodborne pathogen. In this study, the bacteriocins produced by C. maltaromaticum C2 were purified via an extraction with XAD-16 resin, a C18 solid phase extraction, followed by reversed-phase fast protein liquid chromatography. The purified active fractions were characterized using tandem mass spectrometry, permitting the identification of multiple bacteriocins. Carnobacteriocins BM1, B1, and a variant of carnobacteriocin B2 were all found, providing much of the antilisterial activity. Additionally, we herein report the first isolation of the previously predicted antimicrobial peptide carnobacteriocin X. Moreover, C. maltaromaticum C2 produces a novel two-component lantibiotic, termed carnolysin, homologous to enterococcal cytolysin. This lantibiotic is antimicrobially inactive when tested against the non-bacteriocinogenic strain C. maltaromaticum A9b−, likely requiring an additional proteolytic cleavage to reach maturity. |
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Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2 |
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