Characterization of a broad-spectrum endolysin rLysJNwz and its utility against Salmonella in foods
Abstract Salmonella is a common foodborne pathogen worldwide. The use of bacteriophage-encoded endolysins as antimicrobial agents is a promising approach for controlling pathogenic contamination. In this context, a recombinant endolysin named rLysJNwz, consisting of a single domain falling with the...
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| Autor*in: |
Shen, Kaisheng [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2023 |
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© The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer Berlin Heidelberg, 1984, 107(2023), 10 vom: 11. Apr., Seite 3229-3241 |
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| Übergeordnetes Werk: |
volume:107 ; year:2023 ; number:10 ; day:11 ; month:04 ; pages:3229-3241 |
| Links: |
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| DOI / URN: |
10.1007/s00253-023-12500-9 |
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OLC2134807199 |
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| 520 | |a Abstract Salmonella is a common foodborne pathogen worldwide. The use of bacteriophage-encoded endolysins as antimicrobial agents is a promising approach for controlling pathogenic contamination. In this context, a recombinant endolysin named rLysJNwz, consisting of a single domain falling with the L-alanogyl-D-glutamate peptidase-like family, was cloned, expressed, and characterized. The yield of rLysJNwz was about 25 mg/L. Synergy between 7.5 μg/mL rLysJNwz and 0.5 mmol/L EDTA could decrease the viable counts of Salmonella NCTC 8271 by 93.28%. A synergistic effect between rLysJNwz and polymyxin B was demonstrated, exhibiting the MIC of polymyxin B decreased by twofold. Specifically, rlysJNwz had strong thermostability at temperatures (4–95 °C) and maintained high activity at pHs from 5.0 to 11.0. rlysJNwz was a metal ion‐dependent peptidase, which activated by divalent metal ions such as $ Zn^{2+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Moreover, it was also found that the synergism of rlysJNwz and EDTA had bactericidal activities against a broad range of Gram-negative bacteria, including several multidrug-resistant bacteria. The application of rLysJNwz combined with EDTA was evaluated on contaminated eggs and lettuce for 60 min, displaying more than 86.7% and 86.5% reduction of viable Salmonella, respectively. Hence, these results suggest that rLysJNwz is a potential antibacterial agent to control Salmonella, especially antibiotic-resistant pathogen contamination in the field of food safety. Key points • rLysJNwz shows lytic activities against a broad range of Gram-negative bacteria. • Endolysin rLysJNwz is a stable metalloenzyme and has high thermostability. • rLysJNwz and 0.5 mmol/L EDTA synergistically inactivate Salmonella on eggs and lettuce. | ||
| 650 | 4 | |a Endolysin | |
| 650 | 4 | |a Expression | |
| 650 | 4 | |a Characterization | |
| 650 | 4 | |a Multidrug-resistant bacteria | |
| 650 | 4 | |a Bactericidal activity | |
| 700 | 1 | |a Shu, Mei |4 aut | |
| 700 | 1 | |a Zhong, Chan |4 aut | |
| 700 | 1 | |a Zhao, Yuanyang |4 aut | |
| 700 | 1 | |a Bao, Shiwei |4 aut | |
| 700 | 1 | |a Pan, Hong |4 aut | |
| 700 | 1 | |a Wang, Shuchao |4 aut | |
| 700 | 1 | |a Wu, Guoping |0 (orcid)0000-0001-7797-7627 |4 aut | |
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10.1007/s00253-023-12500-9 doi (DE-627)OLC2134807199 (DE-He213)s00253-023-12500-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Shen, Kaisheng verfasserin aut Characterization of a broad-spectrum endolysin rLysJNwz and its utility against Salmonella in foods 2023 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. Abstract Salmonella is a common foodborne pathogen worldwide. The use of bacteriophage-encoded endolysins as antimicrobial agents is a promising approach for controlling pathogenic contamination. In this context, a recombinant endolysin named rLysJNwz, consisting of a single domain falling with the L-alanogyl-D-glutamate peptidase-like family, was cloned, expressed, and characterized. The yield of rLysJNwz was about 25 mg/L. Synergy between 7.5 μg/mL rLysJNwz and 0.5 mmol/L EDTA could decrease the viable counts of Salmonella NCTC 8271 by 93.28%. A synergistic effect between rLysJNwz and polymyxin B was demonstrated, exhibiting the MIC of polymyxin B decreased by twofold. Specifically, rlysJNwz had strong thermostability at temperatures (4–95 °C) and maintained high activity at pHs from 5.0 to 11.0. rlysJNwz was a metal ion‐dependent peptidase, which activated by divalent metal ions such as $ Zn^{2+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Moreover, it was also found that the synergism of rlysJNwz and EDTA had bactericidal activities against a broad range of Gram-negative bacteria, including several multidrug-resistant bacteria. The application of rLysJNwz combined with EDTA was evaluated on contaminated eggs and lettuce for 60 min, displaying more than 86.7% and 86.5% reduction of viable Salmonella, respectively. Hence, these results suggest that rLysJNwz is a potential antibacterial agent to control Salmonella, especially antibiotic-resistant pathogen contamination in the field of food safety. Key points • rLysJNwz shows lytic activities against a broad range of Gram-negative bacteria. • Endolysin rLysJNwz is a stable metalloenzyme and has high thermostability. • rLysJNwz and 0.5 mmol/L EDTA synergistically inactivate Salmonella on eggs and lettuce. Endolysin Expression Characterization Multidrug-resistant bacteria Bactericidal activity Shu, Mei aut Zhong, Chan aut Zhao, Yuanyang aut Bao, Shiwei aut Pan, Hong aut Wang, Shuchao aut Wu, Guoping (orcid)0000-0001-7797-7627 aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 107(2023), 10 vom: 11. Apr., Seite 3229-3241 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:107 year:2023 number:10 day:11 month:04 pages:3229-3241 https://doi.org/10.1007/s00253-023-12500-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4277 AR 107 2023 10 11 04 3229-3241 |
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10.1007/s00253-023-12500-9 doi (DE-627)OLC2134807199 (DE-He213)s00253-023-12500-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Shen, Kaisheng verfasserin aut Characterization of a broad-spectrum endolysin rLysJNwz and its utility against Salmonella in foods 2023 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. Abstract Salmonella is a common foodborne pathogen worldwide. The use of bacteriophage-encoded endolysins as antimicrobial agents is a promising approach for controlling pathogenic contamination. In this context, a recombinant endolysin named rLysJNwz, consisting of a single domain falling with the L-alanogyl-D-glutamate peptidase-like family, was cloned, expressed, and characterized. The yield of rLysJNwz was about 25 mg/L. Synergy between 7.5 μg/mL rLysJNwz and 0.5 mmol/L EDTA could decrease the viable counts of Salmonella NCTC 8271 by 93.28%. A synergistic effect between rLysJNwz and polymyxin B was demonstrated, exhibiting the MIC of polymyxin B decreased by twofold. Specifically, rlysJNwz had strong thermostability at temperatures (4–95 °C) and maintained high activity at pHs from 5.0 to 11.0. rlysJNwz was a metal ion‐dependent peptidase, which activated by divalent metal ions such as $ Zn^{2+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Moreover, it was also found that the synergism of rlysJNwz and EDTA had bactericidal activities against a broad range of Gram-negative bacteria, including several multidrug-resistant bacteria. The application of rLysJNwz combined with EDTA was evaluated on contaminated eggs and lettuce for 60 min, displaying more than 86.7% and 86.5% reduction of viable Salmonella, respectively. Hence, these results suggest that rLysJNwz is a potential antibacterial agent to control Salmonella, especially antibiotic-resistant pathogen contamination in the field of food safety. Key points • rLysJNwz shows lytic activities against a broad range of Gram-negative bacteria. • Endolysin rLysJNwz is a stable metalloenzyme and has high thermostability. • rLysJNwz and 0.5 mmol/L EDTA synergistically inactivate Salmonella on eggs and lettuce. Endolysin Expression Characterization Multidrug-resistant bacteria Bactericidal activity Shu, Mei aut Zhong, Chan aut Zhao, Yuanyang aut Bao, Shiwei aut Pan, Hong aut Wang, Shuchao aut Wu, Guoping (orcid)0000-0001-7797-7627 aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 107(2023), 10 vom: 11. Apr., Seite 3229-3241 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:107 year:2023 number:10 day:11 month:04 pages:3229-3241 https://doi.org/10.1007/s00253-023-12500-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4277 AR 107 2023 10 11 04 3229-3241 |
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10.1007/s00253-023-12500-9 doi (DE-627)OLC2134807199 (DE-He213)s00253-023-12500-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Shen, Kaisheng verfasserin aut Characterization of a broad-spectrum endolysin rLysJNwz and its utility against Salmonella in foods 2023 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. Abstract Salmonella is a common foodborne pathogen worldwide. The use of bacteriophage-encoded endolysins as antimicrobial agents is a promising approach for controlling pathogenic contamination. In this context, a recombinant endolysin named rLysJNwz, consisting of a single domain falling with the L-alanogyl-D-glutamate peptidase-like family, was cloned, expressed, and characterized. The yield of rLysJNwz was about 25 mg/L. Synergy between 7.5 μg/mL rLysJNwz and 0.5 mmol/L EDTA could decrease the viable counts of Salmonella NCTC 8271 by 93.28%. A synergistic effect between rLysJNwz and polymyxin B was demonstrated, exhibiting the MIC of polymyxin B decreased by twofold. Specifically, rlysJNwz had strong thermostability at temperatures (4–95 °C) and maintained high activity at pHs from 5.0 to 11.0. rlysJNwz was a metal ion‐dependent peptidase, which activated by divalent metal ions such as $ Zn^{2+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Moreover, it was also found that the synergism of rlysJNwz and EDTA had bactericidal activities against a broad range of Gram-negative bacteria, including several multidrug-resistant bacteria. The application of rLysJNwz combined with EDTA was evaluated on contaminated eggs and lettuce for 60 min, displaying more than 86.7% and 86.5% reduction of viable Salmonella, respectively. Hence, these results suggest that rLysJNwz is a potential antibacterial agent to control Salmonella, especially antibiotic-resistant pathogen contamination in the field of food safety. Key points • rLysJNwz shows lytic activities against a broad range of Gram-negative bacteria. • Endolysin rLysJNwz is a stable metalloenzyme and has high thermostability. • rLysJNwz and 0.5 mmol/L EDTA synergistically inactivate Salmonella on eggs and lettuce. Endolysin Expression Characterization Multidrug-resistant bacteria Bactericidal activity Shu, Mei aut Zhong, Chan aut Zhao, Yuanyang aut Bao, Shiwei aut Pan, Hong aut Wang, Shuchao aut Wu, Guoping (orcid)0000-0001-7797-7627 aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 107(2023), 10 vom: 11. Apr., Seite 3229-3241 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:107 year:2023 number:10 day:11 month:04 pages:3229-3241 https://doi.org/10.1007/s00253-023-12500-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4277 AR 107 2023 10 11 04 3229-3241 |
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10.1007/s00253-023-12500-9 doi (DE-627)OLC2134807199 (DE-He213)s00253-023-12500-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Shen, Kaisheng verfasserin aut Characterization of a broad-spectrum endolysin rLysJNwz and its utility against Salmonella in foods 2023 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. Abstract Salmonella is a common foodborne pathogen worldwide. The use of bacteriophage-encoded endolysins as antimicrobial agents is a promising approach for controlling pathogenic contamination. In this context, a recombinant endolysin named rLysJNwz, consisting of a single domain falling with the L-alanogyl-D-glutamate peptidase-like family, was cloned, expressed, and characterized. The yield of rLysJNwz was about 25 mg/L. Synergy between 7.5 μg/mL rLysJNwz and 0.5 mmol/L EDTA could decrease the viable counts of Salmonella NCTC 8271 by 93.28%. A synergistic effect between rLysJNwz and polymyxin B was demonstrated, exhibiting the MIC of polymyxin B decreased by twofold. Specifically, rlysJNwz had strong thermostability at temperatures (4–95 °C) and maintained high activity at pHs from 5.0 to 11.0. rlysJNwz was a metal ion‐dependent peptidase, which activated by divalent metal ions such as $ Zn^{2+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Moreover, it was also found that the synergism of rlysJNwz and EDTA had bactericidal activities against a broad range of Gram-negative bacteria, including several multidrug-resistant bacteria. The application of rLysJNwz combined with EDTA was evaluated on contaminated eggs and lettuce for 60 min, displaying more than 86.7% and 86.5% reduction of viable Salmonella, respectively. Hence, these results suggest that rLysJNwz is a potential antibacterial agent to control Salmonella, especially antibiotic-resistant pathogen contamination in the field of food safety. Key points • rLysJNwz shows lytic activities against a broad range of Gram-negative bacteria. • Endolysin rLysJNwz is a stable metalloenzyme and has high thermostability. • rLysJNwz and 0.5 mmol/L EDTA synergistically inactivate Salmonella on eggs and lettuce. Endolysin Expression Characterization Multidrug-resistant bacteria Bactericidal activity Shu, Mei aut Zhong, Chan aut Zhao, Yuanyang aut Bao, Shiwei aut Pan, Hong aut Wang, Shuchao aut Wu, Guoping (orcid)0000-0001-7797-7627 aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 107(2023), 10 vom: 11. Apr., Seite 3229-3241 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:107 year:2023 number:10 day:11 month:04 pages:3229-3241 https://doi.org/10.1007/s00253-023-12500-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4277 AR 107 2023 10 11 04 3229-3241 |
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10.1007/s00253-023-12500-9 doi (DE-627)OLC2134807199 (DE-He213)s00253-023-12500-9-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Shen, Kaisheng verfasserin aut Characterization of a broad-spectrum endolysin rLysJNwz and its utility against Salmonella in foods 2023 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. Abstract Salmonella is a common foodborne pathogen worldwide. The use of bacteriophage-encoded endolysins as antimicrobial agents is a promising approach for controlling pathogenic contamination. In this context, a recombinant endolysin named rLysJNwz, consisting of a single domain falling with the L-alanogyl-D-glutamate peptidase-like family, was cloned, expressed, and characterized. The yield of rLysJNwz was about 25 mg/L. Synergy between 7.5 μg/mL rLysJNwz and 0.5 mmol/L EDTA could decrease the viable counts of Salmonella NCTC 8271 by 93.28%. A synergistic effect between rLysJNwz and polymyxin B was demonstrated, exhibiting the MIC of polymyxin B decreased by twofold. Specifically, rlysJNwz had strong thermostability at temperatures (4–95 °C) and maintained high activity at pHs from 5.0 to 11.0. rlysJNwz was a metal ion‐dependent peptidase, which activated by divalent metal ions such as $ Zn^{2+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Moreover, it was also found that the synergism of rlysJNwz and EDTA had bactericidal activities against a broad range of Gram-negative bacteria, including several multidrug-resistant bacteria. The application of rLysJNwz combined with EDTA was evaluated on contaminated eggs and lettuce for 60 min, displaying more than 86.7% and 86.5% reduction of viable Salmonella, respectively. Hence, these results suggest that rLysJNwz is a potential antibacterial agent to control Salmonella, especially antibiotic-resistant pathogen contamination in the field of food safety. Key points • rLysJNwz shows lytic activities against a broad range of Gram-negative bacteria. • Endolysin rLysJNwz is a stable metalloenzyme and has high thermostability. • rLysJNwz and 0.5 mmol/L EDTA synergistically inactivate Salmonella on eggs and lettuce. Endolysin Expression Characterization Multidrug-resistant bacteria Bactericidal activity Shu, Mei aut Zhong, Chan aut Zhao, Yuanyang aut Bao, Shiwei aut Pan, Hong aut Wang, Shuchao aut Wu, Guoping (orcid)0000-0001-7797-7627 aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 107(2023), 10 vom: 11. Apr., Seite 3229-3241 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:107 year:2023 number:10 day:11 month:04 pages:3229-3241 https://doi.org/10.1007/s00253-023-12500-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_267 GBV_ILN_2018 GBV_ILN_4277 AR 107 2023 10 11 04 3229-3241 |
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Characterization of a broad-spectrum endolysin rLysJNwz and its utility against Salmonella in foods |
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Abstract Salmonella is a common foodborne pathogen worldwide. The use of bacteriophage-encoded endolysins as antimicrobial agents is a promising approach for controlling pathogenic contamination. In this context, a recombinant endolysin named rLysJNwz, consisting of a single domain falling with the L-alanogyl-D-glutamate peptidase-like family, was cloned, expressed, and characterized. The yield of rLysJNwz was about 25 mg/L. Synergy between 7.5 μg/mL rLysJNwz and 0.5 mmol/L EDTA could decrease the viable counts of Salmonella NCTC 8271 by 93.28%. A synergistic effect between rLysJNwz and polymyxin B was demonstrated, exhibiting the MIC of polymyxin B decreased by twofold. Specifically, rlysJNwz had strong thermostability at temperatures (4–95 °C) and maintained high activity at pHs from 5.0 to 11.0. rlysJNwz was a metal ion‐dependent peptidase, which activated by divalent metal ions such as $ Zn^{2+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Moreover, it was also found that the synergism of rlysJNwz and EDTA had bactericidal activities against a broad range of Gram-negative bacteria, including several multidrug-resistant bacteria. The application of rLysJNwz combined with EDTA was evaluated on contaminated eggs and lettuce for 60 min, displaying more than 86.7% and 86.5% reduction of viable Salmonella, respectively. Hence, these results suggest that rLysJNwz is a potential antibacterial agent to control Salmonella, especially antibiotic-resistant pathogen contamination in the field of food safety. Key points • rLysJNwz shows lytic activities against a broad range of Gram-negative bacteria. • Endolysin rLysJNwz is a stable metalloenzyme and has high thermostability. • rLysJNwz and 0.5 mmol/L EDTA synergistically inactivate Salmonella on eggs and lettuce. © The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. |
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Abstract Salmonella is a common foodborne pathogen worldwide. The use of bacteriophage-encoded endolysins as antimicrobial agents is a promising approach for controlling pathogenic contamination. In this context, a recombinant endolysin named rLysJNwz, consisting of a single domain falling with the L-alanogyl-D-glutamate peptidase-like family, was cloned, expressed, and characterized. The yield of rLysJNwz was about 25 mg/L. Synergy between 7.5 μg/mL rLysJNwz and 0.5 mmol/L EDTA could decrease the viable counts of Salmonella NCTC 8271 by 93.28%. A synergistic effect between rLysJNwz and polymyxin B was demonstrated, exhibiting the MIC of polymyxin B decreased by twofold. Specifically, rlysJNwz had strong thermostability at temperatures (4–95 °C) and maintained high activity at pHs from 5.0 to 11.0. rlysJNwz was a metal ion‐dependent peptidase, which activated by divalent metal ions such as $ Zn^{2+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Moreover, it was also found that the synergism of rlysJNwz and EDTA had bactericidal activities against a broad range of Gram-negative bacteria, including several multidrug-resistant bacteria. The application of rLysJNwz combined with EDTA was evaluated on contaminated eggs and lettuce for 60 min, displaying more than 86.7% and 86.5% reduction of viable Salmonella, respectively. Hence, these results suggest that rLysJNwz is a potential antibacterial agent to control Salmonella, especially antibiotic-resistant pathogen contamination in the field of food safety. Key points • rLysJNwz shows lytic activities against a broad range of Gram-negative bacteria. • Endolysin rLysJNwz is a stable metalloenzyme and has high thermostability. • rLysJNwz and 0.5 mmol/L EDTA synergistically inactivate Salmonella on eggs and lettuce. © The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. |
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Abstract Salmonella is a common foodborne pathogen worldwide. The use of bacteriophage-encoded endolysins as antimicrobial agents is a promising approach for controlling pathogenic contamination. In this context, a recombinant endolysin named rLysJNwz, consisting of a single domain falling with the L-alanogyl-D-glutamate peptidase-like family, was cloned, expressed, and characterized. The yield of rLysJNwz was about 25 mg/L. Synergy between 7.5 μg/mL rLysJNwz and 0.5 mmol/L EDTA could decrease the viable counts of Salmonella NCTC 8271 by 93.28%. A synergistic effect between rLysJNwz and polymyxin B was demonstrated, exhibiting the MIC of polymyxin B decreased by twofold. Specifically, rlysJNwz had strong thermostability at temperatures (4–95 °C) and maintained high activity at pHs from 5.0 to 11.0. rlysJNwz was a metal ion‐dependent peptidase, which activated by divalent metal ions such as $ Zn^{2+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Moreover, it was also found that the synergism of rlysJNwz and EDTA had bactericidal activities against a broad range of Gram-negative bacteria, including several multidrug-resistant bacteria. The application of rLysJNwz combined with EDTA was evaluated on contaminated eggs and lettuce for 60 min, displaying more than 86.7% and 86.5% reduction of viable Salmonella, respectively. Hence, these results suggest that rLysJNwz is a potential antibacterial agent to control Salmonella, especially antibiotic-resistant pathogen contamination in the field of food safety. Key points • rLysJNwz shows lytic activities against a broad range of Gram-negative bacteria. • Endolysin rLysJNwz is a stable metalloenzyme and has high thermostability. • rLysJNwz and 0.5 mmol/L EDTA synergistically inactivate Salmonella on eggs and lettuce. © The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. |
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A synergistic effect between rLysJNwz and polymyxin B was demonstrated, exhibiting the MIC of polymyxin B decreased by twofold. Specifically, rlysJNwz had strong thermostability at temperatures (4–95 °C) and maintained high activity at pHs from 5.0 to 11.0. rlysJNwz was a metal ion‐dependent peptidase, which activated by divalent metal ions such as $ Zn^{2+} $, $ Mn^{2+} $, or $ Ca^{2+} $. Moreover, it was also found that the synergism of rlysJNwz and EDTA had bactericidal activities against a broad range of Gram-negative bacteria, including several multidrug-resistant bacteria. The application of rLysJNwz combined with EDTA was evaluated on contaminated eggs and lettuce for 60 min, displaying more than 86.7% and 86.5% reduction of viable Salmonella, respectively. Hence, these results suggest that rLysJNwz is a potential antibacterial agent to control Salmonella, especially antibiotic-resistant pathogen contamination in the field of food safety. Key points • rLysJNwz shows lytic activities against a broad range of Gram-negative bacteria. • Endolysin rLysJNwz is a stable metalloenzyme and has high thermostability. • rLysJNwz and 0.5 mmol/L EDTA synergistically inactivate Salmonella on eggs and lettuce.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Endolysin</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Expression</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Characterization</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Multidrug-resistant bacteria</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Bactericidal activity</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Shu, Mei</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhong, Chan</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhao, Yuanyang</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bao, Shiwei</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pan, Hong</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Shuchao</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wu, Guoping</subfield><subfield code="0">(orcid)0000-0001-7797-7627</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Applied microbiology and biotechnology</subfield><subfield code="d">Springer Berlin Heidelberg, 1984</subfield><subfield code="g">107(2023), 10 vom: 11. Apr., Seite 3229-3241</subfield><subfield code="w">(DE-627)129942634</subfield><subfield code="w">(DE-600)392453-1</subfield><subfield code="w">(DE-576)015507750</subfield><subfield code="x">0175-7598</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:107</subfield><subfield code="g">year:2023</subfield><subfield code="g">number:10</subfield><subfield code="g">day:11</subfield><subfield code="g">month:04</subfield><subfield code="g">pages:3229-3241</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">https://doi.org/10.1007/s00253-023-12500-9</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-TEC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_267</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2018</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4277</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">107</subfield><subfield code="j">2023</subfield><subfield code="e">10</subfield><subfield code="b">11</subfield><subfield code="c">04</subfield><subfield code="h">3229-3241</subfield></datafield></record></collection>
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