Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28
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2024
Authors
Atanasković, MarijaMorić, Ivana
Rokić, Miloš
Đokić, Anđela
Pantović, Jelena
Despotović, Dragana
Šenerović, Lidija
Article (Accepted Version)
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SalmonellaEnteritidis is the most commonly reported pathogen for foodborne illness outbreaks in both underdeveloped and developed regions. S. Enteritidis biofilms, which form on various food contact surfaces, are resistant to conventional physical and chemical cleaning and disinfection procedures routinely used in food processing. The aim of this study was to identify novel, industrially applicable enzymes that are active against S. Enteritidis biofilms. We describe the properties and anti-biofilm activity of heterologously expressed β-glucosidase B derived from the environmental strain Microbacterium sp. BG28 (BglB-BG28) collected from gills of bream fish. The enzyme inhibited adhesion and the early stages of biofilm formation in clinical isolates of S. Enteritidis. At a concentration of 200 μg/mL, BglB-BG28 effectively reduced biofilm formation, by decreasing biofilm biomass by 50% and metabolic activity within biofilms by 80%. The enzyme reduced the formation of air-liquid biofilms ...on various surfaces, including plastic, glass and metal, as observed by fluorescence microscopy. BglB-BG28 inhibited biofilm formation in Escherichia coli, another important food pathogen that also forms cellulose-rich biofilms. Using o-NPG as substrate, the enzyme showed activity at temperatures up to 50 °C and in a pH range between 4 and 8, high tolerance to sodium chloride and glucose, and compatibility with nonionic detergents. Importantly, no toxicity was observed in the model system Caenorhabditis elegans even at an enzyme concentration of 1 mg/mL. These results suggest that the β-glucosidase BglB-BG28 is a promising candidate for the development of a new enzyme-based disinfection protocol that can be used in food processing facilities.
Keywords:
Biofilm / Cellulose / Food-contact surface / Foodborne pathogen / Glycoside hydrolaseSource:
Food Bioscience, 2024, 57, 103543-Publisher:
- Elsevier
Note:
- This is the peer reviewed version of the paper: Atanaskovic, M., Moric, I., Rokic, M. B., Djokic, A., Pantovic, J., Despotović, D., & Senerovic, L. (2024). Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28. Food Bioscience, 57, 103543. https://doi.org/10.1016/j.fbio.2023.103543
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https://www.sciencedirect.com/science/article/pii/S221242922301194Xhttps://imagine.imgge.bg.ac.rs/handle/123456789/2331
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Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Atanasković, Marija AU - Morić, Ivana AU - Rokić, Miloš AU - Đokić, Anđela AU - Pantović, Jelena AU - Despotović, Dragana AU - Šenerović, Lidija PY - 2024 UR - https://www.sciencedirect.com/science/article/pii/S221242922301194X UR - https://imagine.imgge.bg.ac.rs/handle/123456789/2331 AB - SalmonellaEnteritidis is the most commonly reported pathogen for foodborne illness outbreaks in both underdeveloped and developed regions. S. Enteritidis biofilms, which form on various food contact surfaces, are resistant to conventional physical and chemical cleaning and disinfection procedures routinely used in food processing. The aim of this study was to identify novel, industrially applicable enzymes that are active against S. Enteritidis biofilms. We describe the properties and anti-biofilm activity of heterologously expressed β-glucosidase B derived from the environmental strain Microbacterium sp. BG28 (BglB-BG28) collected from gills of bream fish. The enzyme inhibited adhesion and the early stages of biofilm formation in clinical isolates of S. Enteritidis. At a concentration of 200 μg/mL, BglB-BG28 effectively reduced biofilm formation, by decreasing biofilm biomass by 50% and metabolic activity within biofilms by 80%. The enzyme reduced the formation of air-liquid biofilms on various surfaces, including plastic, glass and metal, as observed by fluorescence microscopy. BglB-BG28 inhibited biofilm formation in Escherichia coli, another important food pathogen that also forms cellulose-rich biofilms. Using o-NPG as substrate, the enzyme showed activity at temperatures up to 50 °C and in a pH range between 4 and 8, high tolerance to sodium chloride and glucose, and compatibility with nonionic detergents. Importantly, no toxicity was observed in the model system Caenorhabditis elegans even at an enzyme concentration of 1 mg/mL. These results suggest that the β-glucosidase BglB-BG28 is a promising candidate for the development of a new enzyme-based disinfection protocol that can be used in food processing facilities. PB - Elsevier T2 - Food Bioscience T2 - Food BioscienceFood Bioscience T1 - Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28 SP - 103543 VL - 57 DO - 10.1016/j.fbio.2023.103543 ER -
@article{ author = "Atanasković, Marija and Morić, Ivana and Rokić, Miloš and Đokić, Anđela and Pantović, Jelena and Despotović, Dragana and Šenerović, Lidija", year = "2024", abstract = "SalmonellaEnteritidis is the most commonly reported pathogen for foodborne illness outbreaks in both underdeveloped and developed regions. S. Enteritidis biofilms, which form on various food contact surfaces, are resistant to conventional physical and chemical cleaning and disinfection procedures routinely used in food processing. The aim of this study was to identify novel, industrially applicable enzymes that are active against S. Enteritidis biofilms. We describe the properties and anti-biofilm activity of heterologously expressed β-glucosidase B derived from the environmental strain Microbacterium sp. BG28 (BglB-BG28) collected from gills of bream fish. The enzyme inhibited adhesion and the early stages of biofilm formation in clinical isolates of S. Enteritidis. At a concentration of 200 μg/mL, BglB-BG28 effectively reduced biofilm formation, by decreasing biofilm biomass by 50% and metabolic activity within biofilms by 80%. The enzyme reduced the formation of air-liquid biofilms on various surfaces, including plastic, glass and metal, as observed by fluorescence microscopy. BglB-BG28 inhibited biofilm formation in Escherichia coli, another important food pathogen that also forms cellulose-rich biofilms. Using o-NPG as substrate, the enzyme showed activity at temperatures up to 50 °C and in a pH range between 4 and 8, high tolerance to sodium chloride and glucose, and compatibility with nonionic detergents. Importantly, no toxicity was observed in the model system Caenorhabditis elegans even at an enzyme concentration of 1 mg/mL. These results suggest that the β-glucosidase BglB-BG28 is a promising candidate for the development of a new enzyme-based disinfection protocol that can be used in food processing facilities.", publisher = "Elsevier", journal = "Food Bioscience, Food BioscienceFood Bioscience", title = "Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28", pages = "103543", volume = "57", doi = "10.1016/j.fbio.2023.103543" }
Atanasković, M., Morić, I., Rokić, M., Đokić, A., Pantović, J., Despotović, D.,& Šenerović, L.. (2024). Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28. in Food Bioscience Elsevier., 57, 103543. https://doi.org/10.1016/j.fbio.2023.103543
Atanasković M, Morić I, Rokić M, Đokić A, Pantović J, Despotović D, Šenerović L. Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28. in Food Bioscience. 2024;57:103543. doi:10.1016/j.fbio.2023.103543 .
Atanasković, Marija, Morić, Ivana, Rokić, Miloš, Đokić, Anđela, Pantović, Jelena, Despotović, Dragana, Šenerović, Lidija, "Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28" in Food Bioscience, 57 (2024):103543, https://doi.org/10.1016/j.fbio.2023.103543 . .