Pantović, Jelena

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orcid::0000-0002-5948-3225
  • Pantović, Jelena (2)
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Author's Bibliography

GLYCOSIDE HYDROLASES FROM FRESHWATER FISH GILL MICROBIOTA AS BIOFILM INHIBITORS FOR ENHANCED FOOD SAFETY

Atanasković, Marija; Morić, Ivana; B. Rokić, Miloš; Đokić, Anđela; Pantović, Jelena; Despotović, Dragana; Šenerović, Lidija

(Serbian Society for Microbiology, 2024)

TY  - CONF
AU  - Atanasković, Marija
AU  - Morić, Ivana
AU  - B. Rokić, Miloš
AU  - Đokić, Anđela
AU  - Pantović, Jelena
AU  - Despotović, Dragana
AU  - Šenerović, Lidija
PY  - 2024
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2369
AB  - The formation of biofilms by foodborne pathogens
is a constant challenge in the food industry,
leading to an increased risk of contamination and
compromising food safety. Many of the chemicals
commonly used for sanitation in the food industry
are unable to remove biofilms, are harmful
to surfaces and can be toxic. The effectiveness
of disinfectants can be improved using enzymes
that specifically target biofilm components such
as exopolysaccharides, extracellular DNA, or proteins.
In this study we investigated the potential
of glycoside hydrolases originating from the
gill microbiota of freshwater fish to control biofilm
formation in the most common foodborne
pathogens. We demonstrated that β-glucosidase
from Microbacterium sp. BG28 (BglB-BG28) effectively
inhibits cellulose-rich biofilms formed by
Salmonella enteritidis, S. typhimurium, S. infantis,
and Escherichia coli. When these bacteria were cultivated overnight with 200 μL/mL enzyme, up
to 80% less biofilm was formed. By fluorescence
microscopy, we visualised the inhibition of biofilms
on plastic, glass and aluminium, materials
commonly used in the food industry. When used
as a pre-treatment, BglB-BG28 increased the
bactericidal efficacy of Oxicid®S, a commercially
available surface disinfectant. Its effectiveness at
temperatures up to 50 °C and in a pH range from
4 to 8 together with compatibility with non-ionic
detergents and high tolerance to sodium chloride
and glucose give BglB-BG28 advantages in
harsh and diverse industrial environments. Importantly,
no toxicity to Caenorhabditis elegans
was observed at enzyme concentrations of up
to 1 mg/ml. Overall, these results demonstrate
the suitability of the β-glucosidase BglB-BG28 for
the formulation of a novel enzyme-based disinfectant
to be used in food processing facilities.
PB  - Serbian Society for Microbiology
C3  - XIII Congress of microbiologists of Serbia: From biotechnology to human and planetary health
T1  - GLYCOSIDE HYDROLASES FROM FRESHWATER FISH GILL MICROBIOTA AS BIOFILM INHIBITORS FOR ENHANCED FOOD SAFETY
EP  - 42
SP  - 42
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2369
ER  - 
@conference{
author = "Atanasković, Marija and Morić, Ivana and B. Rokić, Miloš and Đokić, Anđela and Pantović, Jelena and Despotović, Dragana and Šenerović, Lidija",
year = "2024",
abstract = "The formation of biofilms by foodborne pathogens
is a constant challenge in the food industry,
leading to an increased risk of contamination and
compromising food safety. Many of the chemicals
commonly used for sanitation in the food industry
are unable to remove biofilms, are harmful
to surfaces and can be toxic. The effectiveness
of disinfectants can be improved using enzymes
that specifically target biofilm components such
as exopolysaccharides, extracellular DNA, or proteins.
In this study we investigated the potential
of glycoside hydrolases originating from the
gill microbiota of freshwater fish to control biofilm
formation in the most common foodborne
pathogens. We demonstrated that β-glucosidase
from Microbacterium sp. BG28 (BglB-BG28) effectively
inhibits cellulose-rich biofilms formed by
Salmonella enteritidis, S. typhimurium, S. infantis,
and Escherichia coli. When these bacteria were cultivated overnight with 200 μL/mL enzyme, up
to 80% less biofilm was formed. By fluorescence
microscopy, we visualised the inhibition of biofilms
on plastic, glass and aluminium, materials
commonly used in the food industry. When used
as a pre-treatment, BglB-BG28 increased the
bactericidal efficacy of Oxicid®S, a commercially
available surface disinfectant. Its effectiveness at
temperatures up to 50 °C and in a pH range from
4 to 8 together with compatibility with non-ionic
detergents and high tolerance to sodium chloride
and glucose give BglB-BG28 advantages in
harsh and diverse industrial environments. Importantly,
no toxicity to Caenorhabditis elegans
was observed at enzyme concentrations of up
to 1 mg/ml. Overall, these results demonstrate
the suitability of the β-glucosidase BglB-BG28 for
the formulation of a novel enzyme-based disinfectant
to be used in food processing facilities.",
publisher = "Serbian Society for Microbiology",
journal = "XIII Congress of microbiologists of Serbia: From biotechnology to human and planetary health",
title = "GLYCOSIDE HYDROLASES FROM FRESHWATER FISH GILL MICROBIOTA AS BIOFILM INHIBITORS FOR ENHANCED FOOD SAFETY",
pages = "42-42",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2369"
}
Atanasković, M., Morić, I., B. Rokić, M., Đokić, A., Pantović, J., Despotović, D.,& Šenerović, L.. (2024). GLYCOSIDE HYDROLASES FROM FRESHWATER FISH GILL MICROBIOTA AS BIOFILM INHIBITORS FOR ENHANCED FOOD SAFETY. in XIII Congress of microbiologists of Serbia: From biotechnology to human and planetary health
Serbian Society for Microbiology., 42-42.
https://hdl.handle.net/21.15107/rcub_imagine_2369
Atanasković M, Morić I, B. Rokić M, Đokić A, Pantović J, Despotović D, Šenerović L. GLYCOSIDE HYDROLASES FROM FRESHWATER FISH GILL MICROBIOTA AS BIOFILM INHIBITORS FOR ENHANCED FOOD SAFETY. in XIII Congress of microbiologists of Serbia: From biotechnology to human and planetary health. 2024;:42-42.
https://hdl.handle.net/21.15107/rcub_imagine_2369 .
Atanasković, Marija, Morić, Ivana, B. Rokić, Miloš, Đokić, Anđela, Pantović, Jelena, Despotović, Dragana, Šenerović, Lidija, "GLYCOSIDE HYDROLASES FROM FRESHWATER FISH GILL MICROBIOTA AS BIOFILM INHIBITORS FOR ENHANCED FOOD SAFETY" in XIII Congress of microbiologists of Serbia: From biotechnology to human and planetary health (2024):42-42,
https://hdl.handle.net/21.15107/rcub_imagine_2369 .

Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28

Atanasković, Marija; Morić, Ivana; Rokić, Miloš; Đokić, Anđela; Pantović, Jelena; Despotović, Dragana; Šenerović, Lidija

(Elsevier, 2024)

TY  - 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 . .
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