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Respiratory activity in Listeria monocytogenes
R A Patchett1, A F Kelly, R G Kroll
1Department of Microbiology, AFRC Institute of Food Research, Reading Laboratory, Shinfield, U.K.
FEMS Microbiology Letters
|February 1, 1991
Summary
Listeria monocytogenes exhibits glucose oxidase and NADH oxidase activities. The latter is membrane-associated, indicating a respiratory chain in this bacterium.
Area of Science:
- Microbiology
- Bacterial Physiology
Background:
- Listeria monocytogenes is a significant foodborne pathogen.
- Understanding its metabolic pathways is crucial for control strategies.
Purpose of the Study:
- To investigate the enzymatic activities of Listeria monocytogenes.
- To identify potential components of its respiratory system.
Main Methods:
- Enzyme assays were performed on whole cells and lysed protoplasts.
- Activity localization was determined through membrane fractionation.
- Inhibition studies used specific respiratory inhibitors.
Main Results:
- Glucose oxidase activity was detected in whole cells.
- NADH oxidase activity was found in lysed protoplasts and associated with the membrane fraction.
- This NADH oxidase activity was sensitive to rotenone, 2-heptyl-4-hydroxy-quinoline-N-oxide, and cyanide.
Conclusions:
- Listeria monocytogenes possesses both glucose oxidase and membrane-bound NADH oxidase.
- The inhibition patterns suggest a functional, membrane-associated respiratory chain in this bacterium.