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Heme-dependent catalase activity of lactobacilli
1Universität Hohenheim, Institut für Lebensmitteltechnologie, Stuttgart, F.R.G.
International Journal of Food Microbiology
|February 1, 1991
Summary
Heme-dependent catalase production in Lactobacillus and Enterococcus species is influenced by hematin availability and growth phase. Hematin enhances growth yields by protecting cells from endogenous hydrogen peroxide.
Area of Science:
- Microbiology
- Enzymology
- Biochemistry
Background:
- Catalases are crucial enzymes for detoxifying reactive oxygen species.
- Heme-dependent catalases play a significant role in microbial survival under oxidative stress.
- Lactobacillus and Enterococcus species are important in food and human health.
Purpose of the Study:
- To investigate the production and regulation of heme-dependent catalase in Lactobacillus pentosus, Lactobacillus sake, Lactobacillus delbrueckii, and Enterococcus faecalis.
- To determine the optimal conditions for catalase expression.
- To elucidate the physiological role of catalase in L. sake growth.
Main Methods:
- Bacterial cultures grown aerobically with and without hematin.
- Enzyme activity assays to measure catalase production.
- Growth curve analysis to assess growth yields.
- Hydrogen peroxide challenge tests.
Main Results:
- Catalase production was observed in L. pentosus, L. sake, L. delbrueckii, and E. faecalis.
- Hematin addition or incubation induced catalase formation in lactobacilli.
- Peak catalase activity occurred at late stationary phase for L. pentosus and late logarithmic phase for E. faecalis.
- Hematin supplementation increased growth yields in L. sake by protecting against 4.6 mmol/l endogenous hydrogen peroxide.
Conclusions:
- Heme-dependent catalase expression is regulated by hematin availability and growth phase in these bacteria.
- Catalase plays a protective role against endogenous hydrogen peroxide, enhancing growth yields in L. sake.
- Understanding catalase function is vital for microbial physiology and potential biotechnological applications.