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Asparaginase production by human clinical isolates of Vibrio succinogenes
Applied and Environmental Microbiology
|October 1, 1979
Abstract:
Three human isolates of Vibrio succinogenes produced asparaginase. Apparent Km's were 87,220, and 320 microM. The rate of glutamine hydrolysis was between 2.8 and 3.5% of the rate of asparagine hydrolysis. Asparaginase production was not induced by ammonium ions, and enzyme yields were lower than those obtained with the rumen strain.
Insights
Three human Vibrio succinogenes isolates produce asparaginase, with varying kinetic properties. Enzyme production was not induced by ammonium ions, and yields were lower compared to rumen strains.
Area of Science:
- Microbiology
- Enzymology
Background:
- Vibrio succinogenes is a bacterium found in various environments.
- Asparaginase is an enzyme with potential therapeutic applications.
Purpose of the Study:
- To characterize asparaginase production in human isolates of Vibrio succinogenes.
- To compare enzyme kinetics and production levels with other strains.
Main Methods:
- Isolation and cultivation of Vibrio succinogenes from human samples.
- Enzymatic assays to determine asparaginase activity and kinetics (Km values).
- Analysis of enzyme induction by ammonium ions and comparison of yields.
Main Results:
- All three human isolates of Vibrio succinogenes demonstrated asparaginase production.
- Apparent Km values for asparaginase ranged from 87 to 320 microM.
- Glutamine hydrolysis rate was minimal (2.8-3.5%) compared to asparagine hydrolysis.
- Asparaginase production was not induced by ammonium ions.
- Enzyme yields were lower than those reported for rumen strains.
Conclusions:
- Human isolates of Vibrio succinogenes possess asparaginase activity with distinct kinetic parameters.
- Factors influencing enzyme production, such as ammonium ions, do not appear to be significant in these isolates.
- Further research may be needed to optimize asparaginase production from these strains for potential applications.