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Amidase activity of some bacteria
Folia Microbiologica
|January 1, 1976
Summary
Bacterial amidase activity mirrors nitrilase activity across diverse taxonomic groups, though it is more limited. This enzyme does not hydrolyze internal or vinyl-bound amides.
Area of Science:
- Microbiology
- Enzymology
Background:
- Bacteria exhibit diverse enzymatic activities, including nitrilase and amidase.
- Understanding the relationship between these activities is crucial for microbial biochemistry.
Purpose of the Study:
- To investigate and compare the spectrum of amidase activity in bacteria with high nitrilase activity.
- To determine the substrate specificity of bacterial amidases.
Main Methods:
- Enzyme assays were performed on bacterial isolates from various taxonomic groups (Bacillus, Bacteridium, Micrococcus, Brevibacterium).
- The substrate specificity of the amidase activity was characterized.
Main Results:
- The amidase activity spectrum was consistent across different bacterial genera possessing high nitrilase activity.
- Bacterial amidase activity, while broad, was found to be more restricted than nitrilase activity.
- Internal amides and vinyl-bound amides were not hydrolyzed by the tested amidases.
Conclusions:
- A conserved pattern of amidase activity exists in bacteria with high nitrilase activity, irrespective of taxonomic classification.
- Bacterial amidases exhibit specific substrate limitations, excluding internal and vinyl-bound amides.