Development of an assay method for cyanide, alpha-aminonitriles and alpha-hydroxynitriles for the study of the biological hydrolysis of these compounds.
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Colorimetry↗
Biomedical subjects
J C Jallageas
Publications and source records attributed to J C Jallageas.
[Spectrum of amidase activity in a mutant of Brevibacterium].
Brevibacterium R 312 has a fairly non-specific amidase. Following the loss of this enzyme by mutation, the following enzymatic activities could be demonstrated: hydrolysis of urea, formamide, nicotinamide, L-glutamine, glycinamide and L-alpha-amino amids.
Amidohydrolases↗
Nitrilases and amidases: determination of activity by proton magnetic resonance spectrometry.
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Amidohydrolases↗
[Use of gas-liquid chromatography for the study of nitrilases and amidases (author's transl)].
A gas-liquid chromatographic procedure is described for the determination of nitrilasic and amidasic activities. This method allows to monitor the kinetics of the hydrolysis of volatile nitriles and amides and because of its sensitivity, to determine the Michaelis constants Km of the acetonitrilase and the acetamidase of Brevibacterium R 312. For these enzymes, a correlation is shown between the kinetics monitored by proton nuclear magnetic resonance spectroscopy and gas-liquid chromatography.
Amidohydrolases↗
[Nitrilase activity in several bacteria].
Eighteen strains of Bacteria from the genus Bacillus, Bacteridium, Micrococcus and Brevibacterium were isolated. They have a very general nitrilase activity that acts on all the substrates with nitrile function.
Actinomycetales↗
Amidase activity of some bacteria.
The amidase activity of bacteria possessing a high nitrilase activity was found to display the same spectrum although the bacteria may belong to different taxonomic groups, Bacillus, Bacteridium, Micrococcus, Brevibacteriun. The spectrum of amidase activity, although very broad, is more restricted than that of nitrilase activity. Internal amides as well as vinyl-bound amides are not hydrolyzed.
Amides↗