Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Goldschmidt, Millicent C.; Lockhart, Betty M.

doi:10.1128/aem.22.3.350-357.1971

Cited by 14 publications

(6 citation statements)

References 9 publications

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“…Therefore, the induction medium and the three test media described above are required for the simultaneous detection of the dihydrolase and decarboxylase systems in microorganisms. The results listed in Table 1 agree with those obtained by identifying the end products of the arginine dihydrolase enzymes and decarboxylases of arginine, lysine, and ornithine with one-dimensional TLC on cellulose plates (10,11,21,29,31,32) and with gas-liquid chromatography (15,19).…”

Section: Discussionsupporting

confidence: 82%

Rapid method for simultaneous detection of the arginine dihydrolase system and amino acid decarboxylases in microorganisms

Chen¹,

Culbertson²,

Knapp³

et al. 1982

J Clin Microbiol

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A specific procedure has been developed for the detection of the first two enzymes involved in the arginine dihydrolase system and the detection of the decarboxylases of arginine, glutamic acid, histidine, lysine, ornithine, phenylalanine, tryptophan, and tyrosine. A loopful of growth of each organism from dihydrolase-decarboxylase induction agar medium (or broth) was washed and incubated separately with 0.2-ml samples of three test media supplemented with different amino acids. Each spent test medium was dansylated, and the dansyl derivatives were separated by two-dimensional thin-layer chromatography on polyamide sheets. The end products (citrulline, ornithine, y-amino-n-butyric acid, and amines) produced during incubation were estimated by comparing the fluorescent intensities of end products from the spent test media and of the corresponding parent amino acids from test medium controls after thin-layer chromatography. The method is reproducible, requiring incubation of an organism in three test media for 1 h for simultaneous detection of the first two enzymes involved in the arginine dihydrolase system and of eight amino acid decarboxylases. This method has been successfully applied to gram-positive and gramnegative microorganisms and also to Mycoplasmatales. It could simplify and improve the accuracy of the corresponding biochemical tests performed in clinical laboratories for the identification and differentiation of microorganisms, and it may prove particularly useful for the differentiation of species of Pseudomonas and Mycoplasma. Enzymes involved in the arginine dihydrolase system and the amino acid decarboxylases are widely distributed in microorganisms (1, 2, 8). The microbial arginine dihydrolase system which converts arginine to ornithine via citrulline consists of three enzyme reactions: arginine + H20-* citrulline + NH3 by arginine deiminase; citrulline + Pi ornithine + carbamyl

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Section: Discussionsupporting

confidence: 82%

Rapid method for simultaneous detection of the arginine dihydrolase system and amino acid decarboxylases in microorganisms

Chen¹,

Culbertson²,

Knapp³

et al. 1982

J Clin Microbiol

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“…The formation of ornithine from arginine in E. coli could occur from one or more reactions including arginine dihydrolase. The limited activity observed with resting cells of Enterobacteriaceae could be due to a number of factors such as pH (1,4,6,8), cofactors (4, 6), oxygen tension (4, 6), and temperature (1, 4). The effect of these parameters on the resting cell GLC procedure is being investigated.…”

Section: Resultsmentioning

confidence: 99%

Use of Gas Chromatography for Determining Catabolic Products of Arginine by Bacteria

Moss

Lambert

Cherry

1972

Applied Microbiology

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A rapid and sensitive procedure for determining catabolic products of arginine metabolism by bacteria was developed. The method consists of inoculating a solution of L-arginine with a heavy cell suspension of the test organism. After a 2-hr incubation period, dissimilation products (citrulline, ornithine, agmatine, putrescine) are converted to volatile derivatives and analyzed by gas-liquid chromatography. Compared with conventional microbiological tests, the new procedure is rapid and can be used for sensitive quantitative measurements of specific metabolites from arginine.

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“…Nitrogen enters the human large intestine mainly in the form of proteins and peptides (6). After hydrolysis of the macromolecules by colonic proteases and peptidases, either intestinal bacteria can deaminate the amino acids to form a variety of products, including ammonia, carboxylic acids, indoles and phenols (25), or the amino acids may be decarboxylated to produce amines and CO2 (13,14,23). Amines can also be formed by N-dealkylation reactions (16), degradation of polyamines (32), or transamination of aldehydes (10).…”

mentioning

confidence: 99%

Influence of pH, nutrient availability, and growth rate on amine production by Bacteroides fragilis and Clostridium perfringens

Allison

Macfarlane

1989

Appl Environ Microbiol

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Dimethylamine, methylamine, propylamine, and pyrrolidine were the major amines formed by Bacteroides fragilis NCDO 2217 during the active phase of growth in batch culture. Production of these metabolites was strongly pH dependent and was optimal under acidic conditions (pH 6.0). Low pH also favored the formation of pyrrolidine, cadaverine, and dimethylamine by Clostridium perfringens C523, but the reverse was the case with putrescine, butylamine, and propylamine, where production was maximal at neutral pH. B. fragilis was grown in continuous culture under either starch or casein limitation. Amine formation was influenced by carbohydrate availability and was greatest when the bacteria were grown at high growth rates (dilution rate, 0.20/h) under starch limitation, where they constituted about 18% of the total fermentation products measured. Amine production was optimal and increased concomitantly with growth rate when C. perffingens was grown in glucose-limited continuous culture. Under conditions of high growth rate and glucose limitation, amines accounted for approximately 27% of the fermentation products measured. When glucose in the feed medium was increased from 5 to 15 g/liter, amine production was repressed, and under these nutritional conditions the growth rate had little effect on the process.

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Rapid Methods for Determining Decarboxylase Activity: Arginine Decarboxylase

Cited by 14 publications

References 9 publications

Rapid method for simultaneous detection of the arginine dihydrolase system and amino acid decarboxylases in microorganisms

Rapid method for simultaneous detection of the arginine dihydrolase system and amino acid decarboxylases in microorganisms

Use of Gas Chromatography for Determining Catabolic Products of Arginine by Bacteria

Influence of pH, nutrient availability, and growth rate on amine production by Bacteroides fragilis and Clostridium perfringens

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