Herbicide Residues, Separation and Colorimetric Determination of Monuron and Diuron Residues

Pease, Harlan L.

doi:10.1021/jf60122a003

Cited by 46 publications

(19 citation statements)

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“…Both 3-chloroaniline and chloride ion determinations were made daily. The 3-chloroaniline content of the perfusate was determined according to the procedure of Pease (1962); chloride ion determinations were made by the procedure of Iwasaki, Utsumi, and Ozawa (1952). After the initial lag phase and degradation period, a second application of the chemical was made to the perfused soils.…”

Section: Methodsmentioning

confidence: 99%

Microbial Degradation of Isopropyl-N-3-Chlorophenylcarbamate and 2-Chloroethyl-N-3-Chlorophenylcarbamate

Kaufman

Kearney

1965

Applied Microbiology

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KEARNEY. Microbial degradation of isopropyl-N-3-chlorophenylcarbamate and 2-chloroethyl-N-3-chlorophenylcarbamate. Appl Microbiol. 13:443-446. 1965.-Microbial degradation of isopropyl-N-3-chlorophenylcarbamate (CIPC) and 2-chloroethyl-N-3chlorophenylcarbamate (CEPC) was observed in a soil perfusion system. Degradation in perfused soils, and by pure cultures of effective bacterial isolates, was demonstrated by the production of 3-chloroaniline and the subsequent liberation of free chloride ion. Identified isolates effective in degrading and utilizing CIPC as a sole source of carbon included Pseudomonas striata Chester, a Flavobacterium sp., an Agrobacterium sp., and an Achromobacter sp. Identified isolates, effective in degrading and utilizing CEPC as a sole source of carbon, included an Achromobacter sp. and an Arthrobacter sp. CIPCeffective isolates degraded CEPC more slowly than CIPC, whereas CEPC-effective isolates degraded CIPC more rapidly than CEPC. Both CIPCand CEPC-effective isolates degraded isopropyl N-phenylcarbamate (IPC) more rapidly than either CIPC or CEPC.

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Section: Methodsmentioning

confidence: 99%

Microbial Degradation of Isopropyl-N-3-Chlorophenylcarbamate and 2-Chloroethyl-N-3-Chlorophenylcarbamate

Kaufman

Kearney

1965

Applied Microbiology

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“…Both PCMC and carbaryl proved to be strong inhibitors of the propanil hydrolyzing enzyme (Table 11). The reaction was terminated by the addition of the reagents necessary for DCA determination (Pease, 1962). insecticide under current investigation for use in rice soil, was not a strong inhibitor of this enzyme system. The reaction was terminated by the addition of the reagents necessary for DCA determination (Pease, 1962). insecticide under current investigation for use in rice soil, was not a strong inhibitor of this enzyme system.…”

Section: Results a N D Discussionmentioning

confidence: 99%

Methylcarbamates effect acylanilide herbicide residues in soil

Kaufman¹,

Blake²,

Miller³

1971

J. Agric. Food Chem.

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“…Protein purity was assessed by means of 10% SDS-PAGE and Lumitein Protein gel staining (Biotium). To assess the linuron amidohydrolase activity of the different fractions at each purification step, first the production of DCA from linuron was measured using a colorimetric assay consisting of a diazotization-coupling reaction that detects DCA and measurement of absorption at 500 nm according to the method of Pease (7). Then, the activity was checked and quantified by monitoring the degradation of linuron and production of DCA by HPLC as described above.…”

Section: Methodsmentioning

confidence: 99%

HylA, an Alternative Hydrolase for Initiation of Catabolism of the Phenylurea Herbicide Linuron in Variovorax sp. Strains

Bers

Batisson

Proost

et al. 2013

Appl Environ Microbiol

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f Variovorax sp. strain WDL1, which mineralizes the phenylurea herbicide linuron, expresses a novel linuron-hydrolyzing enzyme, HylA, that converts linuron to 3,4-dichloroaniline (DCA). The enzyme is distinct from the linuron hydrolase LibA enzyme recently identified in other linuron-mineralizing Variovorax strains and from phenylurea-hydrolyzing enzymes (PuhA, PuhB) found in Gram-positive bacteria. The dimeric enzyme belongs to a separate family of hydrolases and differs in K m , temperature optimum, and phenylurea herbicide substrate range. Within the metal-dependent amidohydrolase superfamily, HylA and PuhA/PuhB belong to two distinct protein families, while LibA is a member of the unrelated amidase signature family. The hylA gene was identified in a draft genome sequence of strain WDL1. The involvement of hylA in linuron degradation by strain WDL1 is inferred from its absence in spontaneous WDL1 mutants defective in linuron hydrolysis and its presence in linuron-degrading Variovorax strains that lack libA. In strain WDL1, the hylA gene is combined with catabolic gene modules encoding the downstream pathways for DCA degradation, which are very similar to those present in Variovorax sp. SRS16, which contains libA. Our results show that the expansion of a DCA catabolic pathway toward linuron degradation in Variovorax can involve different but isofunctional linuron hydrolysis genes encoding proteins that belong to evolutionary unrelated hydrolase families. This may be explained by divergent evolution and the independent acquisition of the corresponding genetic modules.is a phenylurea herbicide widely used in agriculture to control germinating and newly emerging grasses and broad-leafed weeds. Biodegradation contributes largely to the dissipation of linuron in the environment. Several single bacterial strains (1, 2) and consortia (3, 4) that degrade (3, 5) or even mineralize and use linuron as the sole source of carbon, nitrogen, and energy have been reported (1-4). Bacterial degradation of linuron is initiated by amide hydrolysis of linuron to 3,4-dichloroaniline (DCA) and N,O-dimethylhydroxylamine (N,O-DMHA). In the case of linuron mineralization, DCA is further converted to water and carbon dioxide (Fig. 1). Bacteria belonging to the genus Variovorax appear to play a crucial role in linuron biodegradation. In linuron-degrading consortia, they are almost always responsible for at least the initial hydrolysis step in linuron degradation, and most linuron-mineralizing single-strain isolates are of the genus Variovorax (1, 2). The genetic basis of linuron degradation in the linuron-mineralizing Variovorax sp. strain SRS16 was recently elucidated (6) and involves three major catabolic gene modules. In strain SRS16, conversion of linuron to DCA is catalyzed by the hydrolase LibA, encoded by the libA gene. Further mineralization of DCA involves a multicomponent dioxygenase complex encoded by dcaQTA 1 A 2 BR, which degrades DCA to a chlorocatechol intermediate. The latter is further degraded by a modified ortho-cleava...

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Herbicide Residues, Separation and Colorimetric Determination of Monuron and Diuron Residues

Cited by 46 publications

References 0 publications

Microbial Degradation of Isopropyl-N-3-Chlorophenylcarbamate and 2-Chloroethyl-N-3-Chlorophenylcarbamate

Microbial Degradation of Isopropyl-N-3-Chlorophenylcarbamate and 2-Chloroethyl-N-3-Chlorophenylcarbamate

Methylcarbamates effect acylanilide herbicide residues in soil

HylA, an Alternative Hydrolase for Initiation of Catabolism of the Phenylurea Herbicide Linuron in Variovorax sp. Strains

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