Effect of yeast extract on the degradation of organophosphorus insecticides by soil enrichment and bacterial cultures

1989 ◽  
Vol 35 (12) ◽  
pp. 1105-1110 ◽  
Author(s):  
M. Sharmila ◽  
K. Ramanand ◽  
N. Sethunathan

Soil enrichment cultures were prepared by repeated additions of methyl parathion to flooded alluvial and laterite soils incubated at 35 °C. These cultures were tested for their ability to degrade methyl parathion in a mineral salts medium in the presence and absence of yeast extract. Addition of yeast extract (0.05% w/v) accelerated the degradation of methyl parathion by both enriched cultures. Methyl parathion was degraded by the enrichment culture from alluvial soil essentially by hydrolysis in the absence of yeast extract and by nitro group reduction in its presence. The enrichment culture from laterite soil degraded methyl parathion (by hydrolysis) only in the presence of yeast extract. A Bacillus sp., isolated from laterite soil, degraded methyl parathion essentially by hydrolysis in the presence of a concentration (w/v) of yeast extract of 0.05%, by both hydrolysis and nitro group reduction at 0.1 and 0.25%, and exclusively by nitro group reduction at 0.5%. A similar trend was also noticed with parathion. However, fenitrothion was degraded by Bacillus sp. mainly by hydrolysis at all concentrations of yeast extract, whereas diazinon was not degraded.Key words: organophosphorothioates, biodegradation, yeast extract dependent pathway.

1984 ◽  
Vol 30 (12) ◽  
pp. 1458-1466 ◽  
Author(s):  
B. S. Rajagopal ◽  
V. R. Rao ◽  
G. Nagendrappa ◽  
N. Sethunathan

Metabolism of side chain and ring 14C-labelled carbaryl and carbofuran in a mineral salts medium by soil-enrichment cultures and a Bacillus sp. was studied. A change in the substrate of the medium from carbaryl to carbofuran led to a marked shift in the dominant bacterium from Bacillus sp. to Arthrobacter sp. although carbaryl-enrichment culture was the primary inoculum in both media. Hydrolysis was the major route of microbial degradation of both carbamate insecticides. During carbaryl degradation by enrichment cultures and Bacillus sp., 1-naphthol and 1,4-naphthoquinone accumulated in the medium. Of the three metabolites formed from carbofuran, 3-hydroxycarbofuran and 3-ketocarbofuran were further metabolized rapidly, while carbofuran phenol was resistant to further degradation. Evolution of 14CO2 and other gaseous 14C-labelled products from both side chain and ring labels was negligible. This and slow degradation of the hydrolysis products led to significant accumulation of 14C in the medium even after prolonged incubation.


2011 ◽  
Vol 76 (9) ◽  
pp. 3484-3497 ◽  
Author(s):  
Laura A. McAllister ◽  
Bruce M. Bechle ◽  
Amy B. Dounay ◽  
Edelweiss Evrard ◽  
Xinmin Gan ◽  
...  

Author(s):  
David S. B. Daniels ◽  
Robert Crook ◽  
Olivier Dirat ◽  
Steven J. Fussell ◽  
Adam Gymer ◽  
...  

1997 ◽  
Vol 36 (6-7) ◽  
pp. 117-124 ◽  
Author(s):  
Tae Ho Lee ◽  
Masaharu Yoshimi ◽  
Michihiko Ike ◽  
Masanori Fujita

An anaerobic soil enrichment culture could dechlorinate high concentrations of tetrachloroethylene (PCE; 150 mg/liter nominal concentration; approximately 58 mg/liter in aqueous concentration) nearly stoichiometrically to cis-1,2-dichloroethylene (cis-DCE) via trichloroethylene (TCE) at high rates; a maximum dechlorination rate was 0.4 μmol of PCE transformed/mg volatile suspended solids per hr, using citrate as an electron and carbon source and yeast extract as a nutritional requirement. This dechlorinating activity was comparable with those of the previously-reported, efficient bacterial cultures. Some substrates such as pyruvate, succinate, formate, acetate, and acetate with H2 could replace citrate but propionate could not, and yeast extract could be replaced by a vitamin mixture. However the PCE dechlorination rate decreased more than threefold by the addition of the vitamin mixture, suggesting that the vitamin mixture could not be a complete supplement for the nutritional requirement. Optimal pH and temperature of the enrichment for PCE dechlorination were 7 and 30 °C, respectively. Dechlorination of PCE was completely inhibited by the addition of NO3− and NO2− as potential alternative electron acceptors. S2O3−2 and SO3−2 delayed PCE dechlorination but SO4−2 had no significant effect on PCE reduction. 2-bromoethanesulfonic acid (BES, an inhibitor of methanogenesis) also showed no influence on PCE dechlorination, suggesting methanogens were not concerned with PCE removal in this enrichment. Further, microbial investigations on the enrichment showed that it contains four types of bacteria; cocci, large rods, curved rods, and small rods. The small rods seemed to nutritionally support the PCE dechlorinating bacteria, presumably the curved rods.


2015 ◽  
Vol 5 (1) ◽  
pp. 286-295 ◽  
Author(s):  
Puran Singh Rathore ◽  
Rajesh Patidar ◽  
T. Shripathi ◽  
Sonal Thakore

A magnetically separable core–shell iron oxide@nickel nanocatalyst was synthesized, characterized and applied for the aromatic nitro group reduction.


1999 ◽  
Vol 65 (6) ◽  
pp. 2317-2323 ◽  
Author(s):  
Andreas Schenzle ◽  
Hiltrud Lenke ◽  
Jim C. Spain ◽  
Hans-Joachim Knackmuss

ABSTRACT Ralstonia eutropha JMP134 utilizes 2-chloro-5-nitrophenol as a sole source of nitrogen, carbon, and energy. The initial steps for degradation of 2-chloro-5-nitrophenol are analogous to those of 3-nitrophenol degradation in R. eutropha JMP134. 2-Chloro-5-nitrophenol is initially reduced to 2-chloro-5-hydroxylaminophenol, which is subject to an enzymatic Bamberger rearrangement yielding 2-amino-5-chlorohydroquinone. The chlorine of 2-amino-5-chlorohydroquinone is removed by a reductive mechanism, and aminohydroquinone is formed. 2-Chloro-5-nitrophenol and 3-nitrophenol induce the expression of 3-nitrophenol nitroreductase, of 3-hydroxylaminophenol mutase, and of the dechlorinating activity. 3-Nitrophenol nitroreductase catalyzes chemoselective reduction of aromatic nitro groups to hydroxylamino groups in the presence of NADPH. 3-Nitrophenol nitroreductase is active with a variety of mono-, di-, and trinitroaromatic compounds, demonstrating a relaxed substrate specificity of the enzyme. Nitrosobenzene serves as a substrate for the enzyme and is converted faster than nitrobenzene.


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