55701-05-8Relevant articles and documents
Biodegradation of β-Cyfluthrin by Fungi
Saikia, Nirmali,Gopal, Madhuban
, p. 1220 - 1223 (2004)
Five fungal species, namely, Trichoderma viride strain 5-2, T. viride strain 2211, Aspergillus niger, A. terricola, and Phanerochaete chrysoporium were screened for degradation study of β-cyfluthrin. Each fungal species was allowed to grow in Czapek dox medium containing β-cyfluthrin (5 mg/mL) as the major carbon source of the medium. The highest degradation of β-cyfluthrin was observed by T. viride 5-2 (T1/2 = 7.07 days), followed by T. viride 2211 (T1/2 = 10.66 days). The degradation of β-cyfluthrin followed first-order kinetics with a fast degradation rate during first 7 days of growth of the fungi. In the case of T. viride strain 5-2, five degradation products were isolated after 20 days of growth of the fungi, out of which three products were identified as α -cyano-4-fluorobenzyl-3-(2,2-dichlorovinyl)-2,2-dimethyl cyclopropane carboxylate, α-cyano-4-fluoro-3-phenoxy benzyl alcohol, and 3(2,2-dichlorovinyl)-2,2-dimethyl cyclopropanoic acid.
Synthesis method of DV-chrysanthemic acid
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Paragraph 0022, (2021/04/26)
The invention provides a synthesis method of DV-chrysanthemic acid. The synthesis method comprises the steps of firstly, heating isopentenol and ethyltrivinyl under an acidic condition to synthesize an intermediate dimethyl-pentenoic acid ethyl ester; secondly, adding carbon tetrachloride, isopropanol and aluminum trichloride, mixing, and cooling for reaction to obtain methyl dichlorochrysanthemate; and finally, hydrolyzing and distilling under reduced pressure to remove the organic solvent to obtain the product 3-(2,2-dichloroethyenyl)-2,2-dimethylcyclopropanecarboxylic acid. The product 3-(2,2-dichloroethyenyl)-2,2-dimethylcyclopropanecarboxylic acid is obtained through a three-step reaction, and the preparation method has the advantages of small side reaction, safety, environmental protection, suitableness for large-batch industrial production, and wide application prospect.
Characterization of a novel thermophilic pyrethroid-hydrolyzing carboxylesterase from Sulfolobus tokodaii into a new family
Wei, Tao,Feng, Shengxue,Shen, Yulong,He, Peixin,Ma, Geli,Yu, Xuan,Zhang, Fei,Mao, Duobin
, p. 225 - 232 (2013/10/21)
A novel gene ST2026 encoding a putative carboxylesterase from the thermophilic crenarchaeota Sulfolobus tokodaii (named EstSt7) was cloned and functionally overexpressed in Escherichia coli. The recombinant enzyme was purified to homogeneity after heat treatment, Ni-NTA affinity and Superdex-200 gel filtration chromatography. EstSt7 showed maximum activity at 80 C over 30 min and had a half-life of 180 min at 90 C. Its enzymatic activity was stable in the pH range of 8.0-10.0 with an optimum at 9.0. The enzyme exhibited significant esterase activity toward various p-nitrophenyl esters and the most preferable substrate was p-nitrophenyl butyrate (kcat/Km of 246.3 s-1 mM-1). In addition, EstSt7 showed high activity and stability against organic solvents (20% and 50% v/v) and detergents (1% and 5% v/v). Furthermore, EstSt7 could efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation. Sequence alignment, phylogenetic analysis and comparison of the conserved motif reveal that this novel carboxylesterase EstSt7 should be grouped into a new bacterial lipase and esterase family.
Stereoselective biotransformation of permethrin to estrogenic metabolites in fish
Nillos, Mae Grace,Chajkowski, Sarah,Rimoldi, John M.,Gan, Jay,Lavado, Ramon,Schlenk, Daniel
experimental part, p. 1568 - 1575 (2011/03/19)
This study investigated the stereoselective biotransformation and resulting estrogenic activity of the pyrethroid insecticide, permethrin (PM). Results of both in vivo (male Japanese medaka, vitellogenin (VTG) protein in plasma) and in vitro (primary rainbow trout hepatocyte VTG-mRNA expression) assays indicated stereoselective estrogenic activity of PM. 1S-cis-PM was observed to have significantly higher activity (P ≤ 0.05) than the 1R-cis enantiomer in both in vivo and in vitro evaluations. All enantiomers of PM were oxidized to a 4′-hydoxy PM (4OH PM) metabolite and underwent esterase cleavage to 3-phenoxybenzyl alcohol (3-PBOH) and 3-(4′-hydroxyphenoxy)-benzyl alcohol) (3,4′-PBOH). Racemic 4OH PM as well as 3-PBOH, and 3,4′-PBOH possessed significant (P ≤ 0.05) estrogenicity. 1S-trans-PM underwent esterase cleavage more extensively than the corresponding 1R-trans-PM. Inhibition studies with ketoconazole confirmed cytochrome P450-catalyzed hydroxylation as well as esterase cleavage of PM for all stereoisomers. These studies indicated stereoselectivity in the estrogenic activity of PM resulting from stereoselective biotransformation of the parent compound to more estrogenic metabolites.
Molecular cloning, purification, and biochemical characterization of a novel pyrethroid-hydrolyzing esterase from Klebsiella sp. strain ZD112
Wu, Pei C.,Liu, Yu H.,Wang, Zhuo Y.,Zhang, Xiao Y.,Li, He,Liang, Wei Q.,Luo, Na,Hu, Ji M.,Lu, Jia Q.,Luan, Tian G.,Cao, Li X.
, p. 836 - 842 (2007/10/03)
The gene encoding pyrethroid-hydrolyzing esterase (EstP) from Klebsiella sp. strain ZD112 was cloned into Escherichia coli and sequenced. A sequence analysis of the DNA responsible for the esfP gene revealed an open reading frame of 1914 bp encoding for a protein of 637 amino acid residues. No similarities were found by a database homology search using the nucleotide and deduced amino acid sequences of the esterases and lipases. EstP was heterologously expressed in E. coli and purified. The molecular mass of the native enzyme was approximately 73 kDa as determined by gel filtration. The results of sodium dodecyl sulfate - polyacrylamide gel electrophoresis and the deduced amino acid sequence of EstP indicated molecular masses of 73 and 73.5 kDa, respectively, suggesting that EstP is a monomer. The purified EstP not only degraded many pyrethroid pesticides and the organophosphorus insecticide malathion, but also hydrolyzed ρ-nitrophenyl esters of various fatty acids, indicating that EstP is an esterase with broad substrates. The Km for trans- and cis-permethrin and kcat/Km values indicate that EstP hydrolyzes both these substrates with higher efficiency than the carboxylesterases from resistant insects and mammals. The catalytic activity of EstP was strongly inhibited by Hg2+, Ag+, and ρ-chloromercuribenzoate, whereas a less pronounced effect (3-8% inhibition) was observed in the presence of divalent cations, the chelating agent EDTA, and phenanthroline.
Purification and characterization of a novel pyrethroid hydrolase from Aspergillus niger ZD11
Liang, Wei Q.,Wang, Zhuo Y.,Li, He,Wu, Pei C.,Hu, Ji M.,Luo, Na,Cao, Li X.,Liu, Yu H.
, p. 7415 - 7420 (2007/10/03)
The pyrethroid pesticides residues on foods and environmental contamination are a public safety concern. Pretreatment with pyrethroid hydrolase has the potential to alleviate the conditions. For this purpose, a fungus capable of using pyrethroid pesticides as a sole carbon source was isolated from the soil and characterized as Aspergillus niger ZD11. A novel pyrethroid hydrolase from cell extract was purified 41.5-fold to apparent homogeneity with 12.6% overall recovery. It is a monomeric structure with a molecular mass of 56 kDa, a pl of 5.4, and the enzyme activity was optimal at 45°C and pH 6.5. The activities were strongly inhibited by Hg2+, Ag+, and p-chloromercuribenzoate, whereas less pronounced effects (5-10% inhibition) were observed in the presence of the remaining divalent cations, the chelating agent EDTA and phenanthroline. The purified enzyme hydrolyzed various insecticides with similar carboxylester. trans-Permethrin is the preferred substrate.
Development of pyrethroid substrates for esterases associated with pyrethroid resistance in the tobacco budworm, Heliothis virescens (F.)
Huang, Huazhang,Ottea, James A.
, p. 6539 - 6545 (2007/10/03)
Assays to detect esterases associated with resistance to organophosphorus and pyrethroid insecticides in larvae of H. virescens were developed and evaluated. Cross-resistance to a variety of insecticides was measured in strains resulting from selection with either profenofos (OP-R) or cypermethrin (PYR-R), and resistance in both strains appeared to have a metabolic component. Esters were synthesized that coupled 3-(2,2-dichlorovinyl)-2,2- dimethylcyclopropanecarboxylate, the acid moiety of some pyrethroid insecticides, with groups (e.g., p-nitrophenyl-) that could be detected spectrophotometrically following hydrolysis of the resulting esters. Activities toward these pyrethroid esters were significantly higher in both resistant strains than those in a susceptible reference strain. In addition, all pyrethroid esters significantly increased the toxicity of cypermethrin in bioassays with larvae from both PYR-R and OP-R strains. The biological and biochemical activities of these compounds are compared with those with more conventional esterase substrates and insecticide synergists, and the utility of pyrethroid esters as components of rapid assays for detecting esterases associated with insecticide resistance is discussed.
Process for racemizing optically active vinyl-substituted cyclopropanecarboxylic acid compound
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, (2008/06/13)
There is disclosed a process for the racemization of a vinyl-substituted cyclopropanecarboxylic acid or a derivative thereof, which is characterized by reacting an optically active vinyl-substituted cyclopropanecarboxylic acid compound of formula (1): 1wherein R1, R2, R3 and R4 each independently represent a hydrogen atom, a halogen atom, alkyl which may be substituted having 1-4 carbon atoms, aryl which may be substituted, or alkoxycarbonyl which may be substituted, or R1 and R2 are bonded to form an alkylene group, which may be substituted; and wherein X represents hydroxyl, a halogen atom, alkoxy which may be substituted having 1-20 carbon atoms, or aryloxy which may be substituted, with a nitric compound or a nitrogen oxide.
Free radical addition of haloalkanes to polymer bound olefins and its application to the solid-phase synthesis of pyrethroids
Kumar,Chakravarthy, P.Pawan,Shesha Rao,Reddy, P.Sunder Ram,Yadav
, p. 7817 - 7819 (2007/10/03)
Polymer bound olefins undergo free radical initiated 1,2-addition when reacted with a variety of haloalkanes. The strategy could be applied successfully to the solid-phase synthesis of dihaloethenylcyclopropane carboxylic acids which are the key fragments of synthetic pyrethroids.
