39515-47-4

Usage

Uses

Used in Pest Control Industry:
3-PHENOXYBENZALDEHYDE CYANOHYDRIN, 70 WT% SOLUTION IN ETHER is used as an intermediate in the synthesis of τ-Fluvalinate (F601100) for controlling Varroa jacobsoni, a parasitic mite that poses a significant threat to honey bee colonies. The solution plays a crucial role in the development of effective pest control measures to protect the health and sustainability of honey bee populations.

InChI:InChI=1/C14H11NO2/c15-10-14(16)11-5-4-8-13(9-11)17-12-6-2-1-3-7-12/h1-9,14,16H

Upstream product

• 113301-28-3 O-acetyl-(S)-2-hydroxy-2-(3-phenoxyphenyl)acetonitrile 
• 82129-02-0 2-(3-phenoxyphenyl)-2-[(trimethylsilyl)oxy]acetonitrile 
• 151-50-8 potassium cyanide 
• 39515-51-0 3-Phenoxybenzaldehyde 
• 52918-63-5 deltametrin 
• 52315-07-8 cypermethrine 
• 7677-24-9 trimethylsilyl cyanide 
• 6192-52-5 p-toluenesulfonic acid monohydrate 
• 71621-92-6 (1R,5S) 6,6-dimethyl-4(R)-[(S)-cyano-(3'-phenoxyphenyl)-methoxy]-3-oxa-bicyclo-(3,1,0)-hexan-2-one 
• 39515-41-8 fenpropathrin 
• 68085-85-8 α-cyano-3-phenoxybenzyl-3-(2-chloro-3,3,3-trifluoro-1-propenyl)-2,2-dimethylcyclopropanecarboxylate 
• 773837-37-9 sodium cyanide 
• 61066-87-3 alpha-cyano-3-phenoxybenzyl acetate 
• 90394-09-5 (2R,4S)-4-Methyl-2-(3-phenoxy-phenyl)-[1,3]dioxane 

Downstream Products

• 51628-48-9 3'-Phenoxy-α'-cyanobenzyl-α-ethyl-phenylacetat 
• 63402-90-4 α-(4-tolyloxy)-isovaleric acid α'-cyano-3'-phenoxybenzyl ester 
• 63439-08-7 α-(4-methoxyphenoxy)-isovaleric acid α'-cyano-3'-phenoxybenzyl ester 
• 51631-10-8 (E)-2-Isopropyl-3-methyl-pent-3-enoic acid cyano-(3-phenoxy-phenyl)-methyl ester 
• 71278-58-5 2-Methoxy-2,3,3-trimethyl-cyclopropanecarboxylic acid cyano-(3-phenoxy-phenyl)-methyl ester 
• 70459-33-5 3-Ethoxy-2,2-dimethyl-cyclopropanecarboxylic acid cyano-(3-phenoxy-phenyl)-methyl ester 
• 70459-36-8 3-Butoxy-2,2-dimethyl-cyclopropanecarboxylic acid cyano-(3-phenoxy-phenyl)-methyl ester 
• 51630-88-7 2-Cyclohex-1-enyl-3-methyl-butyric acid cyano-(3-phenoxy-phenyl)-methyl ester 
• 51715-81-2 3-Methyl-2-(3-methyl-cyclopent-2-enyl)-butyric acid cyano-(3-phenoxy-phenyl)-methyl ester 
• 71278-83-6 3-(2,2-Dichloro-ethoxy)-2,2-dimethyl-cyclopropanecarboxylic acid cyano-(3-phenoxy-phenyl)-methyl ester 
• 51628-69-4 3'-phenoxy-α'-cyanobenzyl α-isopropyl(p-ethoxyphenyl)acetate 
• 71279-41-9 2-Cyclohexyloxy-2,3,3-trimethyl-cyclopropanecarboxylic acid cyano-(3-phenoxy-phenyl)-methyl ester 
• 68085-91-6 2,2-Dimethyl-3-((E)-3,3,3-trifluoro-2-methyl-propenyl)-cyclopropanecarboxylic acid cyano-(3-phenoxy-phenyl)-methyl ester 
• 68085-97-2 3-(2-Difluoromethyl-3,3-difluoro-propenyl)-2,2-dimethyl-cyclopropanecarboxylic acid cyano-(3-phenoxy-phenyl)-methyl ester 

Relevant academic research and scientific papers

Enantioselective Autoinduction in the Asymmetric Hydrocyanation of 3-Phenoxybenzaldehyde Catalyzed by Cyclo

A new example of enantioselective autoinduction, i.e., and asymmetric reaction that is promted by a chiral catalyst into which the chiral product has been incorporated, has been found in the asymmetric hydrocyanation of 3-phenoxybenzaldehyde catalyzed by cyclo.

Asymmetric hydrocyanation of aldehydes with cyclo-dipeptides: A new mechanistic approach

A new mechanistic suggestion for the asymmetric hydrocyanation reaction of aldehydes with cyclo[-(S)-phenylalanyl-(S)-histidyl] (CPH) as catalyst is presented. Kinetic measurements indicate a second order reaction in the cyclopeptide catalyst. A heterogeneous hydrogen bonded polymer of CPH is considered to be the reactive state of the catalyst where two adjacent imidazole bases function as the reactive sites. This structural proposition is also supported by MNDO calculations performed on a dimer of CPH.

'Gelozymes' in organic synthesis: Synthesis of enantiomerically pure (S)-2-hydroxy-(3-phenoxy)phenylacetonitrile with lipase immobilised in a gelatin matrix

Lipase from Pseudomonas cepacia (Amano PS and PS Lipase, Fluka) immobilised in microemulsion-based organogels formed by gelatin solubilisation and crosslinking with glutaraldehyde ('Gelozyme') has been used for the alcoholysis of the butanoate ester of racemic 2-hydroxy-(3-phenoxy)phenylacetonitrile with 1-butanol in hexane to obtain (S)-2-hydroxy-(3-phenoxy)phenylacetonitrile. The immobilised enzyme can be used over 25 days (25 cycles) without significant loss of enzyme activity (10%). Copyright (C) 2000 Elsevier Science Ltd.

A study on increasing enzymatic stability and activity of Baliospermum montanum hydroxynitrile lyase in biocatalysis

HNL catalysis is usually carried out in a biphasic solvent and at low pH to suppress the non-enzymatic synthesis of racemic cyanohydrins. However, enzyme stability under these conditions remain a challenge. We have investigated the effect of different biocatalytic parameters, i.e., pH, temperature, buffer concentrations, presence of stabilizers, organic solvents, and chemical additives on the stability of Baliospermum montanum hydroxynitrile lyase (BmHNL). Unexpectedly, glycerol (50 mg/mL) added BmHNL biocatalysis had produced >99% of (S)-mandelonitrile from benzaldehyde, while without glycerol it is 54% ee. Similarly, BmHNL had converted 3-phenoxy benzaldehyde and 3,5-dimethoxy benzaldehyde, to their corresponding cyanohydrins in the presence of glycerol. Among the different stabilizers added to BmHNL at low pH, 400 mg/mL of sucrose had increased enzyme's half-life more than fivefold. BmHNL's stability study showed half-lives of 554, 686, and 690 h at its optimum pH 5.5, temperature 20 °C, buffer concentration, i.e., 100 mM citrate-phosphate pH 5.5. Addition of benzaldehyde as inhibitor, chemical additives, and the presence of organic solvents have decreased both the stability and activity of BmHNL, compared to their absence. Secondary structural study by CD-spectrophotometer showed that BmHNL's structure is least affected in the presence of different organic solvents and temperatures.

Immobilized Baliospermum montanum hydroxynitrile lyase catalyzed synthesis of chiral cyanohydrins

Hydroxynitrile lyase (HNL) catalyzed enantioselective C–C bond formation is an efficient approach to synthesize chiral cyanohydrins which are important building blocks in the synthesis of a number of fine chemicals, agrochemicals and pharmaceuticals. Immobilization of HNL is known to provide robustness, reusability and in some cases also enhances activity and selectivity. We optimized the preparation of immobilization of Baliospermium montanum HNL (BmHNL) by cross linking enzyme aggregate (CLEA) method and characterized it by SEM. Optimization of biocatalytic parameters was performed to obtain highest % conversion and ee of (S)-mandelonitrile from benzaldehyde using CLEA-BmHNL. The optimized reaction parameters were: 20 min of reaction time, 7 U of CLEA-BmHNL, 1.2 mM substrate, and 300 mM citrate buffer pH 4.2, that synthesized (S)-mandelonitrile in ～99% ee and ～60% conversion. Addition of organic solvent in CLEA-BmHNL biocatalysis did not improve in % ee or conversion of product unlike other CLEA-HNLs. CLEA-BmHNL could be successfully reused for eight consecutive cycles without loss of conversion or product formation and five cycles with a little loss in enantioselectivity. Eleven different chiral cyanohydrins were synthesized under optimal biocatalytic conditions in up to 99% ee and 59% conversion, however the % conversion and ee varied for different products. CLEA-BmHNL has improved the enantioselectivity of (S)-mandelonitrile synthesis compared to the use of purified BmHNL. Nine aldehydes not tested earlier with BmHNL were converted into their corresponding (S)-cyanohydrins for the first time using CLEA-BmHNL. Among the eleven (S)-cyanohydrins syntheses reported here, eight of them have not been synthesized by any CLEA-HNL. Overall, this study showed preparation, characterization of a stable, robust and recyclable biocatalyst i.e. CLEA-BmHNL and its biocatalytic application in the synthesis of different (S)-aromatic cyanohydrins.

Hydroxynitrile Lyase Isozymes from Prunus communis: Identification, Characterization and Synthetic Applications

Biocatalysts originating from Badamu (Prunus communis) have been applied to catalyze the asymmetric synthesis of (R)-4-methylsulfanylmandelonitrile, a key building block of thiamphenicol and florfenicol. Here, four hydroxynitrile lyase (HNL) isozymes from Badamu were cloned and heterologously expressed in Pichia pastoris. The biochemical properties and catalytic performances of these isozymes were comprehensively explored to evaluate their efficiency and selectivity in asymmetric synthesis. Among then, PcHNL5 was identified with outstanding activity and enantioselectivity in asymmetric hydrocyanation. Under the optimized mild biphasic reaction conditions, seventeen prochiral aromatic aldehydes were converted to valuable chiral cyanohydrins with good yields (up to 94%) and excellent optical purities (up to >99.9% ee), which provide a facile access to numerous chiral amino alcohols, hypoglycemic agents, angiotension converting enzyme (ACE) inhibitors and β-blockers. This work therefore underlines the importance of discovering the most potent biocatalyst among a group of isozymes for converting unnatural substrates into value-added products. (Figure presented.).

PYRETHROID COMPOUND, AND HAIR RESTORER AND HAIR RESTORER COMPOSITION COMPRISING THE SAME

PROBLEM TO BE SOLVED: To provide a pyrethroid compound having hair growth effect. SOLUTION: The present invention provides a pyrethroid compound represented by general formula (1) [in general formula (1), R1 is selected from a hydrogen atom, a halogen atom, an azido group, an alkoxy group having 1 to 4 carbon atoms, and an alkyl group having 1 to 4 carbon atoms, R2 is selected from a methyl group, an ethyl group and an isopropyl group, R3 is selected from -C≡N, -C≡CH, -C≡C-CH3 and -CH=CH2, and R4 is selected from a methyl group, a phenyl group, a 2-methoxy ethyl group, a methoxymethyl group, and a propargyl group]. SELECTED DRAWING: None COPYRIGHT: (C)2017,JPOandINPIT

Fast microwave-assisted resolution of (±)-cyanohydrins promoted by lipase from Candida antarctica

Enzymatic kinetic resolution (EKR) of (±)-cyanohydrins was performed by using immobilized lipase from Candida antarctica (CALB) under conventional ordinary conditions (orbital shaking) and under microwave radiation (MW). The use of microwave radiation contributed very expressively on the reduction of the reaction time from 24 to 2 h. Most importantly, high selectivity (up to 92percent eep) as well as conversion was achieved under MW radiation (50-56percent).

Fenpropathrin biodegradation pathway in bacillus sp. DG-02 and its potential for bioremediation of pyrethroid-contaminated soils

The widely used insecticide fenpropathrin in agriculture has become a public concern because of its heavy environmental contamination and toxic effects on mammals, yet little is known about the kinetic and metabolic behaviors of this pesticide. This study reports the degradation kinetics and metabolic pathway of fenpropathrin in Bacillus sp. DG-02, previously isolated from the pyrethroid-manufacturing wastewater treatment system. Up to 93.3% of 50 mg L-1 fenpropathrin was degraded by Bacillus sp. DG-02 within 72 h, and the degradation rate parameters qmax, Ks, and K i were determined to be 0.05 h-1, 9.0 mg L-1, and 694.8 mg L-1, respectively. Analysis of the degradation products by gas chromatography-mass spectrometry led to identification of seven metabolites of fenpropathrin, which suggest that fenpropathrin could be degraded first by cleavage of its carboxylester linkage and diaryl bond, followed by degradation of the aromatic ring and subsequent metabolism. In addition to degradation of fenpropathrin, this strain was also found to be capable of degrading a wide range of synthetic pyrethroids including deltamethrin, λ-cyhalothrin, β-cypermethrin, β-cyfluthrin, bifenthrin, and permethrin, which are also widely used insecticides with environmental contamination problems with the degradation process following the first-order kinetic model. Bioaugmentation of fenpropathrin-contaminated soils with strain DG-02 significantly enhanced the disappearance rate of fenpropathrin, and its half-life was sharply reduced in the soils. Taken together, these results depict the biodegradation mechanisms of fenpropathrin and also highlight the promising potentials of Bacillus sp. DG-02 in bioremediation of pyrethroid-contaminated soils.

Characterization of a novel thermophilic pyrethroid-hydrolyzing carboxylesterase from Sulfolobus tokodaii into a new family

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.