16197-93-6

Upstream product

• 1445-91-6 (S)-1-phenylethanol 
• 108-24-7 acetic anhydride 
• 108-22-5 Isopropenyl acetate 
• 98-85-1 1-Phenylethanol 
• 93-92-5 1-phenylethyl acetate 
• 2206-94-2 1-acetoxy-1-phenylethene 
• 1528-10-5 (Z)-1-acetoxypropene 
• 71-36-3 butan-1-ol 
• 5177-66-2 1-ethoxyvinyl acetate 
• 108-05-4 vinyl acetate 
• 155095-22-0 2-acetyl-3-phenyl-l-menthopyrazole 
• 406-95-1 2,2,2-trifluoroethyl acetate 
• 141-78-6 ethyl acetate 
• 769-59-5 3-phenyl-butan-2-one 

Downstream Products

• 110744-07-5 (1'S,3S)-3-Hydroxy-3-phenylpropansaeure-(1-phenylethyl)ester 
• 110773-04-1 (1'S,3R)-3-Hydroxy-3-phenylpropansaeure-(1-phenylethyl)ester 
• 535-17-1 (S)-2-acetoxypropionic acid 
• 60492-39-9 2-(1-phenylethyl)anisole 
• 2605-18-7 1-methoxy-4-(1-phenylethyl)benzene 
• 19144-86-6 (S)-N-acetyl-1-phenylethylamine 
• 1445-91-6 (S)-1-phenylethanol 

Relevant academic research and scientific papers

PHANE-TetraPHOS, the First D2 Symmetric Chiral Tetraphosphane. Synthesis, Metal Complexation, and Application in Homogeneous Stereoselective Hydrogenation

PHANE-TetraPHOS, a new D2 symmetric tetraphosphane based on the [2.2]paracyclophane scaffold, has been synthesized and characterized. The peculiarity of this system is the presence of four homotopic diphenylphosphane groups, exchangeable through C2 symmetry operations and consequently indistinguishable. Their spatial arrangement allows the simultaneous complexation of two metal atoms. Enantiomeric purity was attained at tetra-phosphane oxide level by fractional crystallization of the diastereomeric adducts obtained from the racemate with enantiopure dibenzoyltartaric acids. Alkaline treatment of diastereomerically pure adducts followed by exhaustive P?O groups reduction with HSiCl3 gave both PHANE-TetraPHOS antipodes in an enantiopure state. They were tested as rhodium ligands in the homogeneous enantioselective hydrogenation of some benchmark unsaturated compounds. Catalytic activity and enantiodiscrimination ability were found comparable to those exhibited by the complexes of the parent bidentate ligand PHANEPHOS, but only half a mole of precious chiral ligand was employed.

Enantioselective resolution of (±)-1-phenylethyl acetate using the immobilized extracellular proteases from deep-sea Bacillus sp. DL-1

Bacillus sp. DL-1 was isolated from the deep sea of the Western Pacific Ocean and behaved very good resistance to NaCl. The extracellular proteases of Bacillus sp. DL-1 were found to exhibit excellent enantioselectivity for the kinetic resolution of (±)-1-phenylethyl acetate. To improve the stability of the enzyme, the immobilized extracellular proteases were preparated by using 60 g kieselguhr and 1-L crude fermentation broth containing extracellular proteases of Bacillus sp. DL-1, shaking at 25 °C, 200 r/min for 10 h. Every gram of kieselguhr adsorbed 25.7 mg extracellular protease and the enzymatic activity recovery was 79.86%. The immobilized proteases preserved about 35.8% of its activity after 6 repeated uses, which were also used as biocatalyst to asymmetrically hydrolyse (±)-1-phenylethyl acetate for the preparation of (R)-1-phenylethanol and (S)-1-phenylethyl acetate with high optical purities. The effects of pH, temperature, enzyme concentration, substrate concentration, reaction time and additives (metal ions/surfactants) on the resolution were investigated by single factor experiments. Under the optimal reaction conditions (10 mM (±)-1-phenylethyl acetate, 40 mg/mL immobilized extracellular proteases, pH 7.5 (Tris-HCl), 5% (v/v) methanol and 45 °C for 2 h), (R)-1-phenylethanol was generated with the e.e.p being > 97%, and the yield being 53%, respectively. Analogously, under the optimal reaction conditions (10-mM (±)-1-phenylethyl acetate, 360 mg/mL immobilized extracellular proteases, pH 6.0 (PB), 5% (v/v) DMSO and 35 °C for 1.5 h), (S)-1-phenylethyl acetate was generated with the e.e.s being over 99% and the yield being 79%, respectively. Compared with the extracellular proteases from Bacillus sp. DL-2, the immobilized extracellular proteases from Bacillus sp. DL-1 exhibited higher hydrolytic activity and could asymmetrically hydrolyse (±)-1-phenylethyl acetate by using higher substrate concentrations, shorter reaction times to obtain higher yields. Notably, the extracellular proteases of Bacillus sp. DL-1 were demonstrated to behave the same enantio-preference as those of most other reported esterases/lipases. Proteases from deep-sea Bacillus sp. DL-1 are promising biocatalysts for the synthesis of valuable chiral chemicals.

Two Approaches for CAL-B-Catalyzed Enantioselective Deacylation of a Set of α-Phenyl Ethyl Esters: Organic Solvent with Sodium Carbonate and Micro-aqueous Medium

Herein, we report an efficient enantioselective cleavage of the acyl- moiety of a set of α- phenyl ethyl esters with different chain-lengths catalyzed by lipase B from Candida antarctica (CAL-B) by comparing two reactional approaches: anhydrous media with sodium carbonates and micro-aqueous medium. The deacylation is performed in organic solvent, in the presence of Na2CO3 in the first case, and by addition of a drop of phosphate buffer solution pH 7 in the second. The results show the high efficiency of the deacylation in the presence of the sodium carbonate for the enzymatic resolution of all the esters and that in term of reactivity (31% ≤ conv ≤ 50%) and selectivity (E > 200). While, during the hydrolysis in micro-aqueous media, the conversion is strongly affected by the length of the acyl-chain side, the conversion decreases from conv = 50% with the 1-phenylethyl acetate 1a to conv = 19% with 1-phenyethyl dodecanoate 6a, and this, even if the selectivity remains high (E > 89). In both conditions, the lipase CAL-B shows a high enantioselectivities in favor of (R)-1-phenyl ethanol enantiomer (conv > 45%, E > 200) but the reactivity is modulated by the form and the size of the acyl-chain side. Graphic Abstract: [Figure not available: see fulltext.].

Pickering-Droplet-Derived MOF Microreactors for Continuous-Flow Biocatalysis with Size Selectivity

Enzymatic microarchitectures with spatially controlled reactivity, engineered molecular sieving ability, favorable interior environment, and industrial productivity show great potential in synthetic protocellular systems and practical biotechnology, but their construction remains a significant challenge. Here, we proposed a Pickering emulsion interface-directed synthesis method to fabricate such a microreactor, in which a robust and defect-free MOF layer was grown around silica emulsifier stabilized droplet surfaces. The compartmentalized interior droplets can provide a biomimetic microenvironment to host free enzymes, while the outer MOF layer secludes active species from the surroundings and endows the microreactor with size-selective permeability. Impressively, the thus-designed enzymatic microreactor exhibited excellent size selectivity and long-term stability, as demonstrated by a 1000 h continuous-flow reaction, while affording completely equal enantioselectivities to the free enzyme counterpart. Moreover, the catalytic efficiency of such enzymatic microreactors was conveniently regulated through engineering of the type or thickness of the outer MOF layer or interior environments for the enzymes, highlighting their superior customized specialties. This study provides new opportunities in designing MOF-based artificial cellular microreactors for practical applications.

Chiral ferrocene-indole diphosphine ligand as well as preparation method and application thereof

The invention relates to a chiral ferrocene-indole diphosphine ligand as well as a preparation method and application thereof. The specific preparation method comprises the following steps: dissolving an indole compound and a chiral ferrocene phosphine ac

Chiral ferrocene phosphine-indole aminophosphine ligand as well as preparation method and application thereof

The invention discloses a chiral ferrocene phosphine-indole aminophosphine ligand as well as a preparation method and application thereof. The preparation method comprises the following steps: dissolving a chiral ferrocene phosphine-indole intermediate in

PQXdpap: Helical Poly(quinoxaline-2,3-diyl)s Bearing 4-(Dipropylamino)pyridin-3-yl Pendants as Chirality-Switchable Nucleophilic Catalysts for the Kinetic Resolution of Secondary Alcohols

Helically chiral poly(quinoxaline-2,3-diyl)s bearing 4-(dipropylamino)pyridin-3-yl pendants at the 5-position of the quinoxaline ring (PQXdpap) exhibited high catalytic activities and moderate to high selectivities (up to s = 87) in the acylative kinetic resolution of secondary alcohols. The solvent-dependent helical chirality switching of PQXdpap between pure toluene and a 1:1 mixture of toluene and 1,1,2-trichloroethane enabled the preparation of either compound of a pair of enantiomerically pure alcohols (>99% ee) from a single catalyst.

Development of environmentally friendly lipase-catalysed kinetic resolution of (R,S)-1-phenylethyl acetate using aqueous natural deep eutectic solvents

Over the past decade, natural deep eutectic solvents (NADES) have become promising green solvent from both environmental and technological perspectives. The number of structural combinations encompassed by NADES is tremendous; thus, NADES with unique physicochemical properties can be designed for a particular purpose, such as for efficient biocatalytic processes. The aim of this work was to prepare several NADES based on renewable sources (biomass energy) and to apply these solvents in the industrially interesting process of lipase-catalysed (R)-1-phenylethanol synthesis. Based on experimental data on lipase behaviour in the tested NADES, choline chloride:glycerol (ChGly) was selected as the most promising solvent for the given reaction. The resulting (R)-1-phenylethanol was also successfully isolated and purified from the reaction mixture using liquid-liquid extraction with ethyl acetate, whilst ChGly was recycled and reused. (R)-1-phenylethanol and unreacted (S)-1-phenylethyl acetate were purified on silica gel columns with yields of 81.91 %. The biocatalyst was also successfully recycled and reused in 4 cycles. Based on laboratory-scale optimum conditions, (R)-1-phenylethanol synthesis performed in a 500 mL batch reactor achieved reaction conversions comparable to those obtained with millilitre-scale biocatalytic reactions. The downstream process was also performed on a preparative scale with a yield of 49.48 %.

Acylative Dynamic Kinetic Resolution of Secondary Alcohols: Tandem Catalysis by HyperBTM and B?ckvall's Ruthenium Complex

Non-enzymatic dynamic kinetic resolution (DKR) of secondary alcohols by enantioselective acylation using an isothiourea-derived HyperBTM catalyst and racemization of slowly reacting alcohol by B?ckvall's ruthenium complex is reported. The DKR approach fea

Lipase-oxovanadium heterogeneous catalysis system: a robust protocol for the dynamic kinetic resolution of sec-alcohols

Herein, we present a robust and eco-friendly dynamic kinetic resolution (DKR) protocol for secondary alcohols using a combined heterogeneous catalytic CAL?B/VOSO4 system at 50 °C in the relatively green solvent heptane. This catalytic system is