Efficient dynamic kinetic resolution of arylamines with Pd/layered double-hydroxide-dodecyl sulfate anion for racemization

Xu, Gang; Dai, Xiaoting; Fu, Simin; Wu, Jianping; Yang, Lirong

doi:10.1016/j.tetlet.2013.11.041

Cited by 19 publications

(8 citation statements)

References 18 publications

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“…The applicability of DKR to amines is limited by the scarcity of reported efficient enzyme‐compatible racemization methods, which usually require expensive transition‐metal chemo‐catalysts (mostly Raney‐Ni,, Shvo‐type, palladium‐, or ruthenium based), expensive non‐selective reducing agents such as ammonia borane and/or harsh conditions, that are not suitable for large‐scale application or in combination with enzymatic steps. The best‐known example of a successful DKR on a laboratory scale was reported by Reetz and Schimossek in 1996.…”

Section: Introductionmentioning

confidence: 99%

Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions

Ruggieri

Langen²,

Logan

et al. 2018

ChemCatChem

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Dynamic kinetic resolution (DKR) reactions in which a stereoselective enzyme and a racemization step are coupled in one pot would represent powerful tools for the production of enantiopure amines through enantioconvergence of racemates. The exploitation of DKR strategies is currently hampered by the lack of effective, enzyme‐compatible and scalable racemization strategies for amines. In the present work, the proof of concept of a fully biocatalytic method for amine racemization is presented. Both enantiomers of the model compound 1‐methyl‐3‐phenylpropylamine could be racemized in water and at room temperature using a couple of wild‐type, non‐proprietary, enantiocomplementary amine transaminases and a minimum amount of pyruvate/alanine as a co‐substrate couple. The biocatalytic simultaneous parallel cascade reaction presented here poses itself as a customizable amine racemization system with potential for the chemical industry in competition with traditional transition‐metal catalysis.

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Section: Introductionmentioning

confidence: 99%

Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions

Ruggieri

Langen²,

Logan

et al. 2018

ChemCatChem

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“…A relatively high number of articles and reviews have been published on the application of enzymatic DKR . Several DKR studies were based on the use of metal catalysts, such as ruthenium, or palladium complexes, whereas others used non‐metal racemisation agents such as zeolites . When the asymmetric centre has an acidic proton, in situ base‐catalysed racemisation may occur .…”

Section: Introductionmentioning

confidence: 99%

Dynamic Kinetic Resolution of Ethyl 1,2,3,4‐Tetrahydro‐β‐carboline‐1‐carboxylate: Use of Different Hydrolases for Stereocomplementary Processes

et al. 2017

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Both enantiomers of 1,2,3,4‐tetrahydro‐β‐carboline‐1‐carboxylic acid have been prepared by dynamic kinetic resolution of the corresponding ethyl ester (±)‐1. CAL‐B‐catalysed hydrolysis of (±)‐1·HCl in NH4OAc buffer (pH 8.0, 30 °C) provided amino acid (R)‐2·HCl with 98 % ee and 90 % yield in 20 min. The hydrolysis with Alcalase in borate buffer (pH 8.0, 30 °C) showed S selectivity and the product (S)‐2·HCl was obtained with 60 % ee and 66 % yield in 45 h. The absolute configuration of (S)‐2 was determined by TDDFT electronic circular dichroism and optical rotation calculations.

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“…In recent years, there have been increased investigations on racemization catalysts, including Ru complexes (Pàmies and Bäckvall, 2001), Raney Ni (Parvulescu et al, 2008), Pd nanoparticles (Kim et al, 2007), Pd=C (Reetz and Schimossek, 1996;Choi et al, 2001), Pd=BaSO 4 (Parvulescu et al, 2007;Parvulescu et al, 2009), Pd=layered double hydroxide (LDH) (Xu et al, 2014), and Pt (Shi et al, 2012). However, the compatibilities of the racemization catalysts with that of the enzymes have not been studied.…”

Section: Introductionmentioning

confidence: 99%

Synergistic Effect of Pd/C and Novozyme 435 on the Dynamic Kinetic Resolution of 1,1,1-trifluoroisopropylamine

Jiang

Cheng

2016

Chemical Engineering Communications

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Response surface methodology (RSM) was successfully applied to study the synergistic effect of Pd=C and Novozyme 435 on the dynamic kinetic resolution of 1,1,1-trifluoroisopropylamine (TFPA). The variables taken into consideration were reaction temperature, substrate concentration, the Pd=C amount, and the Novozyme 435 amount. A statistical model was used to evaluate the influence of the variables on the conversion and enantiomeric excess (ee). It was found that the interaction between the Novozyme 435 and Pd=C was a significant parameter that affected TFPA conversion. The optimum conditions for RSM were: reaction temperature of 35 C, substrate (AE) À 1 concentration of 0.4 mol=L, 60 g=L of Novozyme 435, and 42.4 g=L of Pd=C (3 wt% of Pd on active carbon). The actual experimental conversion was 95.6% under optimum conditions, which was comparable to the maximum predicted value of 95.7%.

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Efficient dynamic kinetic resolution of arylamines with Pd/layered double-hydroxide-dodecyl sulfate anion for racemization

Cited by 19 publications

References 18 publications

Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions

Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions

Dynamic Kinetic Resolution of Ethyl 1,2,3,4‐Tetrahydro‐β‐carboline‐1‐carboxylate: Use of Different Hydrolases for Stereocomplementary Processes

Synergistic Effect of Pd/C and Novozyme 435 on the Dynamic Kinetic Resolution of 1,1,1-trifluoroisopropylamine

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