Unprecedented, Fully Recyclable, Solid-Supported Reagent for the Kinetic Resolution of Racemic Amines Through Enantioselective N-Acetylation.

Immobilization of transaminases creates promising biocatalysts for production of chiral amines in batch or continuous-flow mode reactions. E. coli cells containing overexpressed transaminases of various selectivities and hollow silica microspheres as supporting agent were immobilized by an improved sol-gel process to produce immobilized transaminase biocatalysts with suitable stability and mechanical properties for continuous-flow applications. The immobilized cell-based transaminase biocatalyst proved to be durable and easy-to-use in kinetic resolution of four racemic amines 1a–d. The batch and continuous-flow mode kinetic resolutions with transaminase biocatalyst of opposite stereopreference provided access to both enantiomers of the corresponding amines. By using the most suitable immobilized transaminase biocatalysts, this study describes the first transaminase-based approach for the production of both pure enantiomers of 1-(3,4-dimethoxyphenyl)ethan-1-amine 1d.

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The Kinetic Resolution of Racemic Amines Using a Whole-Cell Biocatalyst Co-Expressing Amine Dehydrogenase and NADH Oxidase

Catalysts ◽

10.3390/catal7090251 ◽

2017 ◽

Vol 7 (9) ◽

pp. 251 ◽

Cited By ~ 8

Author(s):

Hyunwoo Jeon ◽

Sanghan Yoon ◽

Md Ahsan ◽

Sihyong Sung ◽

Geon-Hee Kim ◽

...

Keyword(s):

Kinetic Resolution ◽

Nadh Oxidase ◽

Whole Cell ◽

Whole Cell Biocatalyst ◽

Amine Dehydrogenase ◽

Racemic Amines

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Covalently immobilized Trp60Cys mutant of ω-transaminase from Chromobacterium violaceum for kinetic resolution of racemic amines in batch and continuous-flow modes

Biochemical Engineering Journal ◽

10.1016/j.bej.2018.01.022 ◽

2018 ◽

Vol 132 ◽

pp. 270-278 ◽

Cited By ~ 19

Author(s):

Emese Abaházi ◽

Péter Sátorhelyi ◽

Balázs Erdélyi ◽

Beáta G. Vértessy ◽

Henrik Land ◽

...

Keyword(s):

Continuous Flow ◽

Kinetic Resolution ◽

Chromobacterium Violaceum ◽

Racemic Amines

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SYNTHETIC CONTROL BASED ON CHIRAL 2-HALOPYRIDINIUM SALTS II. THE KINETIC RESOLUTION OF RACEMIC AMINES

Chemistry Letters ◽

10.1246/cl.1977.651 ◽

1977 ◽

Vol 6 (6) ◽

pp. 651-654 ◽

Cited By ~ 4

Author(s):

Teruaki Mukaiyama ◽

Makoto Onaka ◽

Manzo Shiono

Keyword(s):

Kinetic Resolution ◽

Synthetic Control ◽

Racemic Amines

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Parallel kinetic resolution of racemic amines using 3-N,N-diacylaminoquinazolin-4(3H)-ones

Chemical Communications ◽

10.1039/b109297a ◽

2001 ◽

pp. 2684-2685 ◽

Cited By ~ 18

Author(s):

Abdullah G. Al-Sehemi ◽

Robert S. Atkinson ◽

Christopher K. Meades

Keyword(s):

Kinetic Resolution ◽

Parallel Kinetic Resolution ◽

Racemic Amines

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Kinetic Resolution and Deracemization of Racemic Amines Using a Reductive Aminase

ChemCatChem ◽

10.1002/cctc.201701484 ◽

2018 ◽

Vol 10 (3) ◽

pp. 515-519 ◽

Cited By ~ 23

Author(s):

Godwin A. Aleku ◽

Juan Mangas-Sanchez ◽

Joan Citoler ◽

Scott P. France ◽

Sarah L. Montgomery ◽

...

Keyword(s):

Kinetic Resolution ◽

Racemic Amines

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ChemInform Abstract: Nonenzymatic Acylative Kinetic Resolution of Racemic Amines and Related Compounds.

ChemInform ◽

10.1002/chin.201229253 ◽

2012 ◽

Vol 43 (29) ◽

pp. no-no

Author(s):

Victor P. Krasnov ◽

Dmitry A. Gruzdev ◽

Galina L. Levit

Keyword(s):

Kinetic Resolution ◽

Racemic Amines ◽

Related Compounds

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How the mode of Candida antarctica lipase B immobilization affects the continuous-flow kinetic resolution of racemic amines at various temperatures

Journal of Molecular Catalysis B Enzymatic ◽

10.1016/j.molcatb.2012.09.004 ◽

2013 ◽

Vol 85-86 ◽

pp. 119-125 ◽

Cited By ~ 25

Author(s):

Zoltán Boros ◽

Péter Falus ◽

Mária Márkus ◽

Diána Weiser ◽

Márk Oláh ◽

...

Keyword(s):

Continuous Flow ◽

Kinetic Resolution ◽

Candida Antarctica ◽

Candida Antarctica Lipase B ◽

Candida Antarctica Lipase ◽

Lipase B ◽

Racemic Amines

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Lipase B from Candida antarctica Immobilized on Epoxy-functionalized Hollow Silica Microspheres: Efficient Biocatalysts for Enantiomer Selective Acylation of Alcohols and Amines

Periodica Polytechnica Chemical Engineering ◽

10.3311/ppch.12517 ◽

2018 ◽

Vol 62 (4) ◽

Cited By ~ 2

Author(s):

Márk Oláh ◽

Szandra Suba ◽

Zoltán Boros ◽

Péter Kovács ◽

Mathilde Gosselin ◽

...

Keyword(s):

Continuous Flow ◽

Kinetic Resolution ◽

Operation Time ◽

Candida Antarctica ◽

Effect Of Temperature ◽

Flow Mode ◽

Silica Microspheres ◽

Lipase B ◽

Hollow Silica ◽

Racemic Amines

Hollow silica microspheres with promising physical properties (MAT540TM) as support for enzyme immobilization and biocatalyst were investigated in this study. The amine-functionalized MAT540TM was activated by six bisepoxides inclosing different spacers and used as epoxy-functionalized carrier for immobilization of lipase B from Candida antarctica (CaLB). The novel, covalently fixed CaLB biocatalysts were compared in kinetic resolution (KR) of racemic 1-phenyethanol rac-1 and five racemic amines rac-3a-e using shaken flasks and continuous-flow packed-bed microreactors. Mechanic stability, re-usability and the effect of temperature (0–90 °C) on productivity and enantiomer selectivity of the covalently immobilized CaLB were investigated. The best performing CaLB biocatalyst showed good mechanic stability after 24 h operation time in continuous-flow mode at 60 °C and provided in KRs of racemic 1-phenyethanol rac-1 with vinyl acetate and of five racemic amines with isopropyl 2-ethoxyacetate as acylating agent the non-reacted (S)-alcohol [(S)-1] or (S)-amines [(S)-3a-e] and the forming (R)-ester [(R)-2] or (R)-amide [(R)-4a-e] in good yields with high enantiomeric excess (ee > 99 %, for all).

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