Evidence map›Paper›PMID 28986983›Full record

ArticleBiotechnology and bioengineering2018

Enzymatic synthesis of chiral amino-alcohols by coupling transketolase and transaminase-catalyzed reactions in a cascading continuous-flow microreactor system.

Pia Gruber, Filipe Carvalho, Marco P C Marques, Brian O'Sullivan, Fabiana Subrizi, Dragana Dobrijevic, John Ward, Helen C Hailes, Pedro Fernandes, Roland Wohlgemuth and 2 more

Abstract read
In one paragraph

Article in Biotechnology and bioengineering, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Synthetic and systems biotechnology · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Biocatalysis in Continuous-Flow Microfluidic Reactors.Advances in biochemical engineering/biotechnology · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Continuous flow biocatalysis.Chemical Society reviews · 2018
    Review
  15. Article
  16. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Pia GruberDepartment of Biochemical Engineering, University College London, London, United Kingdom.
Filipe CarvalhoDepartment of Bioengineering and IBB-Institute for Bioengineering and Biosciences, Instituto Superior Técnico, Universidade de Lisboa, Lisboa, Portugal.
Marco P C MarquesDepartment of Biochemical Engineering, University College London, London, United Kingdom.
Brian O'SullivanDepartment of Biochemical Engineering, University College London, London, United Kingdom.
Fabiana SubriziDepartment of Chemistry, University College London, London, United Kingdom.
Dragana DobrijevicDepartment of Biochemical Engineering, University College London, London, United Kingdom.
John WardDepartment of Biochemical Engineering, University College London, London, United Kingdom.
Helen C HailesDepartment of Chemistry, University College London, London, United Kingdom.
Pedro FernandesDepartment of Bioengineering and IBB-Institute for Bioengineering and Biosciences, Instituto Superior Técnico, Universidade de Lisboa, Lisboa, Portugal.
Roland WohlgemuthSigma-Aldrich, Member of Merck Group, Buchs, Switzerland.
Frank BaganzDepartment of Biochemical Engineering, University College London, London, United Kingdom.
Nicolas SzitaDepartment of Biochemical Engineering, University College London, London, United Kingdom.ORCID 0000-0002-6204-5074

Funding

Biotechnology and Biological Sciences Research Council BB/L000997/1
6 · The paper itself

Abstract

Rapid biocatalytic process development and intensification continues to be challenging with currently available methods. Chiral amino-alcohols are of particular interest as they represent key industrial synthons for the production of complex molecules and optically pure pharmaceuticals. (2S,3R)-2-amino-1,3,4-butanetriol (ABT), a building block for the synthesis of protease inhibitors and detoxifying agents, can be synthesized from simple, non-chiral starting materials, by coupling a transketolase- and a transaminase-catalyzed reaction. However, until today, full conversion has not been shown and, typically, long reaction times are reported, making process modifications and improvement challenging. In this contribution, we present a novel microreactor-based approach based on free enzymes, and we report for the first time full conversion of ABT in a coupled enzyme cascade for both batch and continuous-flow systems. Using the compartmentalization of the reactions afforded by the microreactor cascade, we overcame inhibitory effects, increased the activity per unit volume, and optimized individual reaction conditions. The transketolase-catalyzed reaction was completed in under 10 min with a volumetric activity of 3.25 U ml

Indexed as

AminoacyltransferasesAmino AlcoholsCatalysisEscherichia coliEscherichia coli ProteinsTransketolaseAminoacyltransferasesAmino AlcoholsEscherichia coli ProteinstransamidasesTransketolasecascading reactor systemcontinuous-flow microreactorsmulti-step bioconversiontransaminasetransketolase

Identifiers

PMID28986983
PMCPMC5813273

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.