Evidence map›Paper›PMID 34746608›Full record

ArticleACS omega2021

Three Steps, Two Enzymes, One Pot, but a Multitude of Nanocompartments: Combined Cycles of Kinetic Resolutions and Re-racemization with Incompatible Biocatalysts.

Florian Golombek, Marco Haumann, Matthias S G Knoll, Andreas Paul Fröba, Kathrin Castiglione

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 37% of its field
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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Biocatalytic Synthesis Using Self-Assembled Polymeric Nano- and Microreactors.Angewandte Chemie (International ed. in English) · 2022
    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

5 authors at 1 institution in 2 countries.

Florian GolombekDepartment of Chemical and Biological Engineering, Institute of Bioprocess Engineering, Friedrich-Alexander University Erlangen-Nürnberg, Paul-Gordan-Str. 3, 91052 Erlangen, Germany.
Marco HaumannDepartment Chemie- und Bioingenieurwesen, Lehrstuhl für Chemische Reaktionstechnik (CRT), Friedrich-Alexander Universität Erlangen-Nürnberg (FAU), Egerlandstr. 3, Erlangen 91058, Germany.ORCID https://orcid.org/0000-0002-3896-365X
Matthias S G KnollDepartment of Chemical and Biological Engineering, Institute of Advanced Optical Technologies - Thermophysical Properties, Friedrich-Alexander University Erlangen-Nürnberg, Paul-Gordan-Str. 8, Erlangen 91052, Germany.
Andreas Paul FröbaDepartment of Chemical and Biological Engineering, Institute of Advanced Optical Technologies - Thermophysical Properties, Friedrich-Alexander University Erlangen-Nürnberg, Paul-Gordan-Str. 8, Erlangen 91052, Germany.
Kathrin CastiglioneDepartment of Chemical and Biological Engineering, Institute of Bioprocess Engineering, Friedrich-Alexander University Erlangen-Nürnberg, Paul-Gordan-Str. 3, 91052 Erlangen, Germany.ORCID https://orcid.org/0000-0001-9086-0036
Friedrich-Alexander-Universität Erlangen-Nürnberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deracemizations are clearly preferable to kinetic resolutions in the production of chiral molecules from racemates, as they allow up to 100% chemical and optical yield. Here we present a new process route for multienzymatic deracemizations that is relevant for reaction systems with incompatible reaction conditions of the biocatalysts. This often applies to combinations of lipases used for stereoselective acylation and solvent-sensitive racemases. By encapsulating a model racemase in polymeric vesicles, it was protected from inactivation by the organic solvent up to phase proportions of 99%. As high yields in the lipase reaction required either water proportions well below 1% or racemase-denaturating acyl donor concentrations, a one-pot reaction was implemented through the sequential use of lipase and racemase-containing nanocompartments. This strategy allowed us to perform two kinetic resolutions with intermittent re-racemization in one pot yielding 72% (0.72 mM after 120 h) of an enantiopure product.

Identifiers

PMID34746608
PMCPMC8567398
OpenAlexW3209256333

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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.