Evidence map›Paper›PMID 32589387›Full record

ArticleACS applied materials & interfaces2020

Continuous Flow Reactors from Microfluidic Compartmentalization of Enzymes within Inorganic Microparticles.

Tuuli A Hakala, Friedrich Bialas, Zenon Toprakcioglu, Birgit Bräuer, Kevin N Baumann, Aviad Levin, Gonçalo J L Bernardes, Christian F W Becker, Tuomas P J Knowles

Open access · hybridAbstract read
In one paragraph

Article in ACS applied materials & interfaces, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

8 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Sequential storage and release of microdroplets.Microsystems & nanoengineering · 2021
    Article
  8. 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

9 authors at 3 institutions in 3 countries.

Tuuli A HakalaDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
Friedrich BialasInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Street 38, 1090 Vienna, Austria.
Zenon ToprakciogluDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.ORCID http://orcid.org/0000-0003-1964-8432
Birgit BräuerInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Street 38, 1090 Vienna, Austria.
Kevin N BaumannDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.ORCID http://orcid.org/0000-0001-5613-6394
Aviad LevinDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.ORCID http://orcid.org/0000-0002-3949-1033
Gonçalo J L BernardesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.ORCID http://orcid.org/0000-0001-6594-8917
Christian F W BeckerInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Währinger Street 38, 1090 Vienna, Austria.ORCID http://orcid.org/0000-0002-8890-7082
Tuomas P J KnowlesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.ORCID http://orcid.org/0000-0002-7879-0140
University of Cambridge · GBUniversity of Vienna · ATUniversity of Lisbon · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Compartmentalization and selective transport of molecular species are key aspects of chemical transformations inside the cell. In an artificial setting, the immobilization of a wide range of enzymes onto surfaces is commonly used for controlling their functionality but such approaches can restrict their efficacy and expose them to degrading environmental conditions, thus reducing their activity. Here, we employ an approach based on droplet microfluidics to generate enzyme-containing microparticles that feature an inorganic silica shell that forms a semipermeable barrier. We show that this porous shell permits selective diffusion of the substrate and product while protecting the enzymes from degradation by proteinases and maintaining their functionality over multiple reaction cycles. We illustrate the power of this approach by synthesizing microparticles that can be employed to detect glucose levels through simultaneous encapsulation of two distinct enzymes that form a controlled reaction cascade. These results demonstrate a robust, accessible, and modular approach for the formation of microparticles containing active but protected enzymes for molecular sensing applications and potential novel diagnostic platforms.

Indexed as

Microfluidic Analytical TechniquesEndopeptidase KGlucoseHumansParticle SizeSilicon DioxideSurface PropertiesEndopeptidase KGlucoseSilicon Dioxideencapsulationenzymesglucose sensingmicrofluidic flow reactorsilica microparticle

Identifiers

PMID32589387
PMCPMC7383928
OpenAlexW3037149441

What OpenQuestion holds

Textmetadata
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.