Evidence map›Paper›PMID 29242048›Full record

ArticleNew biotechnology2018

Simplified immobilisation method for histidine-tagged enzymes in poly(methyl methacrylate) microfluidic devices.

Gulsim Kulsharova, Nikolay Dimov, Marco P C Marques, Nicolas Szita, Frank Baganz

Open access · hybridAbstract read
In one paragraph

Article in New biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

11 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  5. Enzyme immobilization studied through molecular dynamic simulations.Frontiers in bioengineering and biotechnology · 2023
    Review
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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 1 country.

Gulsim KulsharovaDepartment of Biochemical Engineering, University College London, London, WC1H 0AH, United Kingdom. Electronic address: g.kulsharova@ucl.ac.uk.
Nikolay DimovDepartment of Biochemical Engineering, University College London, London, WC1H 0AH, United Kingdom. Electronic address: n.dimov@ucl.ac.uk.
Marco P C MarquesDepartment of Biochemical Engineering, University College London, London, WC1H 0AH, United Kingdom. Electronic address: marco.marques@ucl.ac.
Nicolas SzitaDepartment of Biochemical Engineering, University College London, London, WC1H 0AH, United Kingdom. Electronic address: n.szita@ucl.ac.uk.
Frank BaganzDepartment of Biochemical Engineering, University College London, London, WC1H 0AH, United Kingdom. Electronic address: f.baganz@ucl.ac.uk.
University College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly(methyl methacrylate) (PMMA) microfluidic devices have become promising platforms for a wide range of applications. Here we report a simple method for immobilising histidine-tagged enzymes suitable for PMMA microfluidic devices. The 1-step-immobilisation described is based on the affinity of the His-tag/Ni-NTA interaction and does not require prior amination of the PMMA surface, unlike many existing protocols. We compared it with a 3-step immobilisation protocol involving amination of PMMA and linking NTA via a glutaraldehyde cross-linker. These methods were applied to immobilise transketolase (TK) in PMMA microfluidic devices. Binding efficiency studies showed that about 15% of the supplied TK was bound using the 1-step method and about 26% of the enzyme was bound by the 3-step method. However, the TK-catalysed reaction producing l-erythrulose performed in microfluidic devices showed that specific activity of TK in the device utilising the 1-step immobilisation method was approximately 30% higher than that of its counterpart. Reusability of the microfluidic device produced via the 1-step method was tested for three cycles of enzymatic reaction and at least 85% of the initial productivity was maintained. The device could be operated for up to 40 h in a continuous flow and on average 70% of the initial productivity was maintained. The simplified immobilisation method required fewer chemicals and less time for preparation of the immobilised microfluidic device compared to the 3-step method while achieving higher specific enzyme activity. The method represents a promising approach for the development of immobilised enzymatic microfluidic devices and could potentially be applied to combine protein purification with immobilisation.

Indexed as

Enzymes, ImmobilizedHistidineMicrofluidicsPolymethyl MethacrylateSurface PropertiesTransketolaseEnzymes, ImmobilizedHistidinePolymethyl MethacrylateTransketolaseEnzyme immobilisationHistidine-tagged enzymeMicrofluidicsPoly(methyl methacrylate) (PMMA)Transketolase

Identifiers

PMID29242048
PMCPMC6191535
OpenAlexW2771983930

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.