Evidence map›Paper›PMID 28361348›Full record

ArticleDie Naturwissenschaften2017

Controlling enzymatic activity by immobilization on graphene oxide.

Paulina Bolibok, Marek Wiśniewski, Katarzyna Roszek, Artur P Terzyk

Open access · hybridAbstract read
In one paragraph

Article in Die Naturwissenschaften, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 47 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Paulina BolibokFaculty of Chemistry, Physicochemistry of Carbon Materials Research Group, Nicolaus Copernicus University in Toruń, Gagarin St. 7, 87-100, Toruń, Poland.
Marek WiśniewskiFaculty of Chemistry, Physicochemistry of Carbon Materials Research Group, Nicolaus Copernicus University in Toruń, Gagarin St. 7, 87-100, Toruń, Poland. marekw@umk.pl.
Katarzyna RoszekDepartment of Biochemistry, Faculty of Biology and Environment Protection, Nicolaus Copernicus University in Toruń, Gagarin St. 7, 87-100, Toruń, Poland.
Artur P TerzykFaculty of Chemistry, Physicochemistry of Carbon Materials Research Group, Nicolaus Copernicus University in Toruń, Gagarin St. 7, 87-100, Toruń, Poland.
Nicolaus Copernicus University · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, graphene oxide (GO) has been applied as a matrix for enzyme immobilization. The protein adsorption capacity of GO is much higher than of other large surface area carbonaceous materials. Its structure and physicochemical properties are reported beneficial also for enzymatic activity modifications. The experimental proof was done here that GO-based biocatalytic systems with immobilized catalase are modifiable in terms of catalyzed reaction kinetic constants. It was found that activity and stability of catalase, considered here as model enzyme, closely depend on enzyme/GO ratio. The changes in kinetic parameters can be related to secondary structure alterations. The correlation between enzyme/GO ratio and kinetic and structure parameters is reported for the first time and enables the conscious control of biocatalytic processes and their extended applications. The biological activity of obtained biocatalytic systems was confirmed in vitro by the use of functional test. The addition of immobilized catalase improved the cells' viability after they were exposed to hydrogen peroxide and tert-butyl-hydroperoxide used as source of reactive oxygen species.

Indexed as

AnimalsBiocatalysisCatalaseCell SurvivalCHO CellsCricetulusEnzyme ActivationEnzymes, ImmobilizedEnzyme StabilityGraphiteHydrogen PeroxideKineticsProtein Structure, Secondarytert-ButylhydroperoxideCatalaseEnzymes, ImmobilizedGraphiteHydrogen Peroxidetert-ButylhydroperoxideCatalaseGraphene oxideImmobilizationKinetic parametersSecondary structure alterations

Identifiers

PMID28361348
PMCPMC5374183
OpenAlexW2602727669

What OpenQuestion holds

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LicenceCC BY
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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.