Evidence map›Paper›PMID 35327664›Full record

ReviewBiomolecules2022

Glucose Oxidase, an Enzyme "Ferrari": Its Structure, Function, Production and Properties in the Light of Various Industrial and Biotechnological Applications.

Jacob A Bauer, Monika Zámocká, Juraj Majtán, Vladena Bauerová-Hlinková

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
17.9field-weighted citation impact, top 1% 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

63 citing papers in PubMed, 212 citations in OpenAlex.

  1. Article
  2. Article
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  20. Micro-Environment Programmable Quinoline COFs for High-Performance Photocatalytic HAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article

3 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Jacob A BauerInstitute of Molecular Biology, Slovak Academy of Sciences, 845 51 Bratislava, Slovakia.ORCID 0000-0002-1396-1340
Monika ZámockáInstitute of Molecular Biology, Slovak Academy of Sciences, 845 51 Bratislava, Slovakia.
Juraj MajtánInstitute of Molecular Biology, Slovak Academy of Sciences, 845 51 Bratislava, Slovakia.ORCID 0000-0002-7268-1584
Vladena Bauerová-HlinkováInstitute of Molecular Biology, Slovak Academy of Sciences, 845 51 Bratislava, Slovakia.ORCID 0000-0003-0777-4407
Slovak Academy of Sciences · SKSlovak Medical University · SK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glucose oxidase (GOx) is an important oxidoreductase enzyme with many important roles in biological processes. It is considered an "ideal enzyme" and is often called an oxidase "Ferrari" because of its fast mechanism of action, high stability and specificity. Glucose oxidase catalyzes the oxidation of β-d-glucose to d-glucono-δ-lactone and hydrogen peroxide in the presence of molecular oxygen. d-glucono-δ-lactone is sequentially hydrolyzed by lactonase to d-gluconic acid, and the resulting hydrogen peroxide is hydrolyzed by catalase to oxygen and water. GOx is presently known to be produced only by fungi and insects. The current main industrial producers of glucose oxidase are

Indexed as

Glucose OxidaseHydrogen PeroxideBiotechnologyGlucoseOxygenGlucoseGlucose OxidaseHydrogen PeroxideOxygenantimicrobial effectbiosensorscatalytic mechanismFAD binding domainglucose oxidaseGOx producing organismsnanosensors

Identifiers

PMID35327664
PMCPMC8946809
OpenAlexW4221078211

What Socratic 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 Socratic graph.