Biomimetic mineralization of chemically modified glucose oxidase from Aspergillus niger in ZIF-8.

Marija Stanišić, Milica Crnoglavac Popović, Marko Radenković, Branimir Bajac, Vojin Tadić, Olivera Prodanović, Radivoje Prodanović

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In one paragraph

Article in Biotechnology letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

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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

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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

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Marija StanišićFaculty of Chemistry, University of Belgrade, Studentski Trg 12, 11000, Belgrade, Serbia.

Milica Crnoglavac PopovićFaculty of Chemistry, University of Belgrade, Studentski Trg 12, 11000, Belgrade, Serbia.

Marko RadenkovićBioSense Institute, University of Novi Sad, Dr Zorana Đinđića 1, 21000, Novi Sad, Serbia.

Branimir BajacBioSense Institute, University of Novi Sad, Dr Zorana Đinđića 1, 21000, Novi Sad, Serbia.

Vojin TadićJoint Stock Company "Elektroprivreda Srbije", Balkanska 13, 11000, Belgrade, Serbia.

Olivera ProdanovićUniversity of Belgrade - Institute of Multidisciplinary Research, Kneza Višeslava 1, 11030, Belgrade, Serbia.

Radivoje ProdanovićFaculty of Chemistry, University of Belgrade, Studentski Trg 12, 11000, Belgrade, Serbia. rprodano@chem.bg.ac.rs.ORCID http://orcid.org/0000-0003-4662-1825

Funding

Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja 451-03-136/2025-03/200053Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja 451-03-136/2025-03/200168

6 · The paper itself

Abstract

Chemical surface modification of enzymes represents a powerful strategy to improve immobilization and catalytic performance. In this study, glucose oxidase (GOx) from Aspergillus niger was chemically modified via periodate oxidation and reductive amination to incorporate L-aspartate (D-GOx) and L-histidine (H-GOx) residues. These modifications enhanced electrostatic and coordinative interactions with Zn

Indexed as

Aspergillus nigerEnzymes, ImmobilizedGlucose OxidaseZeolitesBiomimeticsEnzyme StabilityImidazolesMetal-Organic Frameworks2-methylimidazoleEnzymes, ImmobilizedGlucose OxidaseImidazolesMetal-Organic FrameworksZeolitesZIF-8 metal-organic frameworkGlucose oxidaseImmobilizationPeriodateReductive aminationZeolite imidazolate framework

Identifiers

PMID41831077

DOI10.1016/J.COLSURFB.2020.111108

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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.