Evidence map›Paper›PMID 41561900›Full record

ArticleData in brief2026

Dataset on the analysis of β-galactosidase immobilization efficiency on aminomethyl polystyrene (AMP) resin in syringe and column reactors.

Tabea Boehme, Bernadette Straub, Ursula Eschenhagen, Magnus S Schmidt

Abstract read
In one paragraph

Article in Data in brief, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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.

Tabea BoehmeInstitute of Precision Medicine, Organic and Bioorganic Chemistry Labs, Faculty Health Medical and Life Sciences, Furtwangen University, Jakob-Kienzle-Str. 17, D-78054 VS-Schwenningen, Germany.
Bernadette StraubInstitute of Precision Medicine, Organic and Bioorganic Chemistry Labs, Faculty Health Medical and Life Sciences, Furtwangen University, Jakob-Kienzle-Str. 17, D-78054 VS-Schwenningen, Germany.
Ursula EschenhagenInstitute of Precision Medicine, Organic and Bioorganic Chemistry Labs, Faculty Health Medical and Life Sciences, Furtwangen University, Jakob-Kienzle-Str. 17, D-78054 VS-Schwenningen, Germany.
Magnus S SchmidtInstitute of Precision Medicine, Organic and Bioorganic Chemistry Labs, Faculty Health Medical and Life Sciences, Furtwangen University, Jakob-Kienzle-Str. 17, D-78054 VS-Schwenningen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Galactosidase was covalently immobilized on AMP resin using a p-phenylenediisothiocyanate (PDC) linker. Resin loading was determined by measuring the protein concentration difference between the original lactase solution and the reactor supernatant using a Bradford assay. Enzyme activity of the supernatants was assessed with ONPG as the substrate, and lactose turnover rates were measured using a lactose solution. The dataset provides detailed results for five different approaches with several syringe reactors and two column reactors, enabling comparison of immobilization efficiency and catalytic performance. The dataset may be valuable for industrial applications where stable and efficient immobilized β-galactosidase systems are required, such as lactose-free dairy production.

Indexed as

Covalent enzyme immobilizationLactoseONPGΒ-galactosidase

Identifiers

PMID41561900
PMCPMC12813484

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.