Evidence map›Paper›PMID 42527817›Full record

ArticleFolia microbiologica2026

High-level expression and characterization of a thermostable thermolysin-like metalloprotease with industrial potential.

Sezgin Karaman, Kubilay Metin

Abstract read
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In one paragraph

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

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Sezgin KaramanDepartment of Plant and Animal Production, Vocational School of Yuksekova, Hakkari University, Hakkari, 30300, Türkiye. sezginkaraman@hakkari.edu.tr.ORCID http://orcid.org/0009-0000-6622-2229
Kubilay MetinDepartment of Biology, Faculty of Science, Aydın Adnan Menderes University, Aydın, 09010, Türkiye.ORCID http://orcid.org/0000-0002-8952-0744

Funding

Aydın Adnan Menderes University ADU-FEF-21009
6 · The paper itself

Abstract

Proteases with high thermostability and catalytic efficiency are highly sought after for industrial applications, particularly within the M4 family of thermolysin-like metalloproteases. In this study, a thermostable thermolysin-like metalloprotease from Geobacillus thermoleovorans HBB208 was cloned and heterologously expressed in Escherichia coli BL21(DE3), yielding a soluble recombinant enzyme. The purified mature enzyme (GtRS1pro; ~34.6 kDa) contains the conserved HEXXH + E catalytic motif, a Zn

Indexed as

CharacterizationIndustrial enzyme applicationsPurificationRecombinant metalloprotease

Identifiers

What OpenQuestion holds

Textmetadata
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.