Evidence map›Paper›PMID 39585503›Full record

ArticleMolecular biotechnology2025

A Simple and Cost-Efficient Method for the Production of Recombinant Horseradish Peroxidase in E. coli.

Kimia Abraheh, Maryam Esmaeili, Nazanin Shans, Saba Ghaffari, Marjan Mohammadi

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular biotechnology, 2025. 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

5 authors.

Kimia AbrahehHPGC Research Group, Department of Medical Biotechnology, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Maryam EsmaeiliHPGC Research Group, Department of Medical Biotechnology, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Nazanin ShansHPGC Research Group, Department of Medical Biotechnology, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Saba GhaffariHPGC Research Group, Department of Medical Biotechnology, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran.
Marjan MohammadiHPGC Research Group, Department of Medical Biotechnology, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran. marjan.mohammadi@pasteur.ac.ir.ORCID http://orcid.org/0000-0003-4970-3455

Funding

Pasteur Institute of Iran #2040Pasteur Institute of Iran IR.PII.REC.1400.079
6 · The paper itself

Abstract

Horseradish peroxidase (HRP) is a chromogenic glycoenzyme widely used in research, diagnostics, and therapeutics. Due to its high demand, various eukaryotic and prokaryotic expression systems have been employed for the production of recombinant HRP. Eukaryotic systems yield properly folded, fully functional enzymes with the necessary post-translational modifications. However, these systems can be costly, time-consuming, and prone to hyperglycosylation. In contrast, prokaryotic systems are simple, inexpensive, and readily available, but achieving proper folding and subsequent modifications can be challenging. In this study, we employed a simple and cost-effective method to produce recombinant HRP in soluble form, using the E. coli expression system. The produced enzyme demonstrated substantial activity (89.75 ± 3.25 U/mg) and resistance to heat (T

Indexed as

Escherichia coliRecombinant ProteinsHorseradish PeroxidaseHydrogen-Ion ConcentrationHydrogen PeroxideHorseradish PeroxidaseHydrogen PeroxideRecombinant ProteinsActivityHRPNativeProkaryoticStability

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.