ArticleScientific reports2026
Heterologous expression of a heme-dependent catalase from Avicennia marina confers multi-stress tolerance in Escherichia coli for biotechnological applications.
Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The study of antioxidant enzymes in Avicennia marina, a mangrove species, is crucial because of the plant's exceptional ability to survive in harsh environments. Catalase (CAT) is particularly important in reducing the damaging effects of reactive oxygen species (ROS), which are generated as a result of various stresses. In the present work, the gene encoding CAT from A. marina (AmCAT) was amplified from the full-length cDNA, cloned into pET32a and expressed as a Thioredoxin (Trx)-tagged fusion protein in E. coli. The recombinant enzyme, which was mainly soluble, exhibited 55,000 U/mg activity after purification. It showed optimal activity at 35 °C and pH 7, with high stability up to 40 °C and pH 6-8. Trx-AmCAT likely forms a homotetramer with a molecular mass of 280 kDa and incorporates four moles of Fe²⁺ per tetramer, essential for its hydrogen peroxide-decomposing activity. The expression and activity of AmCAT in A. marina seedlings were significantly upregulated under stress conditions, particularly in the leaves, indicating its role in stress tolerance. Furthermore, heterologous expression of AmCAT in E. coli enhanced its tolerance to NaCl, H
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.