ArticleMolecular biotechnology2026
Heterologous Reconstitution of the Biosynthesis Pathway for Producing Holo-C-Phycocyanin Alpha Subunit (CpcA) from Thermosynechococcus sp. TUBT-T01.
Article in Molecular biotechnology, 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
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
C-phycocyanin (C-PC), a blue protein pigment found in cyanobacteria, has potential properties for use in food and medical applications, including antioxidants, antimicrobial, and anti-inflammatory. Generally, C-PC is extracted from mesophilic cyanobacteria, such as Arthrospira platensis, which is unstable under high-temperature conditions. Therefore, thermophilic cyanobacteria represent potential sources of thermostable C-PC. This study aimed to produce a holo-C-PC alpha subunit (holo-CpcA) from the thermophilic cyanobacterium Thermosynechococcus sp. TUBT-T01 by reconstituting the pathway in Escherichia coli. The constructed expression plasmid was designed with a polycistronic transcription unit containing ho1, pcyA, cpcE, and cpcF inserted into pET3a. Together with the pET28a carrying cpcA gene, two plasmids were co-transformed and co-expressed in E. coli Rosetta (DE3). Following induction, the cell pellet exhibited a visible color change, suggesting successful expression of the C-PC alpha subunit. The antioxidant activity of crude holo-CpcA was analyzed; it showed higher antioxidant activity compared to crude apo-CpcA in both the ABTS radical cation decolorization assay and the ORAC-Fluorescein Assay. This study reported the successful heterologous production of holo-CpcA from Thermosynechococcus sp. in E. coli, and the protein also demonstrated antioxidant activities.
Indexed as
Identifiers
41168617What 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.