ArticleMicrobial cell factories2025
Efficient refolding, purification, and characterization of barley oxalate oxidase in Escherichia coli.
Article in Microbial cell factories, 2025. 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
6 authors.
Funding
Abstract
backgroundOxalate oxidase (OxOx) is an important enzyme commonly used in the determination of urine oxalate concentration. It is naturally expressed by a variety of plants and microorganisms and recombinant OxOx enzyme has been successfully expressed in yeast, but not in Escherichia coli (E. coli) due to its aggregation in insoluble inclusion bodies. This study aimed to (1) develop a method for purification of active OxOx following expression in E. coli and (2) demonstrate the feasibility of using filter paper coated with recombinant OxOx as a method to measure oxalate concentration in solution.
resultsA synthetic gene optimized for E. coli codon bias expression was derived from barley and cloned into the pRSET expression vector. Phenyl-Sepharose CL-4B and Q-Sepharose Fast Flow chromatography purified the active enzyme to over 90% purity. Using these methods, 21 mg of purified active OxOx enzyme was obtained from a 1 L culture. The purified OxOx exhibited an activity of 3.4 U/mg with the minimum oxalate concentration needed for visual detection on filter paper of 25 µM (range 25-500 µM).
conclusionOur study highlights the feasibility of using E. coli for the expression and purification of OxOx, providing a promising approach for future applications in the field of healthcare. Our study has also laid the foundation for further developing an oxalate test strip for urinary oxalate assays based on OxOx.
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.