ArticleBMC biotechnology2025
Novel thrombolytic protease from the rare halophile Brachybacterium paraconglomeratum: bioprocessing and in vitro application.
Article in BMC 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.
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
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAlkaline proteases are hydrolytic enzymes that play a crucial role in various biological processes. Proteases produced by halophiles showed exceptional efficiency in breaking down the complex structures ranging from pigments to extracellular proteins, tissue proteins to tumors, and thrombin clots. There is a huge global demand for naturally occurring thrombolytic proteases to treat intravascular thrombosis, as they are cost-effective and have minimal detrimental effects, making them widely used in the biomedical applications.
resultsThe production of thrombolytic protease from the rare halophile Brachybacterium paraconglomeratum strain M4 and its in-vitro thrombolytic activity is investigated for the first time. On skim milk agar, a distinct zone of casein hydrolysis was observed, in submerged fermentation a substantial protease production was noted. The enzyme was purified through a four-step purification process following an initial precipitation with 60% ammonium sulfate, subsequent ion-exchange chromatography using DEAE-cellulose, and final gel-filtration chromatography utilizing Sephadex G-100. As a result, a protein with a specific activity of 300 ± 32 U/mg was obtained with a purification fold of 19 and a recovery percentage of 38.2%. The molecular mass of the purified enzyme was 14.4 kDa via SDS-PAGE while MALDI/MS analysis further revealed a 131 amino acid sequence with an isoelectric point of 8.55 and on comparison, the strain M4 alkaline protease aligns with the proteasome subunit alpha. The protease is classified as a serine protease based on the inhibition by PMSF and its activity profile. The in-vitro thrombolytic assay revealed that the purified enzyme achieved a clot lysis rate of 65 ± 3%, performing effectively in comparison to the standard.
conclusionThe findings indicate that strain M4 is an efficient producer of thrombolytic protease and the purified form effectively dissolves thrombin clots. Currently, the studies are underway to explore its potential for biomedical applications and industrial-scale production.
Indexed as
Identifiers
What Socratic 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 Socratic graph.