ArticleBMC biotechnology2024
Characterization, modeling, and anticancer activity of L.arginase production from marine Bacillus licheniformis OF2.
Article in BMC biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- In Silico Characterization and Molecular Docking of the L-Arginase Gene From Alcaligenes aquatilis BC2.Biotechnology and applied biochemistry · 2026Article
- Purification and characterization of arginase from a new Aspergillus niger AUMC16187 isolate from sandy soil.Archives of microbiology · 2026Article
- Characterization and Modeling of Marine Bacillus cereus Strain MSS1 Exopolysaccharide and Its Antagonistic Effect on Colon Cancer.Probiotics and antimicrobial proteins · 2026Article
- Optimization of fermentation conditions for enhanced L-arginase production by Alcaligenes aquatilis BC2 using response surface methodology.Journal, genetic engineering & biotechnology · 2025Article
- Production of extracellular L-arginase by Alcaligenes aquatilis BC2 isolated from soda lakes (Lake Chitu) of Ethiopia.Journal of industrial microbiology & biotechnology · 2024Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundL-arginase, is a powerful anticancer that hydrolyzes L-arginine to L-ornithine and urea. This enzyme is widely distributed and expressed in organisms like plants, fungi, however very scarce from bacteria. Our study is based on isolating, purifying, and screening the marine bacteria that can produce arginase.
resultsThe highest arginase producing bacteria will be identified by using microbiological and molecular biology methods as Bacillus licheniformis OF2. Characterization of arginase is the objective of this study. The activity of enzyme was screened, and estimated beside partial sequencing of arginase gene was analyzed. In silico homology modeling was applied to generate the protein's 3D structure, and COACH and COFACTOR were applied to determine the protein's binding sites and biological annotations based on the I-TASSER structure prediction. The purified enzyme was undergone an in vitro anticancer test.
conclusionsL-arginase demonstrated more strong anti-cancer cells with an IC50 of 21.4 ug/ml in a dose-dependent manner. L-arginase underwent another investigation for its impact on the caspase 7 and BCL2 family of proteins (BCL2, Bax, and Bax/Bcl2). Through cell arrest in the G1/S phase, L-arginase signals the apoptotic cascade, which is supported by a flow cytometry analysis of cell cycle phases.
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