ArticleMicrobial cell factories2026
Novel L-lysine α-oxidase from marine streptomyces: production, optimization and potent antibacterial activity against drug-resistant pathogens.
Article in Microbial cell factories, 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
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study reported the optimization, purification and characterization of a novel L-lysine α-oxidase (LLO) from marine-derived Streptomyces griseobrunneus strain S15. Among the twenty-two Streptomyces isolates, S15 showed the highest production of LLO (8 U/mg) after 96 h of cultivation. Molecular identification via 16S rRNA sequencing confirmed its phylogenetic relationship to S. griseobrunneus (GenBank PQ416578). Optimization of LLO production using response surface methodology enhanced the enzyme production by about five-fold compared to the control. Purification of LLO resulted in a yield of 49.99% and 2.356-fold purification through a single-step Sephacryl S-300 column. The purified homodimeric enzyme (115 kDa native, 58 kDa subunit) exhibited optimal activity at pH 6.4 and 50 °C, with exceptional thermal stability at physiological temperatures. According to kinetic studies, the enzyme has a high substrate affinity (Km 0.050 mM for L-lysine) and a broad specificity for basic and hydrophobic amino acids. Moreover, the enzyme showed potent antibacterial effects against multidrug-resistant pathogens (MIC 1.99–5.33 U/mL), demonstrated comparable or enhanced antibacterial activity relative to tested antibiotics. The unique combination of catalytic efficiency, stability, and antimicrobial activity makes this LLO a promising candidate for therapeutic and industrial applications.
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.