ArticleMicrobial cell factories2023
Purification, Characterization and anticancer activity of L-methionine γ-lyase from thermo-tolerant Aspergillus fumigatus.
Article in Microbial cell factories, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.
What it found
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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.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Review
- Article
- Integrated production and protein-protein docking analysis of3 Biotech · 2025Article
- Production and purification of methionine gamma-lyase from Iranian soil mulds: investigation of physicochemical properties and anticancer effects.BMC cancer · 2025Article
- Application of microbial enzymes in medicine and industry: current status and future perspectives.Future microbiology · 2024Review
- Revealing culturable fungal microbiome communities from the Arabian Peninsula desert representing a unique source of biochemicals for drug discovery and biotechnology.F1000Research · 2024Article
- Isolation and characterization ofSaudi journal of biological sciences · 2023Article
- Biochemical, molecular and anti-tumor characterization of L-methionine gamma lyase produced by localSaudi journal of biological sciences · 2023Article
- Taxonomy and Phylogeny of Eight NewJournal of fungi (Basel, Switzerland) · 2023Article
- GC-MS Based Characterization, Antibacterial, Antifungal and Anti-Oncogenic Activity of Ethyl Acetate Extract ofCurrent issues in molecular biology · 2023Article
- A multi-aspect analysis of two analogous aspergillus spp. belonging to section Flavi: aspergillus flavus and aspergillus oryzae.BMC microbiology · 2023Article
- Editorial: Ligninolytic enzymes and their potential applications.Frontiers in microbiology · 2023Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Purification of L-methionine γ-lyase (MGL) from A. fumigatus was sequentially conducted using heat treatment and gel filtration, resulting in 3.04 of purification fold and 73.9% of enzymatic recovery. The molecular mass of the purified MGL was approximately apparent at 46 KDa based on SDS-PAGE analysis. The enzymatic biochemical properties showed a maximum activity at pH 7 and exhibited plausible stability within pH range 5.0-7.5; meanwhile the highest catalytic activity of MGL was observed at 30-40 °C and the enzymatic stability was noted up to 40 °C. The enzyme molecule was significantly inhibited in the presence of Cu
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