ArticleBiotechnology research international2015
Purification, Characterization of L-Methioninase from Candida tropicalis, and Its Application as an Anticancer.
Article in Biotechnology research international, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
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- Production and purification of methionine gamma-lyase from Iranian soil mulds: investigation of physicochemical properties and anticancer effects.BMC cancer · 2025Article
- 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
- Purification, Characterization and anticancer activity of L-methionine γ-lyase from thermo-tolerant Aspergillus fumigatus.Microbial cell factories · 2023Article
- Article
- BacteriumSaudi journal of biological sciences · 2020Article
- Antibacterial and Anticancer Activity and Untargeted Secondary Metabolite Profiling of Crude Bacterial Endophyte Extracts fromInternational journal of microbiology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aim of the present study is to purify L-methioninase from Candida tropicalis 34.19-fold with 27.98% recovery after ion exchange chromatography followed by gel filtration. The purified enzyme revealed a single band on SDS-PAGE gel with a molecular weight of 46 KDa. Its optimum temperature was 45 to 55 and thermal stability was 55°C for 15 min. The enzyme had optimum pH at 6.5 and stability at a pH range of 5.5 to 7.0 for 24 hr. The maximum activity was observed with substrate concentration of 30 µM and Km was 0.5 mM. The enzyme was strongly inhibited by Cd(+2) and Cu(+2) while it was enhanced by Na(+), Ni(+2), and Mg(+2) at 10 mM while Ca(+2) had slight activation at 20 mM. In addition, the potential application of the L-methioninase as an anticancer agent against various types of tumor cell lines is discussed.
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Registered trials
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