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Aims <p>Methionine gamma-lyase (MGL) specifically targets L-methionine-dependent cancer cells, making it a promising candidate for anti-cancer drug development. This study aims to purify and characterize L-methioninase from <i>Pseudomonas mosselii</i> and evaluate its potential anti-cancer properties.</p> Methods and results <p>MGL was purified through heat treatment, ion exchange chromatography, and gel filtration, achieving a 6-fold purification and a 58.43% recovery rate. The enzyme displayed an activity of 61.16 U/mg and had a molecular weight of 48&#xa0;kDa. Optimal activity was observed at a pH of 6 and temperatures ranging from 30 to 37℃. Kinetic studies revealed a Km value of 8.458 mM and a Vmax of 0.2702 U/mL/min for L-methionine. The anti-cancer effects of MGL were tested on MCF-7, MOLT-4, HepG-2, and U87MG cell lines. MTT assays demonstrated significant anti-cancer activity, inducing apoptosis in cancer cells while sparing normal fibroblasts. Real-time PCR results demonstrated decreased expression of BCL-2 and increased expression of caspase-3. This further confirms that apoptosis is enhanced by the use of gamma-lyase enzyme and methionine restriction in cancer cells.</p> Conclusions <p>MGL shows promise as a targeted treatment for L-methionine-dependent cancers by selectively inducing apoptosis in cancer cells. Its specific action and effective purification establish MGL as a potential therapeutic candidate.</p>

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Purification, characterization, and anti-cancer activity of methionine gamma-lyase from a native strain of Pseudomonas mosselii for human cancer treatment

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  • 发表日期：

    2025年7月1日

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  • Matin Nasirian,
  • Mohsen Mobini-Dehkordi,
  • Pegah Khosravian

摘要

Aims

Methionine gamma-lyase (MGL) specifically targets L-methionine-dependent cancer cells, making it a promising candidate for anti-cancer drug development. This study aims to purify and characterize L-methioninase from Pseudomonas mosselii and evaluate its potential anti-cancer properties.

Methods and results

MGL was purified through heat treatment, ion exchange chromatography, and gel filtration, achieving a 6-fold purification and a 58.43% recovery rate. The enzyme displayed an activity of 61.16 U/mg and had a molecular weight of 48 kDa. Optimal activity was observed at a pH of 6 and temperatures ranging from 30 to 37℃. Kinetic studies revealed a Km value of 8.458 mM and a Vmax of 0.2702 U/mL/min for L-methionine. The anti-cancer effects of MGL were tested on MCF-7, MOLT-4, HepG-2, and U87MG cell lines. MTT assays demonstrated significant anti-cancer activity, inducing apoptosis in cancer cells while sparing normal fibroblasts. Real-time PCR results demonstrated decreased expression of BCL-2 and increased expression of caspase-3. This further confirms that apoptosis is enhanced by the use of gamma-lyase enzyme and methionine restriction in cancer cells.

Conclusions

MGL shows promise as a targeted treatment for L-methionine-dependent cancers by selectively inducing apoptosis in cancer cells. Its specific action and effective purification establish MGL as a potential therapeutic candidate.