Purification, Characterization and anticancer activity of L-methionine γ-lyase from thermo-tolerant Aspergillus fumigatus

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 analy...

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Published in:Microbial cell factories 2023-01, Vol.22 (1), p.8-11, Article 8
Main Authors: Hendy, Mahmoud H, Hashem, Amr H, Suleiman, Waleed B, Sultan, Mahmoud H, Abdelraof, Mohamed
Format: Article
Language:English
Subjects:
Anticancer activity
Aspergillus fumigatus
Aspergillus fumigatus - metabolism
Carbon-Sulfur Lyases - chemistry
Carbon-Sulfur Lyases - metabolism
Characterization
Kinetics
L-methionine γ-lyase (MGL)
Methionine
Purification
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Summary: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 , Cd , Li , Mn , Hg , sodium azide, iodoacetate, and mercaptoethanol. Moreover, MGL displayed a maximum activity toward the following substrates, L-methionine 
ISSN:1475-2859
1475-2859
DOI:10.1186/s12934-023-02019-z