Bioactive components derived from medicinal herbs have recently acquired popularity due to their efficacy in treating various ailments, including cancer and infectious diseases. In this study, the anticancer enzyme, L-methioninase isolated from medicinal plants endophytic fungi, evaluated its promising therapeutic agents against different types of human cancers. L methionine was purified using column chromatography with the stationary phase of Sephadex G-200 with 6.6-fold purification, which increased the specific activity of 71.3 U/mg of protein with a recovery rate of 48.2 %. On the SDS-PAGE chromatogram, the apparent molecular mass of the isolated enzyme was 48 kDa, and its highest activity was observed at pH 8 and 35 °C. The enzyme was catalytically stable within the pH range of 6.0-9.0 and below 40 °C. This study demonstrates that isolated L-methioninase is particularly efficient against tumour cell lines in vitro. The crude and purified L-methioninase inhibited 60 and 80 % of the growth of the breast cancer cell line (MCF-7), respectively, with an estimated IC = 12.6 μg/ml (crude) and IC = 5.0 μg/ml for purified L-methioninase from isolate 8 with accession no MZ675362. Because of this, pure L-methioninase has better catalytic characteristics and significant thermal stability, which could be used as a cancer-fighting substance than the enzyme purified from other sources.
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http://dx.doi.org/10.1016/j.sjbs.2023.103870 | DOI Listing |
Sci Rep
November 2024
Enzymology and Fungal Biotechnology Lab, Botany and Microbiology Department, Faculty of Science, Zagazig University, Zagazig, 44519, Egypt.
Aspergillus flavipes L-methionine γ-lyase (MGL) has been authenticated as a powerful anticancer agent towards various solid tumors, however, the catalytic efficiency and stability of this enzyme remains the main challenge for its further in vivo applications. Thus, the objective of this study was to enhance the catalytic efficiency, structural stability of A. flavipes MGL, in addition to boost their anticancer activity, via conjugation with β-cyclodextrin.
View Article and Find Full Text PDFSaudi J Biol Sci
December 2023
Botany Department, Faculty of Science, Mansoura University, Mansoura 35516, Egypt.
Bioactive components derived from medicinal herbs have recently acquired popularity due to their efficacy in treating various ailments, including cancer and infectious diseases. In this study, the anticancer enzyme, L-methioninase isolated from medicinal plants endophytic fungi, evaluated its promising therapeutic agents against different types of human cancers. L methionine was purified using column chromatography with the stationary phase of Sephadex G-200 with 6.
View Article and Find Full Text PDFPak J Pharm Sci
July 2023
Microbial Chemistry Department, National Research Centre, Cairo, Egypt.
Streptomyces MDMMH4 cells were immobilized in various matrices with two different techniques for the enhanced and semi-continuous production of extracellular L-methioninase. Of these, agarose was proven to be the most suitable matrix for the immobilization of cells. The optimal agarose concentration was approximately 3% and the initial cell concentration was 150mg/ml (wet cell weight).
View Article and Find Full Text PDFSaudi J Biol Sci
July 2023
Botany and Microbiology Deparetment, Faculy of Science, Zagazig University, Zagazig, Egypt.
A soil inhabiting sp. has been examined for producing L- methionine gamma-lyase enzyme. The identity of the tested bacteria was verified by VITEK2, and MALDI-TOF analysis in addition to molecular confirmation by 16S rDNA sequence and submitted in Genbank under accession number Production of the targeted enzyme was done using a commercial medium including L-methionine, as the main substrate.
View Article and Find Full Text PDFMicrob Cell Fact
January 2023
Microbial Chemistry Department, National Research Centre, Dokki, Cairo, 12622, Egypt.
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.
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