Bacterial L-Methioninase Enzyme and it's Prospective Application as Anticarcenomic Agent
Sabah Abo El Maaty Ahmed, Hamed Mohamed El Shora, Mervat Gameel Hassan
L-methioninase was isolated and purified from Staphylococcus sciuri using ammonium sulphate, DEAE-cellulose, Sephadex G-200 and Q-Sepharose with specific activity of 168.7 U mg-1 protein and purification fold of 177.5. The SDS-PAGE exhibited a single band at 48 kDa and this confirms purity of the L-methioninase. Analysis of amino acids of the purified enzyme exhibited variation in the content of the amino acids. The most dominant amino acids were cysteine, aspartic acid, and methionine. The values of Vmax and Km of the purified enzyme were 33.3 U mg-1 protein and 1.7 mM. The optimal pH and the optimal temperature of the enzyme were 8.0 and 40 ºC. The phytohormones activated the L-methioninase with different rates. The four reagents of the active groups namely N-bromosuccinimide (NBS), butanedione (BD), N-ethylmaleimide (NEM) and N-trinitromethane (TNM) inhibited L-methioninase in a concentration-dependent manner confirming the necessity of tryptophanyl, arginyl, sulfhydryl and tyrosyl groups for L-methionine catalysis. L-methioninase exhibited appreciable anticancer effect against HeLa and MCF-7 cell lines.
Benha
Egypt
