ArticleScientific reports2024
Stability of immobilized L-arginine deiminase from Penicillium chrysogenum and evaluation of its anticancer activity.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The aim of the present work was to immobilize L-arginine deiminase on suitable supports such as chitosan, alginate, and silica gel to study its stability. Additionally, the study aims to investigate the anticancer effects of the free purified enzyme on hepatocellular carcinoma (Hep-G2) and breast cancer (MCF-7) cell lines. L-arginine deiminase (ADI: EC 3.5.3.6) was immobilized on chitosan, Ca-alginate, and silica gel, with immobilization efficiencies of 89.0%, 72.8%, and 66.5%, respectively. The optimal immobilization time for the highest efficiency was 4 h. Increasing the concentration of glutaraldehyde improved the immobilization efficiency of ADI on chitosan. The chitosan-immobilized ADI retained about 45% of its activity after 8 cycles. The optimal pH values were 6 for the free purified ADI and 7 for the chitosan-immobilized ADI. The optimal temperature increased from 40 °C for the free enzyme to 45 °C after immobilization. The activation energies for the free and chitosan-immobilized enzymes were 71.335 kJ/mol and 64.011 kJ/mol, respectively. The K
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