Purification and characterization of L-arginine deiminase from Penicillium chrysogenum.

ABSTRACT: L-arginine deiminase (ADI, EC 3.5.3.6) hydrolyzes arginine to ammonia and citrulline which is a natural supplement in health care. ADI was purified from Penicillium chrysogenum using 85% ammonium sulfate, DEAE-cellulose and Sephadex G₂₀₀. ADI was purified 17.2-fold and 4.6% yield with a specific activity of 50 Umg^- 1 protein. The molecular weight was 49 kDa. ADI expressed maximum activity at 40^oC and an optimum pH of 6.0. ADI thermostability was investigated and the values of both t_0.5 and D were determined. K_d increased by temperature and the Z value was 38^oC. ATP, ADP and AMP activated ADI up to 0.6 mM. Cysteine and dithiothreitol activated ADI up to 60 µmol whereas the activation by thioglycolate and reduced glutathione (

SUBMITTER: El-Shora HM 

PROVIDER: S-EPMC10829382 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature