Author : Abdulameer Hamzah, Nazar
journal of kerbala university,
Volume 8, Issue 0, Pages 315-322
Caper protease showed maximum activity at pH 6.0 when it was determined at various pH’s while it was no activity in pH 9.0 and 9.5. No effect of chelating agent (EDTA) on activity where as reducing reagent (Cysteine) showed perceptible effect typically at 0.7 mM. Protease was purified by (NH4)2SO4 precipitation, CM Cellulose ion exchange and Sephadex G100 size exclusion. Purification fold for three steps were 1.33, 1.96 and 4.26, respectively. The inhibitor E64 gave complete inhibition compared with other inhibitors. Finally activation energy of thiol protease to convert and denaturation were 37.24 kJ mole-1 and 129.47 respectively.