Arginine deaminase from Pseudomonas aeruginosa PS2: purification, biochemical characterization and in-vitro evaluation of anticancer activity.

ABSTRACT: In the present study, arginine deaminase (ADI) was purified from Pseudomonas aeruginosa PS2 which showed relative molecular mass of 70 ± 3 kDa on native-PAGE and 36 ± 0.5 kDa on SDS-PAGE. Purified ADI exhibited optimum activity at pH 6.5 and temperature 40 ºC. Metal ions, K⁺ and Mg²⁺ had positive, while Mn²⁺, Cr²⁺, Co²⁺, Fe³⁺, Ni²⁺, Cu²⁺, Cd²⁺ and Hg²⁺ had negative effects on catalytic activity of ADI. Purified enzyme showed high substrate specificity towards natural substrate L-arginine and did not hydrolyse its structural analogues. In-vitro serum half-life of purified ADI was 40 h, whereas proteolytic half-life was 28, 27, and 32 min against trypsin, elastase-I and

SUBMITTER: Bala K 

PROVIDER: S-EPMC7196117 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature