Purification, characterization and anticancer evaluation of l-methioninase from Trichoderma harzianum.

ABSTRACT: The Trichoderma harzianum l-methioninase was purified 7.15-fold with a recovery of 47.9% and the specific activity of 74.4 U/mg of protein. The purified enzyme has an apparent molecular mass of 48 kDa on SDS-PAGE and exhibited maximum activity at pH 8 and 35 °C. The enzyme was catalytically stable below 50 °C and at a pH range of 6.0-8.5. The thermal inactivation of l-methioninase exhibited first-order kinetics with the k value between 5.71 × 10^-4 min^-1 and 1.83 × 10^-2 min^-1. The studies on thermodynamic parameters of l-methioninase indicated the compaction and aggregation of the enzyme molecule during denaturation. This is the first report of thermodynamic analysis of thermal inactivation in l-methioninase. The enzyme activity was

SUBMITTER: Salim N 

PROVIDER: S-EPMC7606426 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature