Recombinant l-Asparaginase II from Lactobacillus casei subsp. casei ATCC 393 and Its Anticancer Activity.

ABSTRACT: l-asparaginases from bacterial origin are employed extensively in leukemic treatment and food industry. The present study focuses on the characterization of the recombinant l-asparaginase II from Lactobacillus casei subsp. casei ATCC 393 cloned into Escherichia coli expression system and purified using Ni-NTA chromatography. The recombinant l-asparaginase as a monomer had a molecular weight of 35 kDa. The enzyme was active from 10 to 80 °C with the optimum at 40 °C. The enzyme retained its activity at 28 °C and 37 °C up to 24 h. The enzyme had optimum pH of 6 and retained 50% activity till 18 h. The K_m of the recombinant enzyme was 0.01235 mM and V_max 1.576 mM/min. The half life of recombinant l-asparaginase II in human serum was 44 h and trypsin

SUBMITTER: Aishwarya SS 

PROVIDER: S-EPMC6646611 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature