Investigating Functional and Folding Stability of an Engineered <i>E. coli</i> L-asparaginase Harboring Y176F/S241C Mutations.

ABSTRACT:

Purpose

L-asparaginase has been widely recognized as a critical component in the treatment of various types of lymphoproliferative disorders, since its introduction in 1960s. However, its use in some cases leads to allergic reactions rendering the continuation of treatment unfeasible. Thus, the development of L-asparaginase from alternative sources or the production of engineered enzymes have always been considered. This study aimed to produce and evaluate a novel enzyme designed based on the sequence of L-asparaginase from Escherichia coli bacteria with Y176F/S241C mutations.

Methods

The Y176F/S241C mutant L-asparaginase was successfully expressed as the GST-fusion protein in E. coli, and then was subjected to affinity and size exclusion chromatography. The ac

SUBMITTER: Dastmalchi M 

PROVIDER: S-EPMC11530880 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature