Engineering Escherichia coli for soluble expression and single step purification of active human lysozyme.

ABSTRACT: Genetically engineered variants of human lysozyme represent promising leads in the battle against drug-resistant bacterial pathogens, but early stage development and testing of novel lysozyme variants is constrained by the lack of a robust, scalable and facile expression system. While wild type human lysozyme is reportedly produced at 50–80 kg per hectare of land in recombinant rice, this plant-based system is not readily scaled down to bench top production, and it is therefore not suitable for development and characterization of novel lysozyme variants. Here, we describe a novel and efficient expression system capable of producing folded, soluble and functional human lysozyme in Escherichia coli cells. To achieve this goal, we simultaneously co-express multiple protein folding chaperones

SUBMITTER: Lamppa JW 

PROVIDER: S-EPMC3594478 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature