ArticleJournal of biotechnology2013
Engineering Escherichia coli for soluble expression and single step purification of active human lysozyme.
Article in Journal of biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- A Revised Model for Muscarine Biosynthesis Involving Lysine Trimethylation.Angewandte Chemie (International ed. in English) · 2026Article
- Expression of BSN314 lysozyme genes in Escherichia coli BL21: a study to demonstrate microbicidal and disintegarting potential of the cloned lysozyme.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Computational design and experimental characterisation of a stable human heparanase variant.RSC chemical biology · 2022Article
- Synthetic Liposomal Mimics of Biological Viruses for the Study of Immune Responses to Infection and Vaccination.Bioconjugate chemistry · 2020Article
- Revisiting Escherichia coli as microbial factory for enhanced production of human serum albumin.Microbial cell factories · 2017Article
- Efficient soluble expression of disulfide bonded proteins in the cytoplasm of Escherichia coli in fed-batch fermentations on chemically defined minimal media.Microbial cell factories · 2017Article
- Genetically enhanced lysozyme evades a pathogen derived inhibitory protein.ACS chemical biology · 2015Article
- Engineering cells to improve protein expression.Current opinion in structural biology · 2014Review
- The Natural Antimicrobial Enzyme Lysozyme is Up-Regulated in Gastrointestinal Inflammatory Conditions.Pathogens (Basel, Switzerland) · 2014Review
- Bioengineered lysozyme reduces bacterial burden and inflammation in a murine model of mucoid Pseudomonas aeruginosa lung infection.Antimicrobial agents and chemotherapy · 2013Article
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Authors and funding
3 authors.
Funding
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 as well as harness the lysozyme inhibitory protein, Ivy. Our strategy exploits E. coli's ease of culture, short doubling time, and facile genetics to yield upwards of 30 mg/l of soluble lysozyme in a bioreactor system, a 3000-fold improvement over prior efforts in E. coli. Additionally, molecular interactions between lysozyme and a his-tagged Ivy allows for one-step purification by IMAC, yielding as much as 21 mg/l of purified enzyme. We anticipate that our expression and purification platform will facilitate further development of engineered lysozymes having utility in disease treatment and other practical applications.
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