ArticleProtein expression and purification2015
Efficient in vitro refolding and functional characterization of recombinant human liver carboxylesterase (CES1) expressed in E. coli.
Article in Protein expression and purification, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Experimental and In Silico Approaches to Study Carboxylesterase Substrate Specificity.Journal of xenobiotics · 2026Review
- In vitro evaluation of novel SN-38 prodrug activated by α-rhamnosidase of exogenous enzyme.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2024Article
- Development of recombinant capsid protein-based single serum dilution ELISA for sero-detection of porcine circovirus type 2 infection in pigs.Veterinary research communications · 2024Article
- Expression and characterisation of human glycerol kinase: the role of solubilising agents and molecular chaperones.Bioscience reports · 2023Article
- Simple and Efficient Purification of Recombinant Proteins Using the Heparin-Binding Affinity Tag.Current protocols in protein science · 2017Article
- Human carboxylesterase 2: Studies on the role of glycosylation for enzymatic activity.Biochemistry and biophysics reports · 2016Article
- Comparison of the Structure and Activity of Glycosylated and Aglycosylated Human Carboxylesterase 1.PloS one · 2015Article
- The Role of Disulfide Bridges in the Interaction ofAvicenna journal of medical biotechnologyArticle
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Human liver carboxylesterase 1 (CES1) plays a critical role in the hydrolysis of various ester- and amide-containing molecules, including active metabolites, drugs and prodrugs. However, it has been problematic to express recombinant CES1 in bacterial expression systems due to low solubility, with the CES1 protein being mainly expressed in inclusion bodies, accompanied by insufficient purity issues. In this study, we report an efficient in vitro method for refolding recombinant CES1 from inclusion bodies. A one-step purification with an immobilized-metal affinity column was utilized to purify His-tagged recombinant CES1. Conveniently, both denaturant and imidazole can be removed while the enzyme is refolded via buffer exchange, a dilution method. We show that the refolding of recombinant CES1 was successful in Tris-HCl at pH 7.5 containing a combination of 1% glycerol and 2 mM β-mercaptoethanol, whereas a mixture of other additives (trehalose, sorbitol and sucrose) and β-mercaptoethanol failed to recover a functional protein. His-tagged recombinant CES1 retains its biological activity after refolding and can be used directly without removing the fusion tag. Altogether, our results provide an alternative method for obtaining a substantial amount of functionally active protein, which is advantageous for further investigations such as structural and functional studies.
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