HighlightsExpression of recombinant human carboxylesterase I in E.
coli is mainly insoluble.Refolding using a combination of 1% glycerol and 2 mM β-mercaptoethanol in Tris–HCl, pH 7.5 significantly improved solubility.Purified recombinant human CES1 is functionally active and stable.We provided efficient method to produce large amount and catalytically active CES1.
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