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Updated: Jul 16, 2026

Electricity-Free, Sequential Nucleic Acid and Protein Isolation
Published on: May 15, 2012
[Characterization of Escherichia coli esterase B after separation by chromatography]
Abstract:
Esterase B of Escherichia coli has been purified 56 fold with recovery of 39%. The apparent molecular weight as determined by gel filtration was approximately 57000. The pI as determined by isoelectric focusing was 4.6. This enzyme exhibited Michaelis-Menton kinetics with apparent Km of 0.25 mM for l-naphtyl acetate. It remained stable at 60 degrees C but was sensitive to pH values below 6. The esterase activity was completely inhibited by Di-isopropyl-fluorophosphate (DFP) but was resistant to iodoacetamide and to EDTA.
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