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Purification, properties and reactivity of the esterase from Micrococcus sp
1Chemical Technology Research Laboratories, Daiichi Pharmaceutical Co., Ltd., Tokyo, Japan.
Biological & Pharmaceutical Bulletin
|July 17, 1999
Summary
A Micrococcus sp. esterase was purified and characterized. This enzyme selectively hydrolyzes a specific fluorinated ester, showing consistent enantioselectivity compared to the crude enzyme.
Area of Science:
- Biochemistry
- Enzymology
Background:
- Esterases are crucial enzymes involved in various biological processes.
- Micrococcus sp. esterase shows enantioselective hydrolysis of specific substrates.
Purpose of the Study:
- To highly purify and characterize the esterase from Micrococcus sp.
- To investigate the enzyme's properties and enantioselectivity for n-propyl-2-fluorocyclopropanecarboxylate.
Main Methods:
- Purification using three types of chromatography.
- Enzyme characterization including molecular weight determination.
- Assessment of enzyme activity and inhibition studies.
Main Results:
- The esterase was highly purified and found to be a monomer with a molecular weight of approximately 35,000.
- The enzyme demonstrated esterase activity towards various aliphatic propyl esters.
- Inhibition by mercury (Hg) and diisopropyl fluorophosphate (DFP) was observed.
- The enantioselectivity for the target substrate remained consistent between the purified and crude enzyme preparations.
Conclusions:
- The purified Micrococcus sp. esterase is a monomeric enzyme with broad esterase activity.
- The enzyme's enantioselectivity is maintained after purification.
- The enzyme's sensitivity to Hg and DFP suggests the presence of key active site residues.
