A rapid modified gas chromatographic assay for esterase activity

Area of Science:

• Biochemistry
• Analytical Chemistry

Background:

• Esterase activity is crucial in various biological processes.
• Accurate and efficient determination of esterase activity is essential for biochemical research.

Purpose of the Study:

• To develop a rapid, modified gas chromatographic procedure for esterase activity determination.
• To identify optimal substrates and solvents for the assay.

Main Methods:

• Utilized aliphatic esters (ethyl n-butyrate, n-propyl n-butyrate, n-butyl n-butyrate, n-amyl n-butyrate) as substrates.
• Employed acetone as the solvent to prevent alcoholysis.
• Initiated the enzyme reaction in a 0.03 M phosphate buffer (pH 7.90) and analyzed products via gas chromatography.

Main Results:

• A modified gas chromatographic method for esterase activity was successfully established.
• Acetone proved to be the most suitable solvent, avoiding substrate alcoholysis.
• The procedure allowed for direct injection and separation of produced alcohols.

Conclusions:

• The developed method offers a rapid and reliable approach for quantifying esterase activity.
• This technique enhances biochemical analysis by providing efficient esterase determination.