Abstract
A rapid modified procedure for the gas chromatographic determination of esterase activity was studied. Aliphatic esters such as ethyl n-butyrate, n-propyl n-butyrate, n-butyl n-butyrate and n-amyl n-butyrate were used as substrates and acetone waschosen as the most suitable solvent for dissolving the substrates in order to avoid alcoholysis. The enzyme reaction was started in a mixture of 0.03 M phosphate buffer, pH 7.90, containing an adequate amount of an internal standard and the substrate solution in acetone. At define intervals, an aliquot of the reaction solution was injected directly on to a gas chromatograph and the alcohols produced were separated.
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