Hydrolysis of a model surfactant as measured using ACYL coenzyme a synthetase

Hydrolysis of a model nonionic surfactant, 1‐¹⁴C]methyl palmitate, was compared between porcine esterase and lipase using a new hydrolase assay. The assay incorporates acyl coenzyme A (CoA) synthetase to convert the hydrolytic product of methyl palmitate, palmitic acid, to its acyl CoA derivative; palmitoyl CoA is separated from unreacted substrate for quantitation by a highly efficient extraction. The assay achieves quantitative separation between product and substrate due to the high water solubility of the acyl CoA derivative, eliminating the need for time‐consuming chromatographic separations. After 60 min under optimal conditions, only 20 U/mL porcine hepatic esterase hydrolyzed 93.6+0.9% of 20μM methyl palmitate, while 100U/mL porcine pancreatic lipase was required to hydrolyze only 82.3 ±0.7% of the same substrate. While both enzymes detoxified the surfactant, esterase was more efficient, possibly indicating preferential specificity for simple monoesters; generally selective for endogenous triacylglycerols, lipase may be less specific for surfactants. However, together both enzymes may enable mammals to hydrolyze ingested nonionic surfactants from oil spill dispersants, reducing their toxicity.