Chemiluminescence assay of lipase activity using a synthetic substrate as proenhancer for luminol chemiluminescence reaction

Luminescence : the Journal of Biological and Chemical Luminescence
Tomoko IchibangaseNaotaka Kuroda

Abstract

A novel chemiluminescence (CL) assay method for lipase (triacylglycerol lipase, E.C.3.1.1.3) activity was developed by using the lauric acid ester of 2-(4-hydroxyphenyl)-4,5-diphenylimidazole (HDI) as a substrate. The method is based on the enhanced CL reaction of luminol-hydrogen peroxide-horseradish peroxidase (HRP) with HDI that is liberated from the substrate by enzymatic hydrolysis. To simplify the assay procedure, both the hydrolysis of the substrate and the enhanced CL reaction were performed in the same reaction mixture. Lipases from Candida cylindracea and porcine pancreas were successfully determined with the detection limits (blank signal + 3 SD) of 0.05 and 50.0 mU/tube, respectively. The method is simple and rapid, permitting the completion of single assay within 5 min. The reproducibilities obtained with replicate assays were relative standard deviations (RSDs) of <=> 4.7% for within-day and <=> 6.0% for between-day assays.

Citations

Jun 15, 2006·Analytical Chemistry·Kristin A FletcherIsiah M Warner
Aug 15, 2009·Journal of Microbiological Methods·Sylvain OrengaDavid H Pincus
Oct 6, 2005·Luminescence : the Journal of Biological and Chemical Luminescence·Tomoko IchibangaseNaotaka Kuroda
Feb 13, 2019·Luminescence : the Journal of Biological and Chemical Luminescence·Roberta Albino ReisFernando Heering Bartoloni

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