Determination of Lipase Activity by a Rhodamine-Triglyceride-Agarose Assay
1994; Elsevier BV; Volume: 219; Issue: 2 Linguagem: Inglês
10.1006/abio.1994.1265
ISSN1096-0309
Autores Tópico(s)Diabetes Management and Research
ResumoA quantitative fluorescence lipase assay based on the interaction of rhodamine B with fatty acids released during the enzymatic hydrolysis of triglycerides is described. The assay is linear over the range of 0.5-2 mM oleic acid and 0.05-1 μg pure lipase. The method allows flexibility in the choice of substrate. A large number of samples can be assayed simultaneously, making it practical for assaying lipase activity in column fractions during purification. The substrate profiles of Geotrichum candidum lipase obtained by both a titrimetric assay and the RTA assay indicated the highest activity against triolein. The method is rapid and can be further automated.
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