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Determination of Lipase Activity by a Rhodamine-Triglyceride-Agarose Assay

โœ Scribed by J.F. Jette; E. Ziomek

Publisher
Elsevier Science
Year
1994
Tongue
English
Weight
388 KB
Volume
219
Category
Article
ISSN
0003-2697

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โœฆ Synopsis

A 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 microgram 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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