| Literature DB >> 8080082 |
Abstract
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.Entities:
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Year: 1994 PMID: 8080082 DOI: 10.1006/abio.1994.1265
Source DB: PubMed Journal: Anal Biochem ISSN: 0003-2697 Impact factor: 3.365