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Techniques to measure lipase and esterase activity in vitro
1Department of Cell Biology, CIHR Group in Molecular and Cell Biology of Lipids, #328 HMRC, University of Alberta, Edmonton, Alta., Canada T6G 2S2.
Methods (San Diego, Calif.)
|May 17, 2005
Summary
This study reviews lipases and esterases, ubiquitous enzymes found across nature. It details common in-solution assay protocols, focusing on those measuring triacylglycerol hydrolysis activity.
Area of Science:
- Biochemistry
- Enzymology
Background:
- Lipases and esterases are a large, diverse enzyme class found in bacteria, fungi, and animals.
- These enzymes act on a wide range of structurally varied substrates.
- Numerous in vitro assays exist to measure their activity.
Purpose of the Study:
- To provide an overview of lipases and esterases.
- To present protocols for common solution-based assays.
- To emphasize assays for triacylglycerol-hydrolyzing enzymes.
Main Methods:
- Literature review of enzyme properties and assays.
- Description of established solution-based assay protocols.
- Focus on assays specific to triacylglycerol hydrolysis.
Main Results:
- Comprehensive overview of lipase and esterase families.
- Detailed protocols for standard enzymatic assays.
- Specific attention to assays for triacylglycerol lipases.
Conclusions:
- Lipases and esterases are crucial enzymes with diverse functions.
- Standardized assay methods are essential for their characterization.
- The presented protocols facilitate the study of triacylglycerol hydrolysis.