What is the most commonly employed method of assay for lipase?

The most commonly employed method for lipase assay is based on peroxidase coupling. This method utilizes the enzymatic activity of lipase to hydrolyze triglycerides into glycerol and free fatty acids. The glycerol is then converted to a product that can be detected using peroxidase, which catalyzes the oxidation of a substrate (such as a chromogen) resulting in a measurable color change. This approach is sensitive, provides rapid results, and is well-suited for clinical laboratories.

Peroxidase coupling is particularly advantageous because it allows for a clear endpoint measurement that correlates directly with lipase activity, making it easy to quantify levels in clinical samples. The straightforward nature of this method also contributes to its widespread adoption for routine lipase testing.

Alternative methods, while useful in certain contexts, are either not as commonly employed for routine testing of lipase or are specialized techniques that may not offer the same level of convenience and practicality in a clinical setting.