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Enzyme assays can be split into two groups according to their sampling method: continuous assays, where the assay gives a continuous reading of activity, and discontinuous assays, where samples are taken, the reaction stopped and then the concentration of substrates/products determined.
Fluorescein diacetate (FDA) hydrolysis assays can be used to measure the enzyme activity of microbes in a sample. A bright yellow-green glow is produced and is strongest when enzymatic activity is greatest. This can be quantified using a spectrofluorometer or a spectrophotometer.
In biochemical experiments, a chemical and/or physical property is chosen and the procedure that is used is specific to that property to derive more information about the sample, such as the quantity, purity, enzyme activity, etc. Spectrophotometry can be used for a number of techniques such as determining optimal wavelength absorbance of ...
After 5 minutes of incubation, the absorbance can be read at 595 nm using a spectrophotometer or a mobile smartphone camera (RGBradford method). [9] This assay is one of the fastest assays performed on proteins. [12] The total time it takes to set up and complete the assay is under 30 minutes. [13] The entire experiment is done at room temperature.
Absorbance detection has been available in microplate readers for more than 3 decades and is used for assays such as ELISA assays, protein and nucleic acid quantification or enzyme activity assays [2] (i.e. in the MTT assay for cell viability). [3]
The assay is terminated by the addition of a basic solution that stops the enzymatic reaction and deprotonates the liberated phenolic compound to produce the phenolate species. The cellulase activity of a given sample is directly proportional to the quantity of phenolate liberated which can be measured using a spectrophotometer.
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