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Evolution of a thermostable luciferase for application in ATP assays Rita R. Hannah*; MP Hall; MT Beck; KV Wood Promega Corp, 2800 Woods Hollow Road, Madison, WI 53711-5399, USA      *(rhannah@promega.com) Firefly luciferase purified from Photinus pyralis has been used extensively in ATP assays. However, the enzyme has only moderate stability in vitro and is sensitive to its chemical environment, for example pH and detergents. This has limited its ability to be used in developing robust homogeneous ATP assays. Another firefly luciferase from Photuris pennsylvanica was evolved under select conditions to evolve an enzyme with properties intended to improve performance in ATP assays. Primarily, selection was targeted towards increased thermostability and resistance to degradation products of luciferin, which inhibit luciferase activity. A study of the physical and biochemical characteristics of the thermostable mutant revealed better performance characteristics in comparison to the commonly used luciferase from P. pyralis. The unique characteristics of this mutant enabled novel formulations for ATP assay reagents. These reagents are physically robust, and provide a sensitive and stable luminescent output. [Talk: hannah.ritar.78191]

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