As all these approaches are readily compatible with continuous reaction monitoring and high-throughput experimentation, the PUB module is a remarkably useful tool for kinetic studies and enzyme characterization, as we demonstrated with selected use-cases. For instance, we assessed the thermal stability of the IPP from Geobacillus stearothermophilus and found the value determined through kinetic experiments to be in excellent agreement with the noisy obtained via differential scanning fluorimetry (Fig. ). As the ∆ between 1a and 1b is not temperature-dependent and Y02 readily allows experimentation up to at least 60 °C (see the SI for details), we used the PUB module to obtain Eyring plots for the IPPcatalyzed pyrophosphate hydrolysis (Fig. ). This analysis revealed the presence of a moderate activation heat capacity change ∆ * across different conditions, which would have been impossible or extremely laborious to examine with existing phosphate detection methods. In a similar manner, the PUB module allowed the straightforward characterization of an alkaline phosphatase with a series of model substrates 2a-2d (Figs. and). Notably, these experiments could routinely be performed in a multi-well format running more than 30 reactions in parallel.