A Recurring Misconception Regarding the Fitting and Plotting of Enzyme Kinetics Data Leads to the Loss of Significant Reaction Parameters and Rate Constants

In recent years, an increasing number of published articles on biocatalysis have reported new enzymes that exhibit biotechnologically interesting catalytic activities. Some authors rush to publish their work in an attempt to ensure “novelty” and often present their results with various types of graphs, such as scatter plots or line-and-symbol plots using nonexistent parameters as ordinates, e.g., “Relative Activity (%)” and the like, vs. abscissae such as pH value, temperature, etc. Nevertheless, in vitro enzyme kinetics remains a valuable tool for understanding, optimizing, and effectively applying these biocatalysts under diverse reaction conditions, taking advantage of all available experimental results. This work aims to emphasize the importance of processing experimental data from enzymatic reactions through appropriate fitting with known kinetic equations and to discourage the use of nonexistent parameters. To support this integrated approach, specific examples are provided for the calculation of significant kinetic and thermodynamic parameters, as well as rate constants.