Department of Biology, Faculty of Basic Sciences and Engineering, Gonbad Kavous University, Gonbad Kavous, Iran.
Int J Biol Macromol. 2024 Jan;254(Pt 2):127782. doi: 10.1016/j.ijbiomac.2023.127782. Epub 2023 Nov 3.
Thermodynamic and kinetic parameters, such as enthalpy, entropy, and free energy, are crucial in evaluating enzyme stability and activity. These parameters, including the free energy of activation (ΔG) and the Gibbs free energy of inactivation (ΔG*), are important for predicting energy requirements and reaction rates. However, relying solely on these parameters is insufficient in selecting an enzyme for industrial processes. Numerous studies have explored the measurement of thermodynamic parameters for proteases. Unfortunately, some of the definitions and calculations of key parameters such as ΔG, ΔG*, and substrate-binding free energy have contained significant errors. In this study, these mistakes have been addressed and corrected. Additionally, a new parameter called δ, defined as the difference between ΔG* and ΔG, has been introduced for the first time. It is argued that δ provides a more reliable measure for predicting the potential industrial application of enzymes. The highest calculated value for δ was found to be 39.6 kJ·mol at 55 °C. Furthermore, this study also presents a comprehensive collection and determination of all thermodynamic and kinetic parameters for proteases, providing researchers and professionals in the field with a valuable resource to compare and understand the relationships between these parameters and the industrial potential of enzymes.
热力学和动力学参数，如焓、熵和自由能，对于评估酶的稳定性和活性至关重要。这些参数，包括活化自由能 (ΔG) 和失活吉布斯自由能 (ΔG*)，对于预测能量需求和反应速率非常重要。然而，仅依靠这些参数不足以选择用于工业过程的酶。许多研究都探讨了蛋白酶热力学参数的测量。不幸的是，一些关键参数（如 ΔG、ΔG和底物结合自由能）的定义和计算存在重大错误。在本研究中，已经解决并纠正了这些错误。此外，首次引入了一个名为 δ 的新参数，定义为 ΔG和 ΔG 之间的差值。有人认为，δ 提供了一种更可靠的方法来预测酶的潜在工业应用。在 55°C 时，δ 的计算值最高为 39.6 kJ·mol。此外，本研究还全面收集和确定了所有蛋白酶的热力学和动力学参数，为该领域的研究人员和专业人员提供了一个有价值的资源，可用于比较和理解这些参数与酶的工业潜力之间的关系。
