Theoretical conditions to maximize enzymatic activity
August 24, 2023
Contribution to developing enzymes for food processing, pharmaceutical products and biofuels
RIKEN CSRS identified theoretical conditions to maximize enzymatic reaction rates.
Enzymes are proteins that accelerate specific chemical reactions. The magnitude of acceleration is referred to as enzymatic activity. Establishing a method to enhance this activity as much as possible is a critical issue in both bioengineering and basic science.
In this study, the research team derived a new equation representing enzymatic activity and mathematically determined conditions that maximizes the activity. Consequently, they theoretically concluded that the enzymatic activity is maximized when the Michaelis-Menten constant (Km), which represents the affinity between an enzyme and a substrate, is equal to the substrate concentration ([S]). In addition, the correlation between the Kms of natural enzymes and the concentrations of their intracellular substrates suggests that this principle of maximizing enzymatic activity also applies to nature. In the field of artificial catalysts, tuning the affinity between catalysts and substrates is a well-known approach to improve catalytic activities. The results of this study suggest that the activity of natural enzymes, which can be considered as biological catalysts, can also be enhanced by optimizing their affinities.
The findings of this study would contribute to developing new enzymes for food processing, pharmaceutical synthesis, and biofuel production.
- Original article
- Nature Communications doi: 10.1038/s41467-023-40471-y
- H. Ooka, Y. Chiba, R. Nakamura,
- "Thermodynamic Principle to Enhance Enzymatic Activity using the Substrate Affinity".
- Hideshi Ooka; Research Scientist
Yoko Chiba; Senior Scientist
Ryuhei Nakamura; Teal Leader
Biofunctional Catalyst Research Team