The secret world of enzymes: overloading inhibits their effectiveness!

The secret world of enzymes: overloading inhibits their effectiveness!

Enzymes are essential biological catalysts that play a key role in the metabolism of all organisms, including plants and industrial processes. In a recent study by the Technical University of Munich (TUM) an important aspect of enzyme function was investigated. It turns out that many enzymes slow down their activity when overloaded, which can significantly affect both the effectiveness of drugs and the efficiency of industrial processes.

Researchers at TUM have studied the mechanism of substrate inhibition, a phenomenon in which enzymes work more slowly or even stop functioning altogether when confronted with a large number of molecules. This study is particularly relevant because about 20 percent of known enzymes show reduced activity in such situations, which is considered a significant obstacle in the biochemical reaction. Interestingly, beta-carotene, a well-known antioxidant, can help overcome the inhibition caused by high substrate concentrations.

Interruption of enzyme activity

Substrate inhibition can lead to inefficiency in food production and industrial cleaning processes by negatively affecting reaction rates. According to the Wikipedia page about Enzyme inhibition An inhibitor binds reversibly to an enzyme and reduces its activity. When an inhibitor enters the reaction, it can affect either the enzyme itself or the enzyme-substrate complex, the result being an altered reaction rate.

The interaction between enzyme, substrate and inhibitor is complex. With reversible inhibition, the balance between the different forms – enzyme, substrate and the complex of both – is crucial for the reaction kinetics. This in turn can be described by the Michaelis-Menten equation.

Beta-carotene as a potential therapeutic agent

TUM research shows that the effects of substrate inhibition are relevant not only to the body's metabolism, but also to the effectiveness of pharmaceutical products. High concentrations of active ingredients can lead to slower reactions, which is particularly important in drug development. Beta-carotene could provide valuable support by reducing the negative effects of overload and restoring enzymatic activity.

In summary, elucidating the mechanism of substrate inhibition is not only important for biochemistry and medicine, but could also have far-reaching applications in food engineering and industrial processes. The discovery of beta-carotene as a potential supporter leaves a positive impression in ongoing research into the optimization of enzymatic processes.