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Catalytic Properties of Enzymes

In many ways, biocatalysts like Guest Posting and general catalysts share the same characteristics amlon group. The amount may be small, but catalytic effectiveness is very high. Enzymes, like general catalysts and enzymes in particular, can change only the rate of chemical reaction, but not their equilibrium. Enzymes do not alter before or after the reaction. This means that a relatively small amount of enzyme can be used to catalyze a rapid change in substrate. The enzymes can decrease the activation energies of a reaction but not the change in free energy (3G). This allows the reaction time to be shortened and the energy exchanged during the process.

Catalysis by enzymes is unique compared to general catalysts.

1. Catalysis by enzymes with high efficiency

Enzymes have a much greater catalytic ability than chemical catalysts. Catalase, which contains Fe2+, and inorganic ferrous ions catalyze hydrogen peroxide decomposition as shown below. In 1 minute, 1 mol catalase is able to catalyze 5×106 moles of H2O2. In the same conditions 1 mol Fe2+ chemical catalyst can only decompose 6×10-4 moles of H2O2. Catalase has a catalytic activity about 1010 more efficient than Fe2+.

Turnover number is a way to express the level of catalytic efficacy of an enzyme. When the concentration of substrate is high enough, the conversion number is the number per enzyme of molecules which can catalyze a chemical reaction on the substrate. Catalase’s conversion number can be calculated using the above data. It is 5×106. Most enzymes have a conversion number between 1,000 and 106.

2) High Specificity of Enzyme Catalysis

A specific type of substance or enzyme is the only one that can act. The specificity of the enzyme’s action is reflected in this. For example, glycosidic bonds, ester bonds, peptide bonds, etc. Acid-base catalysis can hydrolyze chemical bonds, but these enzymes are all different. These are glycosidase, esterases and peptidases that are specific to each other. Natural enzymes can hydrolyze it.

Enzymes catalyze mild reaction conditions

In general, mild conditions are required for enzymatic reactions, such as normal temperatures, pressures, and pH levels. Enzymes are proteins and are susceptible to losing their activity when exposed to high temperatures, alkalis, or strong acids. Enzymes are sensitive to external changes and can be easily inactivated and denatured. Therefore, it is important that the conditions of the application are strictly controlled.

The ability to adjust enzyme activity

Comparing enzyme catalysis to chemical catalysts is the fact that it can have its activity automatically controlled. Organisms undergo a wide range of chemical reactions, but they all follow a very orderly and coordinated pattern. The enzyme catalytic activities can be affected by changes in the concentration of substrate, product, and environment conditions. This will control and coordinate biochemical reactions. In the event of a biochemical imbalance, the organism will be prone to disease and even die in extreme cases. Organisms evolved a system to automatically control enzyme activity to maintain life and adapt to environmental changes. Many ways exist to control enzymes. These include inhibitor regulation and feedback regulation.

The catalytic activities of enzymes are related to the coenzyme group, metal ion and prosthetic group

The catalytic activities of some enzymes is closely linked to their small molecules, which include cofactors, metal ions, and coenzymes. The enzyme’s activity is lost if they are removed.