Guest Posting as biocatalysts they are very similar to general catalysts amlon group. In this case, the catalyst efficiency may be high despite the small amount. The same as general catalysers, enzymes are only able to change the speed, and not equilibrium, of chemical processes. Since the enzyme is not changed before or after a reaction, the low amount in the cells can still catalyze many substrates to be converted in a very short period of time. Enzymes may reduce the activation, but will not alter the 3-G free energy changes during the reactions. They can speed up the response and decrease the time it takes to achieve equilibrium.

Comparing enzyme catalysis to other catalysts, it shows distinct characteristics.

1. Highly efficient enzyme catalysis

Chemical catalysts are not as effective at catalyzing reactions like enzymes. Inorganic iron and catalase with Fe2+ can both catalyze decomposition of hydrogen peroxide. One mol (or lb) of catalase catalyzes the breakdown of up to 5×106 mol H2O2 per minute. A chemical catalyst Fe2+ is only able to catalyze 6×10-4 of H2O2 under similar conditions. Comparing the two catalytic efficiencies, catalase’s is 1010-times more effective than Fe2+.

Using the turnover number, you can express how efficient an enzyme is at catalyzing chemical reactions. This number represents the amount of enzyme molecules required to catalyze chemical changes in the substrate when it is sufficiently concentrated. The conversion number for catalase is estimated to be approximately 5×106 based on the data presented. Many enzymes convert around 1,000 units, while the biggest can be over 106.

2. High specificity enzyme catalysis

The enzyme will only work on certain types or substances. That is what we call the specificity in enzyme action. For example, glycosidic bonds, ester bonds, peptide bonds, etc. The acid-base catalyst can hydrolyze the chemical bonds but they are hydrolyzed differently by different enzymes. It is the glycosidases and esterases that hydrolyze these chemical bonds. The enzymes in nature can also hydrolyze the protein.

3.The mild reactions catalyzed through enzymes

The conditions that are most conducive to enzymatic reaction include normal temperature, normal air pressure, and neutral pH. As enzymes contain proteins, the environment can affect their ability to function. This includes high temperatures, strong acids, and even alkalis. The reaction conditions during application must be carefully controlled because enzymes react more readily to environmental changes.

4. Adjustability of the enzyme activity

Another advantage of enzyme-catalysis over chemical catalysers is its ability to be controlled automatically. There are many types of chemical reaction in an organism, yet they are all very well coordinated. The catalytic enzyme activity is affected by environmental factors such as changes in product and substrate concentrations. The imbalance and disorder of biochemical reactions can cause disease in an organism or, even worse, death. As organisms evolve, they have developed systems that regulate enzyme activity automatically. They do this to keep up with changes in environment and to maintain normal living activities. It is possible to control enzymes in several ways: inhibitor regulation (controlling the activity of an enzyme), feedback regulation (regulating covalent modifications), zymogen-activation and hormonal control.

5. Catalytic enzyme activity depends on coenzyme and its prosthetic groups, as well as metal ions.

The cofactors and metal ions in coenzymes and some complex proteins are directly linked to the catalytic function of enzymes. When they are taken out, enzyme activity decreases.