Hydrolytic Enzymes: Characteristics, Classification, Functions

The hydrolytic enzymes or hydrolases, are molecules that catalyze hydrolysis reactions (hydro = water; lysis = rupture), ie catalyzing a chemical reaction between a water molecule and other molecule.

Hydrolases, like most enzymes, are protein in nature, meaning that they are composed of one or more polypeptide or amino acid chains.

Enzymes are present in almost all biochemical reactions in living organisms. They are responsible for accelerating these reactions by reducing the energy level of the reaction.

For example, most digestive enzymes are hydrolytic. These are responsible for accelerating the breakdown of complex molecules in the bolus.

The decomposition results in simpler forms that are easy for organisms to absorb. Enzymes not only serve vital functions in organisms but are also of medical and economic importance.


Enzymes are generally large protein molecules with regulated activity. They all have a specific 3D shape. These work at low concentrations.

They are not modified during the reaction, so they can be recovered without changes in their molecular or protein structure. They can process substrates at a variable speed that can involve thousands of molecules per minute.

They are specific and can be denatured and / or be affected by changes in temperature, pH, concentrations of the substrates, among others.

For their part, hydrolytic enzymes are the largest group of known enzymes. There are more than 200 hydrolases that catalyze reactions that break Carbon – Oxygen, Carbon – Nitrogen, Carbon – Carbon, Phosphorus – Oxygen (Phosphoric Anhydride) bonds, even Phosphorous – Nitrogen bonds.

Other important characteristics of hydrolytic enzymes are their broad substrate specificity and that they are stereoselective.


The classification of hydrolytic enzymes is based primarily on the nature of the hydrolyzed bond, and the substrate. Taxonomic terminology calls this type of enzyme hydrolases or hydrolytic enzymes.

On the other hand, the common names of enzymes are made up of the suffix -ase , for example cholinesterase, esterases and proteases.

Finally, according to the International Union of Biochemistry and Molecular Biology, enzymes are classified by numbers called EC (enzyme commission).

Hydrolases belong to group 3 (EC3). These in turn are subdivided according to the type of bond that they hydrolyze. For example, if enzymes hydrolyze linear amides their number is EC3.5.1, and if they hydrolyze serine proteases their number is EC3.4.16.21.

Functions in the human body


Cholinesterase is one of the most important known hydrolytic enzymes. It hydrolyzes acetylcholine and converts it to choline and acetic acid.

This specific reaction acts after the transmission of the nerve impulse, stopping the action of the neurotransmitter molecules (acetylcholine).

Digestive enzymes

One of the most studied enzymatic reactions is that of the degradation of food in organisms. It is known that during digestion lipase enzymes are responsible for hydrolyzing lipids and proteases cause the breakdown of proteins to obtain amino acids.

Hydrolytic enzymes are responsible for breaking or dividing large molecules and converting them into simpler forms. These molecules obtained will be used in the synthesis, excretion of waste or as carbon sources for obtaining energy.

An outstanding characteristic of digestive hydrolytic enzymes is that they are extracellular and that they mix with food as they pass through the digestive tract.

These enzymes are produced by cells that line the stomach, intestine, and other organs such as the pancreas.

Cellular digestion

Lysosomes are the main protagonists of cellular digestion. There are more than 50 specific hydrolytic enzymes contained within these cellular structures.

These enzymes fulfill the function of digesting complex organic matter, turning it into simpler molecules, for example as: monosaccharides or amino acids.




The technological and scientific advances of the last 20 years have led to important discoveries in the molecular field of the mechanisms of operation of compounds.

Of the six types of known enzymes, the hydrolytic ones are the most used (60%) in the biocatalytic processes of the pharmaceutical industry.

Lipases are hydrolytic enzymes that transform triacylglycerol to glycerol and free fatty acids. These enzymes are used, in the pharmaceutical industry, to develop prophenes (anti-inflammatory drugs) that act against rheumatoid diseases, arthritis, lower back pain, etc.

Other lipases are used to develop compounds such as chiral synthon (an antifungal) and lotrafiban, which is a drug used to prevent thrombotic episodes.


Currently, hydrolases are essential enzymes in the production of various food products, due to the multiple applications they have in almost all industrial processes today.

An area of ​​interest related to the use of hydrolytic enzymes is the synthesis or production of lignocellulosic biomass. This biomass has great potential in the industry to obtain biofuels.

On the other hand, proteases, enzymes that catalyze the hydrolysis of peptide compounds, have a high application in the food industry, especially in the preparation of soy protein hydrolysates.

They also serve to improve the quality of breads, in sweeteners, in reducing the bitter flavors of different foods, even as meat tenderizers.

The agricultural industry uses pectinases. These are a group of enzymes capable of breaking down highly branched acidic and neutral polymers (pectin groups) found in the cell wall of plants. 

The most widely used pectinases at the industrial agricultural level come from the microorganism called Aspergillus niger and are used for fermentation in submerged cultures and fermentation of solid substrates.

Pectinases are also used in the production of fruit juices or juices and serve to lower turbidity or clarify, improving their quality. They also use them for the production of jams and fruit pulps.


Digestive proteases have been known to clean clothes since the beginning of the last century. By the end of the last century, most detergents contained digestive enzymes such as amylases and lipases.

It is well known that the use of these enzymes in the detergent industry makes the washing process more efficient. They reduce the use of water, are biodegradable and ensure total cleaning.

Bacillus licheniformis   and Aspergillus flavus produce proteases used for the production of detergents. The product obtained is used to remove stains of protein origin such as blood for example.

Fungi produce cellulases. Cellulases serve as a detergent to remove soil stains or plant debris. Other enzymes such as lipases are used to remove stains of oleic origin such as grease or lipstick. The fungus Aspergillus oryzae is used industrially to produce these enzymes.


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