Various chemical processes- the basis of the life of any organism. The main role in them is given to enzymes. Enzymes or enzymes are natural biocatalysts. In the human body they take an active part in the process of digestion of food, the functioning of the central nervous system and stimulation of new cell growth. By their nature, enzymes are proteins designed to accelerate various bio chemical reactions in organism. The breakdown of proteins, fats, carbohydrates and minerals are processes in which enzymes are one of the main active components.

There are quite a few types of enzymes, each of which is designed to act on a particular substance. Protein molecules are unique and cannot replace each other. They require a certain temperature range to be active. For human enzymes, the ideal temperature is normal body temperature. Oxygen and sunlight destroys enzymes.

General characteristics of enzymes

Being organic substances of protein origin, enzymes act on the principle of inorganic catalysts, accelerating reactions in the cells in which they are synthesized. A synonym for the name of such protein molecules is enzymes. Almost all reactions in cells occur with the participation of specific enzymes. They consist of two parts. The first is the protein part itself, represented by a protein of tertiary structure and called an apoenzyme, the second is the active center of the enzyme, called a coenzyme. The latter can be organic/inorganic substances, and it is it that acts as the main “accelerator” of biochemical reactions in the cell. Both parts form a single protein molecule called a holoenzyme.

Each enzyme is designed to act on a specific substance called a substrate. The result of the reaction that occurs is called the product. The names of the enzymes themselves are quite often formed on the basis of the name of the substrate with the addition of the ending “-ase”. For example, an enzyme designed to break down succinic acid (succinate) is called succinate dehydrogenase. In addition, the name of a protein molecule is also determined by the type of reaction it provides. Thus, dehydrogenases are responsible for the process of regeneration and oxidation, and hydrolases are responsible for the cleavage of chemical bonds.

The action of enzymes of various types is directed towards specific substrates. That is, the participation of protein molecules in certain biochemical reactions is individual. Each enzyme is associated with its own substrate and can only work with it. The apoenzyme is responsible for the continuity of this connection.

Enzymes can exist in a free state in the cytoplasm of the cell or interact with more complex structures. There are also certain types of them that act outside the cell. These include, for example, enzymes that break down proteins and starch. In addition, enzymes can be produced by various microorganisms.

A separate area of ​​biochemical science – enzymology – is intended for the study of enzymes and the processes occurring with their participation. For the first time, information about special protein molecules acting as catalysts appeared as a result of the study of digestive processes and fermentation reactions occurring in the human body. A significant contribution to the development of modern enzymology is attributed to L. Pasteur, who believed that all biochemical reactions in the body occur with the participation of exclusively living cells. The inanimate “participants” of such reactions were first announced by E. Buchner at the beginning of the 20th century. At that time, the researcher was able to determine that the catalyst in the process of fermentation of sucrose with the subsequent release of ethyl alcohol and carbon dioxide is a cell-free yeast extract. This discovery became a decisive impetus for a detailed study of the so-called catalysts of various biochemical processes in the body.

Already in 1926, the first enzyme, urease, was isolated. The author of the discovery was J. Sumner, an employee of Cornell University. After this, within one decade, scientists isolated a number of other enzymes, and the protein nature of all organic catalysts was finally proven. Today, the world knows over 700 different enzymes. But at the same time, modern enzymology continues to actively study, isolate and study the properties individual species protein molecules.

Enzymes: protein nature

Just like proteins, enzymes are usually divided into simple and complex. The former are compounds consisting of amino acids, such as trypsin, pepsin or lysozyme. Complex enzymes, as mentioned above, consist of a protein part with amino acids (apoenzyme) and a non-protein component, called a cofactor. Only complex enzymes can participate in bioreactions. In addition, like proteins, enzymes are mono- and polymers, that is, they consist of one or more subunits.

The general properties of enzymes as protein structures are:

• effectiveness, implying a significant acceleration of chemical reactions in the body;
• selectivity to the substrate and type of reaction performed;
• sensitivity to temperature, acid-base balance and other nonspecific physicochemical factors of the environment in which enzymes operate;
• sensitivity to the action of chemical reagents, etc.

The main role of enzymes in the human body is the conversion of some substances into others, that is, substrates into products. They act as catalysts in more than 4 thousand biochemical vital reactions. The functions of enzymes are to direct and regulate metabolic processes. As inorganic catalysts, enzymes can significantly accelerate forward and reverse bioreactions. It is worth noting that when they act chemical equilibrium is not violated. The reactions that occur ensure the breakdown and oxidation of nutrients entering the cells. Each protein molecule can perform a huge number of actions per minute. At the same time, the enzyme protein, reacting with various substances, remains unchanged. The energy generated during the oxidation of nutrients is used by the cell in the same way as the breakdown products of substances necessary for the synthesis of organic compounds.

Today, it is not only enzymes used for medical purposes that are widely used. Enzymes are also used in the food and textile industries, and in modern pharmacology.

Classification of enzymes

At the meeting of the V International Biochemical Union, held in Moscow in 1961, the modern classification of enzymes was adopted. This classification implies their division into classes, depending on the type of reaction in which the enzyme acts as a catalyst. In addition, each enzyme class is divided into subclasses. To designate them, a code of four numbers separated by dots is used:

• the first number indicates the reaction mechanism in which the enzyme acts as a catalyst;
• the second number indicates the subclass to which the enzyme belongs;
• the third number is the subclass of the enzyme being described;
• and fourth, the serial number of the enzyme in the subclass to which it belongs.

In total, in the modern classification of enzymes, six classes are distinguished, namely:

• Oxidoreductases are enzymes that act as catalysts in various redox reactions occurring in cells. This class includes 22 subclasses.
• Transferases are a class of enzymes with 9 subclasses. It includes enzymes that provide transport reactions between different substrates, enzymes that take part in reactions of interconversion of substances, as well as the neutralization of various organic compounds.
• Hydrolases are enzymes that break intramolecular bonds of a substrate by attaching water molecules to it. There are 13 subclasses in this class.
• Lyases are a class that contains only complex enzymes. It has seven subclasses. Enzymes belonging to this class act as catalysts in reactions gap S-O, C-C, C-N and other types of organic bonds. Also, enzymes of the lyase class participate in reversible biochemical elimination reactions in a non-hydrolytic way.
• Isomerases are enzymes that act as catalysts in chemical processes of isomeric transformations occurring in one molecule. Like the previous class, these include only complex enzymes.
• Ligases, otherwise called synthetases, are a class that includes six subclasses and represent enzymes that catalyze the process of joining two molecules under the influence of ATP.

The composition of enzymes combines individual areas responsible for performing specific functions. Thus, enzymes usually contain active and allosteric centers. The latter, by the way, is not present in all protein molecules. The active center is a combination of amino acid residues and is responsible for contact with the substrate and catalysis. The active center, in turn, is divided into two parts: anchor and catalytic. Enzymes consisting of several monomers may contain more than one active site.

The allosteric center is responsible for enzyme activity. This part of the enzymes received its name due to the fact that its spatial configuration has nothing to do with the substrate molecule. The change in the rate of the reaction occurring with the participation of the enzyme is caused by the binding of various molecules precisely to the allosteric center. Enzymes containing allosteric centers are polymeric proteins.

Mechanism of action of enzymes

The action of enzymes can be divided into several stages, in particular:

• the first stage involves the addition of the substrate to the enzyme, as a result of which an enzyme-substrate complex is formed;
• the second stage consists of transforming the resulting complex into one or several transition complexes;
• the third stage is the formation of an enzyme-product complex;
• and finally, the fourth stage involves the separation of the final reaction product and the enzyme, which remains unchanged.

In addition, the action of enzymes can occur through various mechanisms of catalysis. Thus, acid-base and covalent catalysis are distinguished. In the first case, the reaction involves enzymes containing specific amino acid residues in their active center. Such groups of enzymes are excellent catalysts for numerous reactions in the body. Covalent catalysis involves the action of enzymes that, upon contact with substrates, form unstable complexes. The result of such reactions is the formation of products through intramolecular rearrangements.

There are also three main types of enzymatic reactions:

• “Ping-pong” is a reaction in which an enzyme combines with one substrate, borrowing certain substances from it, and then interacts with another substrate, giving it the resulting chemical groups.
• Sequential reactions involve the alternating addition of first one and then another substrate to the enzyme, resulting in the formation of a so-called “ternary complex” in which catalysis occurs.
• Random interactions are reactions in which substrates interact with the enzyme in a disorderly manner, and after catalysis, they are cleaved off in the same order.

Enzyme activity is variable and largely depends on various factors environment in which they have to operate. So the main indicators for enzyme activity are factors of internal and external influence on the cell. The activity of enzymes is changed in catalahs, showing the amount of enzyme that converts 1 mole of the substrate with which it interacts in a second. The international unit of measurement is E, demonstrating the amount of enzyme capable of converting 1 µmol of substrate in 1 minute.

Enzyme inhibition: process

One of the main directions in modern medicine and enzymology in particular is the development of methods for controlling the rate of metabolic reactions occurring with the participation of enzymes. Inhibition is usually called a decrease in enzyme activity through the use of various connections. Accordingly, a substance that provides a specific reduction in the activity of protein molecules is called an inhibitor. There are different types of inhibition. Thus, depending on the strength of binding of the enzyme to the inhibitor, the process of their interaction can be reversible and, accordingly, irreversible. And depending on how the inhibitor acts on the active center of the enzyme, the process of inhibition can be competitive or non-competitive.

Activation of enzymes in the body

Unlike inhibition, enzyme activation implies an increase in their action in ongoing reactions. Substances that allow you to obtain the desired result are called activators. Such substances can be organic or inorganic in nature. For example, bile acids, glutathione, enterokinase, vitamin C, various tissue enzymes, etc. can act as organic activators. Pepsinogen and various metal ions, most often divalent, can be used as inorganic activators.

Various enzymes, the reactions occurring with their participation, as well as their results have found their wide application in a variety of fields. For many years, the action of enzymes has been actively used in the food, leather, textile, pharmaceutical and many other industrial sectors. For example, with the help of natural enzymes, researchers are trying to increase the efficiency of alcoholic fermentation in the production of alcoholic beverages, improve the quality of food, develop new methods of losing weight, etc. But it is worth noting that the use of enzymes in various industries is significantly inferior to the use of chemical catalysts. After all, the main difficulty in implementing such a task in practice is the thermal instability of enzymes and their increased sensitivity to various factors. It is also impossible to reuse enzymes in production due to the difficulty of separating them from the finished products of completed reactions.

In addition, the action of enzymes has found its active use in medicine, agriculture and the chemical industry. Let's take a closer look at how and where the action of enzymes can be used:

• Food industry. Everyone knows that good dough should rise and swell when baking. But not everyone understands exactly how this happens. The flour from which the dough is made contains many different enzymes. Thus, amylase in flour is involved in the process of starch decomposition, during which carbon dioxide is actively released, which contributes to the so-called “swelling” of the dough. The stickiness of the dough and the retention of CO2 in it is ensured by the action of an enzyme called protease, which is also found in flour. It turns out that such, it would seem. Simple things like preparing baking dough involve complex chemical processes. Also, some enzymes and the reactions occurring with their participation have found particular demand in the field of alcohol production. Various enzymes are used in yeast to ensure the quality of the alcohol fermentation process. In addition, certain enzymes (such as papain or pepsin) help dissolve sediment in alcoholic beverages. Enzymes are also actively used in the production of fermented milk products and cheese, among others.
• In the leather industry, enzymes are used to effectively break down proteins, which is most important when removing stubborn stains from various food products, blood, etc.
• Cellulase can be used in the production of washing powders. But when using such powders, to obtain the stated result, it is necessary to comply with the permissible washing temperature.

In addition, in the production of feed additives, enzymes are used to increase their nutritional value, hydrolyze proteins and non-starch polysaccharides. In the textile industry, enzymes can modify the surface properties of textiles, and in the pulp and paper industry, they can remove ink and toners during paper recycling.

The huge role of enzymes in the life of modern man is undeniable. Already today, their properties are actively used in various fields, but the search for new options for using the unique properties and functions of enzymes is also ongoing.

Human enzymes and hereditary diseases

Many diseases develop against the background of enzymopathies - dysfunctions of enzymes. Primary and secondary enzymopathies are distinguished. Primary disorders are hereditary, secondary disorders are acquired. Hereditary enzymopathies are usually classified as metabolic diseases. Inheritance of genetic defects or decreased enzyme activity occurs predominantly in an autosomal recessive manner. For example, a disease such as phenylketonuria is a consequence of a defect in an enzyme such as phenylalanine-4-monooxygenase. This enzyme is normally responsible for converting phenylalanine to tyrosine. As a result of enzyme dysfunction, abnormal phenylalanine metabolites accumulate, which are toxic to the body.

Enzymopathies also include gout, the development of which is caused by a disturbance in the metabolism of purine bases and, as a consequence, a stable increase in the level of uric acid in the blood. Galactosemia is another disease caused by a hereditary dysfunction of enzymes. This pathology develops due to a violation of carbohydrate metabolism, in which the body cannot convert galactose into glucose. The consequence of this disorder is the accumulation of galactose and its metabolic products in cells, which leads to damage to the liver, central nervous system and other vital systems of the body. The main manifestations of galactosemia are diarrhea, vomiting that appears immediately after the birth of a child, obstructive jaundice, cataracts, and delayed physical and intellectual development.

Various glycogenoses and lipidoses also belong to hereditary enzymopathies, otherwise called enzyme pathologies. The development of such disorders is due to low enzyme activity in the human body or its complete absence. Hereditary metabolic defects are usually accompanied by the development of diseases of varying severity. However, some enzymopathies can be asymptomatic and are determined only when appropriate diagnostic procedures are carried out. But basically, the first symptoms of hereditary metabolic disorders appear in early childhood. This happens less often in older children and even more so in adults.

When diagnosing hereditary enzymopathies, the genealogical research method plays an important role. In this case, experts check enzyme reactions in the laboratory. Hereditary enzymopathies can lead to disturbances in the production of hormones, which are of particular importance for the full functioning of the body. For example, the adrenal cortex produces glucocorticoids, which are responsible for the regulation of carbohydrate metabolism, mineralocorticoids, which are involved in water-salt metabolism, as well as androgenic hormones, which have a direct effect on the development of secondary sexual characteristics in adolescents. Thus, disruption of the production of these hormones can lead to the development of numerous pathologies in various organ systems.

The process of food processing in the human body occurs with the participation of various digestive enzymes. During the digestion of food, all substances are broken down into small molecules, because only low molecular weight compounds are able to penetrate the intestinal wall and be absorbed into the bloodstream. A special role in this process is given to enzymes that break down proteins into amino acids, fats into glycerol and fatty acids, and starch into sugars. The breakdown of proteins is ensured by the action of the enzyme pepsin, contained in the main organ of the digestive system - the stomach. Some digestive enzymes are produced in the intestines by the pancreas. In particular these include:

• trypsin and chymotrypsin, the main purpose of which is protein hydrolysis;
• amylase – enzymes that break down fats;
• lipase - digestive enzymes that break down starch.

Digestive enzymes such as trypsin, pepsin, chymotrypsin are produced in the form of proenzymes, and only after they enter the stomach and intestines do they become active. This feature protects the tissues of the stomach and pancreas from their aggressive effects. In addition, the inner lining of these organs is additionally covered with a layer of mucus, which ensures their even greater safety.

Some digestive enzymes are also produced in the small intestine. An enzyme with the similar name cellulase is responsible for processing cellulose that enters the body along with plant foods. In other words, almost every part of the gastrointestinal tract produces digestive enzymes, from the salivary glands to the colon. Each type of enzyme performs its own functions, collectively ensuring high-quality digestion of food and complete absorption of all nutrients in the body.

Pancreatic enzymes

The pancreas is an organ of mixed secretion, that is, it performs both endo- and exogenous functions. The pancreas, as mentioned above, produces a number of enzymes that are activated under the influence of bile, which enters the digestive organs along with the enzymes. Pancreatic enzymes are responsible for breaking down fats, proteins and carbohydrates into simple molecules that can pass through the cell membrane into the bloodstream. Thus, thanks to pancreatic enzymes, complete absorption of beneficial substances entering the body along with food occurs. Let us consider in more detail the action of enzymes synthesized by the cells of this organ of the gastrointestinal tract:

• amylase, together with small intestinal enzymes such as maltase, invertase and lactase, ensure the breakdown of complex carbohydrates;
• proteases, otherwise called proteolytic enzymes in the human body, are represented by trypsin, carboxypeptidase and elastase and are responsible for the breakdown of proteins;
• nucleases – pancreatic enzymes, represented by deoxyribonuclease and ribonuclease, acting on amino acids RNA, DNA;
• lipase is a pancreatic enzyme responsible for converting fats into fatty acids.

The pancreas also synthesizes phospholipase, esterase and alkaline phasftase.

The most dangerous in active form are proteolytic enzymes produced by the organ. If the process of their production and release into other organs of the digestive system is disrupted, the enzymes are activated directly in the pancreas, which leads to the development of acute pancreatitis and related complications. Inhibitors of proteolytic enzymes that inhibit their action are pancreatic polypeptide and glucagon, somatostatin, peptide YY, enkephalin and pancreastatin. The listed inhibitors can inhibit the production of pancreatic enzymes by affecting the active elements of the digestive system.

The main processes of digestion of food entering the body take place in the small intestine. In this section of the gastrointestinal tract, enzymes are also synthesized, the process of activation of which occurs jointly with enzymes of the pancreas and gall bladder. The small intestine is a section of the digestive tract in which the final stages of hydrolysis of nutrients entering the body along with food occur. It synthesizes various enzymes that break down oligo- and polymers into monomers, which can be easily absorbed by the mucous membrane of the small intestine and enter the lymph and bloodstream.

Under the influence of enzymes in the small intestine, the process of breakdown of proteins that have undergone preliminary transformation in the stomach into amino acids, complex carbohydrates into monosaccharides, and fats into fatty acids and glycerol occurs. Intestinal juice contains over 20 types of enzymes involved in the process of food digestion. With the participation of pancreatic and intestinal enzymes, complete processing of chyme (partially digested food) is ensured. All processes in the small intestine occur within 4 hours after chyme enters this section of the digestive tract.

An important role in the digestion of food in the small intestine is played by bile, which enters the duodenum during the digestion process. There are no enzymes in the bile itself, but this biological fluid enhances the action of enzymes. Bile is most important for the breakdown of fats, turning them into an emulsion. Such emulsified fat breaks down much faster under the influence of enzymes. Fatty acids, interacting with bile acids, are converted into readily soluble compounds. In addition, the secretion of bile stimulates intestinal motility and the production of digestive juice by the pancreas.

Intestinal juice is synthesized by glands located in the mucous membrane of the small intestine. This liquid contains digestive enzymes, as well as enterokinase, which is designed to activate the action of trypsin. In addition, intestinal juice contains an enzyme called erepsin, which is necessary for the final stage of protein breakdown, enzymes that act on various types of carbohydrates (for example, amylase and lactase), as well as lipase, designed to convert fats.

Gastric enzymes

The process of food digestion occurs in stages in each section of the gastrointestinal tract. So, it begins in the oral cavity, where food is crushed by the teeth and mixed with saliva. It is saliva that contains enzymes that break down sugar and starch. After the oral cavity, the crushed food enters the esophagus into the stomach, where the next stage of its digestion begins. The main gastric enzyme is pepsin, designed to convert proteins into peptides. Also present in the stomach is gelatinase, an enzyme whose main task is the breakdown of collagen and gelatin. Plus, food in the cavity of this organ is exposed to amylase and lipase, which break down starch and fats, respectively.

The ability of the body to obtain all the necessary nutrients depends on the quality of the digestive process. The breakdown of complex molecules into many simple ones ensures their further absorption into the blood and lymph flow at subsequent stages of digestion in other parts of the gastrointestinal tract. Insufficient production of gastric enzymes can cause the development of various diseases.

Liver enzymes are of great importance for the course of various biochemical processes in the body. The functions of protein molecules produced by this organ are so numerous and diverse that all liver enzymes are usually divided into three main groups:

• Secretory enzymes designed to regulate the blood clotting process. These include cholinesterase and prothrombinase.
• Indicator liver enzymes, including aspartate aminotransferase, abbreviated AST, alanine aminotransferase, correspondingly designated ALT, and lactate dehydrogenase, LDH. The listed enzymes signal damage to organ tissues, in which hepatocytes are destroyed, “leave” the liver cells and enter the bloodstream;
• Excretory enzymes are produced by the liver and leave the organ with the sweat of bile. These enzymes include alkaline phosphatase. If the outflow of bile from the organ is impaired, the level of alkaline phosphatase increases.

Impaired functioning of certain liver enzymes in the future can lead to the development of various diseases or signal their presence at the present time.

One of the most informative tests for liver diseases is blood biochemistry, which allows you to determine the level of indicator enzymes AST and ATL. Thus, normal aspartate aminotransferase levels for a woman are 20-40 U/l, and for representatives of the stronger sex – 15-31 U/l. An increase in the activity of this enzyme may indicate damage to hepatocytes of a mechanical or necrotic nature. Normal alanine aminotransferase levels should not exceed 12-32 U/L in women, while for men an ALT activity level of 10-40 U/L is considered normal. An increase in ALT activity, reaching tenfold levels, may indicate the development of infectious diseases of the organ, long before the appearance of their first symptoms.

Additional studies of liver enzyme activity are usually used for differential diagnosis. For this purpose, an analysis can be carried out for LDH, GGT and GLDG:

• The norm for lactate dehydrogenase activity is an indicator ranging from 140-350 U/l.
• Elevated GLDG levels may be a sign of degenerative organ damage, severe intoxication, infectious diseases or oncology. The maximum permissible indicator of such an enzyme for females is 3.0 U/l, and for men – 4.0 U/l.
• The norm for GGT enzyme activity for men is up to 55 U/l, for women – up to 38 U/l. Deviations from this norm may indicate the development of diabetes, as well as diseases of the biliary tract. In this case, the enzyme activity indicator can increase tens of times. In addition, GGT in modern medicine is used to determine alcoholic hepatosis.

Enzymes synthesized by the liver have various functions. Thus, some of them, together with bile, are excreted from the organ through the bile ducts and take an active part in the process of food digestion. A striking example In addition, alkaline phosphatase acts. The normal activity level of this enzyme in the blood should be in the range of 30-90 U/l. It is worth noting that in males this figure can reach 120 U/l (with intense metabolic processes, the figure may increase).

Blood enzymes

Determining the activity of enzymes and their content in the body is one of the main diagnostic methods in determining various diseases. Thus, blood enzymes contained in its plasma may indicate the development of liver pathologies, inflammatory and necrotic processes in tissue cells, diseases of the cardiovascular system, etc. Blood enzymes are usually divided into two groups. The first group includes enzymes secreted into the blood plasma by some organs. For example, the liver produces so-called precursors of enzymes necessary for the functioning of the blood coagulation system.

The second group has a much larger number of blood enzymes. In the body of a healthy person, such protein molecules do not have physiological significance in the blood plasma, since they act exclusively at the intracellular level in the organs and tissues by which they are produced. Normally, the activity of such enzymes should be low and constant. When cells are damaged, which is accompanied by various diseases, the enzymes contained in them are released and enter the bloodstream. The reason for this may be inflammatory and necrotic processes. In the first case, the release of enzymes occurs due to a violation of the permeability of the cell membrane, in the second - due to a violation of the integrity of the cells. Moreover, the higher the level of enzymes in the blood, the greater the degree of cell damage.

Biochemical analysis allows you to determine the activity of certain enzymes in the blood plasma. It is actively used in the diagnosis of various diseases of the liver, heart, skeletal muscles and other types of tissues in the human body. In addition, the so-called enzyme diagnostics, when determining some diseases, takes into account the subcellular localization of enzymes. The results of such studies make it possible to determine exactly what processes occur in the body. Thus, during inflammatory processes in tissues, blood enzymes have a cytosolic localization, and during necrotic lesions the presence of nuclear or mitochondrial enzymes is determined.

It is worth noting that an increase in the content of enzymes in the blood is not always due to tissue damage. Active pathological proliferation of tissues in the body, in particular during cancer, increased production of certain enzymes or impaired excretory capacity of the kidneys can also be determined by an increased content of certain enzymes in the blood.

In modern medicine, a special place is given to the use of various enzymes for diagnostic and therapeutic purposes. Enzymes have also found their use as specific reagents that make it possible to accurately determine various substances. For example, when performing an analysis to determine the level of glucose in urine and blood serum, modern laboratories use glucose oxidase. Urease is used to assess the quantitative content of urea in urine and blood tests. Different types of dehydrogenases make it possible to accurately determine the presence of various substrates (lactate, pyruvate, ethyl alcohol, etc.).

The high immunogenicity of enzymes significantly limits their use for therapeutic purposes. But, despite this, the so-called enzyme therapy is actively developing, using enzymes (drugs containing them) as a means of replacement therapy or an element of complex treatment. Replacement therapy is used for gastrointestinal diseases, the development of which is caused by insufficient production of digestive juice. If there is a deficiency of pancreatic enzymes, their deficiency can be compensated for by oral administration of medications that contain them.

As an additional element in complex treatment, enzymes can be used for various diseases. For example, proteolytic enzymes such as trypsin and chymotrypsin are used in the processing purulent wounds. Preparations with the enzymes deoxyribonuclease and ribonuclease are used in the treatment of adenoviral conjunctivitis or herpetic keratitis. Enzyme preparations are also used in the treatment of thrombosis and thromboembolism, cancer, etc. Their use is important for the resorption of contractures of burns and postoperative scars.

The use of enzymes in modern medicine is very diverse and this area is constantly evolving, which allows us to constantly find new and more effective methods treatment of certain diseases.

Enzymes (enzymes): importance for health, classification, application. Plant (food) enzymes: sources, benefits.

Enzymes (enzymes) are high-molecular substances of protein nature that perform the functions of catalysts in the body (they activate and accelerate various biochemical reactions). Fermentum translated from Latin means fermentation. The word enzyme has Greek roots: “en” - inside, “zyme” - leaven. These two terms, enzymes and enzymes, are used interchangeably, and the science of enzymes is called enzymology.

The importance of enzymes for health. Application of enzymes

Enzymes are called the keys to life for a reason. They have the unique property of acting specifically, selectively, only on a narrow range of substances. Enzymes cannot replace each other.

To date, more than 3 thousand enzymes have been known. Each cell of a living organism contains hundreds of different enzymes. Without them, not only is it impossible to digest food and convert it into substances that cells can absorb. Enzymes take part in the processes of renewal of skin, blood, bones, regulation of metabolism, cleansing of the body, wound healing, visual and auditory perception, the functioning of the central nervous system, and the implementation of genetic information. Breath, muscle contraction, heart function, cell growth and division - all these processes are supported by the uninterrupted operation of enzyme systems.

Enzymes play an extremely important role in supporting our immunity. Specialized enzymes are involved in the production of antibodies necessary to fight viruses and bacteria, and activate the work of macrophages - large predatory cells that recognize and neutralize any foreign particles that enter the body. Removing cell waste products, neutralizing poisons, protecting against infection - all these are the functions of enzymes.

Special enzymes (bacteria, yeast, rennet enzymes) play an important role in the production of pickled vegetables, fermented milk products, dough fermentation, and cheese making.

Classification of enzymes

According to the principle of action, all enzymes (according to the international hierarchical classification) are divided into 6 classes:

1. Oxidoreductases – catalase, alcohol dehydrogenase, lactate dehydrogenase, polyphenol oxidase, etc.;
2. Transferases (transfer enzymes) – aminotransferases, acyltransferases, phosphorustransferases, etc.;
3. Hydrolases – amylase, pepsin, trypsin, pectinase, lactase, maltase, lipoprotein lipase, etc.;
4. Lyases;
5. Isomerases;
6. Ligases (synthetases) – DNA polymerase, etc.

Each class consists of subclasses, and each subclass consists of groups.

All enzymes can be divided into 3 large groups:

1. Digestive - act in the gastrointestinal tract, responsible for the processing of nutrients and their absorption into the systemic bloodstream. Enzymes that are secreted by the walls of the small intestine and the pancreas are called pancreatic;
2. Food (plant) – come (should come) with food. Foods that contain food enzymes are sometimes called live food;
3. Metabolic - trigger metabolic processes inside cells. Each system of the human body has its own network of enzymes.

Digestive enzymes, in turn, are divided into 3 categories:

1. Amylases – salivary amylase, pancreatic juice lactase, salivary maltase. These enzymes are present in both saliva and the intestines. They act on carbohydrates: the latter break down into simple sugars and easily penetrate into the blood;
2. Proteases are produced by the pancreas and gastric mucosa. They help digest proteins and also normalize the microflora of the digestive tract. Present in the intestines and gastric juice. Proteases include gastric pepsin and chymosin, erepsin in sparrow juice, pancreatic carboxypeptidase, chymotrypsin, trypsin;
3. Lipase – produced by the pancreas. Present in gastric juice. Helps break down and absorb fats.

Action of enzymes

The optimal temperature for enzyme activity is about 37 degrees, that is, body temperature. Enzymes have enormous power: they make seeds germinate and fats “burn.” On the other hand, they are extremely sensitive: at temperatures above 42 degrees, enzymes begin to break down. Both culinary processing of food and deep freezing lead to the death of enzymes and loss of their vitality. In canned, sterilized, pasteurized and even frozen foods, enzymes are partially or completely destroyed. But not only dead food, but also too cold and hot dishes kill enzymes. When we eat food that is too hot, we kill digestive enzymes and burn the esophagus. The stomach greatly increases in size, and then, due to spasms of the muscles that hold it, it becomes like a cockscomb. As a result, food enters the duodenum in an unprocessed state. If this happens constantly, problems such as dysbiosis, constipation, intestinal upset, and stomach ulcers may appear. The stomach also suffers from cold foods (ice cream, for example) - first it shrinks, and then increases in size, and the enzymes freeze. The ice cream begins to ferment, gases are released and the person gets bloated.

Digestive enzymes

It's no secret that good digestion is an essential condition for a full life and active longevity. Digestive enzymes play a role in this process decisive role. They are responsible for the digestion, adsorption and assimilation of food, building our body like construction workers. We can have all the building materials - minerals, proteins, fats, water, vitamins, but without enzymes, as without workers, construction will not advance a single step.

Modern man consumes too much food, for the digestion of which there are practically no enzymes in the body, for example, starchy foods - pasta, bakery products, potatoes.

If you eat a fresh apple, it will be digested by its own enzymes, and the effect of the latter is visible to the naked eye: the darkening of a bitten apple is the work of enzymes that are trying to heal the “wound” and protect the body from the threat of mold and bacteria. But if you bake an apple, in order to digest it, the body will have to use its own enzymes for digestion, since cooked food lacks natural enzymes. In addition, we lose forever those enzymes that “dead” foods take from our body, since their reserves in our body are not unlimited.

Plant (food) enzymes

Eating foods rich in enzymes not only facilitates digestion, but also releases energy that the body can use to cleanse the liver, patch holes in the immune system, rejuvenate cells, protect against tumors, etc. At the same time, a person feels light in his stomach, feels cheerful, and looks good. And raw plant fiber, which enters the body with live food, is required to feed microorganisms that produce metabolic enzymes.

Plant enzymes give us life and energy. If you plant two nuts in the ground - one roasted, and the other raw, soaked in water, then the roasted one will simply rot in the ground, and the raw grain will wake up in the spring vitality because it contains enzymes. And it is quite possible that a large lush tree will grow from it. Likewise, a person, consuming food that contains enzymes, receives life along with it. Enzyme-deprived foods cause our cells to work without rest, become overloaded, age and die. If there are not enough enzymes, “waste” begins to accumulate in the body: poisons, toxins, dead cells. This leads to weight gain, disease and early aging. A curious and at the same time sad fact: in the blood of elderly people, the content of enzymes is approximately 100 times lower than in young people.

Enzymes in products. Sources of plant enzymes

Sources of food enzymes are plant products from the garden, garden, and ocean. These are mainly vegetables, fruits, berries, herbs, and grains. Bananas, mangoes, papaya, pineapples, avocados, aspergillus plant, and sprouted grains contain their own enzymes. Plant enzymes are present only in raw, live foods.

Wheat sprouts are a source of amylase (which breaks down carbohydrates), papaya fruits contain proteases, and papaya and pineapple fruits contain peptidases. Sources of lipase (which breaks down fats) are fruits, seeds, rhizomes, tubers of cereal crops, mustard and sunflower seeds, and legume seeds. Bananas, pineapples, kiwi, papaya, and mango are rich in papain (which breaks down proteins). The source of lactase (an enzyme that breaks down milk sugar) is barley malt.

Advantages of plant (food) enzymes over animal (pancreatic) enzymes

Plant enzymes begin to process food already in the stomach, but pancreatic enzymes cannot work in the acidic gastric environment. When food enters the small intestine, plant enzymes will pre-digest it, reducing stress on the intestines and allowing nutrients to be better absorbed. In addition, plant enzymes continue their work in the intestines.

How to eat so that the body has enough enzymes?

Everything is very simple. Breakfast should consist of fresh berries and fruits (plus protein dishes - cottage cheese, nuts, sour cream). Every meal should start with vegetable salads with herbs. It is advisable that one meal every day includes only raw fruits, berries and vegetables. Dinner should be light - consist of vegetables (with a piece chicken breast, boiled fish or a portion of seafood). Several times a month it is useful to arrange fasting days on fruits or freshly squeezed juices.

For high-quality digestion of food and full health, enzymes are simply irreplaceable. Excess weight, allergies, various gastrointestinal diseases - all these and many other problems can be overcome with a healthy diet. And the role of enzymes in nutrition is enormous. Our task is simply to make sure that they are present in our dishes every day and in sufficient quantities. Good health to you!

ChapterIV.3.

Enzymes

Metabolism in the body can be defined as the totality of all chemical transformations to which compounds coming from outside undergo. These transformations include all known types of chemical reactions: intermolecular transfer of functional groups, hydrolytic and non-hydrolytic cleavage of chemical bonds, intramolecular rearrangement, new formation of chemical bonds and redox reactions. Such reactions occur in the body at extremely high speed only in the presence of catalysts. All biological catalysts are substances of protein nature and are called enzymes (hereinafter F) or enzymes (E).

Enzymes are not components of reactions, but only accelerate the achievement of equilibrium by increasing the rate of both direct and reverse conversion. Acceleration of the reaction occurs due to a decrease in the activation energy - the energy barrier that separates one state of the system (the original chemical compound) from another (the reaction product).

Enzymes speed up a variety of reactions in the body. So, quite simple from the point of view of traditional chemistry, the reaction of the elimination of water from carbonic acid with the formation of CO 2 requires the participation of an enzyme, because without it, it proceeds too slowly to regulate blood pH. Thanks to the catalytic action of enzymes in the body, it becomes possible for reactions to occur that without a catalyst would proceed hundreds and thousands of times slower.

Properties of enzymes

1. Influence on the rate of a chemical reaction: enzymes increase the rate of a chemical reaction, but are not consumed themselves.

The rate of a reaction is the change in the concentration of reaction components per unit time. If it goes in the forward direction, then it is proportional to the concentration of the reactants, if in the opposite direction, then it is proportional to the concentration of the reaction products. The ratio of the rates of forward and reverse reactions is called the equilibrium constant. Enzymes cannot change the value of the equilibrium constant, but the state of equilibrium occurs faster in the presence of enzymes.

2. Specificity of enzyme action. 2-3 thousand reactions take place in the cells of the body, each of which is catalyzed by a specific enzyme. The specificity of an enzyme's action is the ability to accelerate the course of one specific reaction without affecting the speed of others, even very similar ones.

There are:

Absolute– when F catalyzes only one specific reaction ( arginase– breakdown of arginine)

Relative(group special) – F catalyzes a certain class of reactions (for example, hydrolytic cleavage) or reactions involving a certain class of substances.

The specificity of enzymes is due to their unique amino acid sequence, which determines the conformation of the active center that interacts with the reaction components.

A substance whose chemical transformation is catalyzed by an enzyme is called substrate ( S ) .

3. Enzyme activity – the ability to accelerate the reaction rate to varying degrees. Activity is expressed in:

1) International units of activity - (IU) the amount of enzyme that catalyzes the conversion of 1 µM of substrate in 1 minute.

2) Catalach (kat) - the amount of catalyst (enzyme) capable of converting 1 mole of substrate in 1 s.

3) Specific activity - the number of activity units (any of the above) in the test sample to the total mass of protein in this sample.

4) Less commonly used is molar activity - the number of substrate molecules converted by one enzyme molecule per minute.

Activity depends primarily on temperature . This or that enzyme exhibits its greatest activity at the optimal temperature. For F of a living organism, this value is in the range +37.0 - +39.0° C, depending on the type of animal. As the temperature decreases, the Brownian motion slows down, the diffusion rate decreases and, consequently, the process of complex formation between the enzyme and the reaction components (substrates) slows down. If the temperature rises above +40 - +50° The enzyme molecule, which is a protein, undergoes a process of denaturation. In this case, the rate of the chemical reaction noticeably drops (Fig. 4.3.1.).

Enzyme activity also depends on pH of the environment . For most of them, there is a certain optimal pH value at which their activity is maximum. Since a cell contains hundreds of enzymes and each of them has its own pH limits, pH changes are one of the important factors in the regulation of enzymatic activity. Thus, as a result of one chemical reaction with the participation of a certain enzyme, the pH value of which lies in the range of 7.0 - 7.2, a product is formed that is an acid. In this case, the pH value shifts to the region of 5.5 – 6.0. The activity of the enzyme decreases sharply, the rate of product formation slows down, but at the same time another enzyme is activated, for which these pH values ​​are optimal and the product of the first reaction undergoes further chemical transformation. (Another example about pepsin and trypsin).

Chemical nature of enzymes. The structure of the enzyme. Active and allosteric centers

All enzymes are proteins with a molecular weight from 15,000 to several million Da. According to their chemical structure they are distinguished simple enzymes (consisting only of AA) and complex enzymes (have a non-protein part or a prosthetic group). The protein part is called - apoenzyme, and non-protein, if it is covalently linked to the apoenzyme, it is called coenzyme, and if the bond is non-covalent (ionic, hydrogen) – cofactor . The functions of the prosthetic group are as follows: participation in the act of catalysis, contact between the enzyme and the substrate, stabilization of the enzyme molecule in space.

The role of cofactor is usually played by inorganic substances - ions of zinc, copper, potassium, magnesium, calcium, iron, molybdenum.

Coenzymes can be considered as an integral part of the enzyme molecule. These are organic substances, among which there are: nucleotides ( ATP, UMF, etc.), vitamins or their derivatives ( TDF– from thiamine ( IN 1), FMN– from riboflavin ( AT 2), coenzyme A– from pantothenic acid ( AT 3), NAD, etc.) and tetrapyrrole coenzymes - hemes.

In the process of catalyzing a reaction, not the entire enzyme molecule comes into contact with the substrate, but a certain part of it, which is called active center. This zone of the molecule does not consist of a sequence of amino acids, but is formed by twisting the protein molecule into a tertiary structure. Individual sections of amino acids come closer to each other, forming a specific configuration of the active center. Important Feature structure of the active center - its surface is complementary to the surface of the substrate, i.e. AK residues in this zone of the enzyme are capable of entering into chemical interactions with certain groups of the substrate. One can imagine that The active site of the enzyme coincides with the structure of the substrate like a key and a lock.

IN active center two zones are distinguished: binding center, responsible for substrate attachment, and catalytic center, responsible for the chemical transformation of the substrate. The catalytic center of most enzymes includes AAs such as Ser, Cys, His, Tyr, Lys. Complex enzymes have a cofactor or coenzyme at the catalytic center.

In addition to the active center, a number of enzymes are equipped with a regulatory (allosteric) center. Substances that affect its catalytic activity interact with this zone of the enzyme.

Mechanism of action of enzymes

The act of catalysis consists of three successive stages.

1. Formation of an enzyme-substrate complex upon interaction through the active center.

2. Binding of the substrate occurs at several points in the active center, which leads to a change in the structure of the substrate and its deformation due to changes in the bond energy in the molecule. This is the second stage and is called substrate activation. In this case, a certain chemical modification of the substrate occurs and it is converted into a new product or products.

3. As a result of this transformation, the new substance (product) loses its ability to be retained in the active center of the enzyme and the enzyme-substrate, or rather, enzyme-product complex dissociates (breaks up).

Types of catalytic reactions:

A+E = AE = BE = E + B

A+B +E = AE+B = ABE = AB + E

AB+E = ABE = A+B+E, where E is the enzyme, A and B are substrates or reaction products.

Enzymatic effectors - substances that change the rate of enzymatic catalysis and thereby regulate metabolism. Among them there are inhibitors - slow down the reaction rate and activators - accelerating the enzymatic reaction.

Depending on the mechanism of reaction inhibition, competitive and non-competitive inhibitors are distinguished. The structure of the competitive inhibitor molecule is similar to the structure of the substrate and coincides with the surface of the active center like a key and a lock (or almost coincides). The degree of this similarity may even be higher than with the substrate.

If A+E = AE = BE = E + B, then I+E = IE¹

The concentration of the enzyme capable of catalysis decreases and the rate of formation of reaction products drops sharply (Fig. 4.3.2.).

A large number of chemical substances of endogenous and exogenous origin (i.e., those formed in the body and coming from outside - xenobiotics, respectively) act as competitive inhibitors. Endogenous substances are regulators of metabolism and are called antimetabolites. Many of them are used in the treatment of oncological and microbial diseases, as. they inhibit key metabolic reactions of microorganisms (sulfonamides) and tumor cells. But with an excess of substrate and a low concentration of the competitive inhibitor, its effect is canceled.

The second type of inhibitors is non-competitive. They interact with the enzyme outside the active site and excess substrate does not affect their inhibitory ability, as is the case with competitive inhibitors. These inhibitors interact either with certain groups of the enzyme (heavy metals bind to the thiol groups of Cys) or most often with the regulatory center, which reduces the binding ability of the active center. The actual process of inhibition is the complete or partial suppression of enzyme activity while maintaining its primary and spatial structure.

A distinction is also made between reversible and irreversible inhibition. Irreversible inhibitors inactivate the enzyme, forming AK or other components of the structure chemical bond. This is usually a covalent bond to one of the active site sites. Such a complex practically does not dissociate under physiological conditions. In another case, the inhibitor disrupts the conformational structure of the enzyme molecule and causes its denaturation.

The effect of reversible inhibitors can be removed when there is an excess of substrate or under the influence of substances that change the chemical structure of the inhibitor. Competitive and non-competitive inhibitors are in most cases reversible.

In addition to inhibitors, activators of enzymatic catalysis are also known. They:

1) protect the enzyme molecule from inactivating influences,

2) form a complex with the substrate that binds more actively to the active center of F,

3) interacting with an enzyme that has a quaternary structure, they separate its subunits and thereby open up access for the substrate to the active center.

Distribution of enzymes in the body

Enzymes involved in the synthesis of proteins, nucleic acids and energy metabolism enzymes are present in all cells of the body. But cells that perform special functions also contain special enzymes. Thus, the cells of the islets of Langerhans in the pancreas contain enzymes that catalyze the synthesis of the hormones insulin and glucagon. Enzymes that are characteristic only of the cells of certain organs are called organ-specific: arginase and urokinase- liver, acid phosphatase- prostate. By changing the concentration of such enzymes in the blood, the presence of pathologies in these organs is judged.

In a cell, individual enzymes are distributed throughout the cytoplasm, others are embedded in the membranes of mitochondria and the endoplasmic reticulum, such enzymes form compartments, in which certain, closely interconnected stages of metabolism occur.

Many enzymes are formed in cells and secreted into anatomical cavities in an inactive state - these are proenzymes. Proteolytic enzymes (that break down proteins) are often formed as proenzymes. Then, under the influence of pH or other enzymes and substrates, their chemical modification occurs and the active center becomes accessible to the substrates.

There are also isoenzymes - enzymes that differ in molecular structure, but perform the same function.

Nomenclature and classification of enzymes

The name of the enzyme is formed from the following parts:

1. name of the substrate with which it interacts

2. nature of the catalyzed reaction

3. name of the enzyme class (but this is optional)

4. suffix -aza-

pyruvate - decarboxyl - aza, succinate - dehydrogen - aza

Since about 3 thousand enzymes are already known, they need to be classified. Currently, an international classification of enzymes has been adopted, which is based on the type of reaction catalyzed. There are 6 classes, which in turn are divided into a number of subclasses (presented only selectively in this book):

1. Oxidoreductases. Catalyze redox reactions. They are divided into 17 subclasses. All enzymes contain a non-protein part in the form of heme or derivatives of vitamins B2, B5. The substrate undergoing oxidation acts as a hydrogen donor.

1.1. Dehydrogenases remove hydrogen from one substrate and transfer it to other substrates. Coenzymes NAD, NADP, FAD, FMN. They accept the hydrogen removed by the enzyme, transforming it into a reduced form (NADH, NADPH, FADH) and transfer it to another enzyme-substrate complex, where they release it.

1.2. Oxidases - catalyze the transfer of hydrogen to oxygen to form water or H 2 O 2. F. Cytochrome oxidase respiratory chain.

RH + NAD H + O 2 = ROH + NAD + H 2 O

1.3. Monoxidases - cytochrome P450. According to its structure, it is both a hemoprotein and a flavoprotein. It hydroxylates lipophilic xenobiotics (according to the mechanism described above).

1.4. PeroxidasesAnd catalase- catalyze the decomposition of hydrogen peroxide, which is formed during metabolic reactions.

1.5. Oxygenases - catalyze reactions of oxygen addition to the substrate.

2. Transferases - catalyze the transfer of various radicals from a donor molecule to an acceptor molecule.

A A+ E + B = E A+ A + B = E + B A+ A

2.1. Methyltransferase (CH 3 -).

2.2.Carboxyl- and carbamoyltransferases.

2.2. Acyltransferases – Coenzyme A (transfer of acyl group - R -C=O).

Example: synthesis of the neurotransmitter acetylcholine (see chapter “Protein Metabolism”).

2.3. Hexosyltransferases catalyze the transfer of glycosyl residues.

Example: the cleavage of a glucose molecule from glycogen under the influence of phosphorylases.

2.4. Aminotransferases - transfer of amino groups

R 1- CO - R 2 + R 1 - CH - N.H. 3 - R 2 = R 1 - CH - N.H. 3 - R 2 + R 1- CO - R 2

They play an important role in the transformation of AK. The common coenzyme is pyridoxal phosphate.

Example: alanine aminotransferase(ALT): pyruvate + glutamate = alanine + alpha-ketoglutarate (see chapter “Protein Metabolism”).

2.5. Phosphotransferase (kinase) - catalyze the transfer of a phosphoric acid residue. In most cases, the phosphate donor is ATP. Enzymes of this class mainly take part in the breakdown of glucose.

Example: Hexo(gluco)kinase.

3. Hydrolases - catalyze hydrolysis reactions, i.e. splitting of substances with addition at the site where the water bond is broken. This class includes mainly digestive enzymes; they are single-component (do not contain a non-protein part)

R1-R2 +H 2 O = R1H + R2OH

3.1. Esterases - break down ester bonds. This is a large subclass of enzymes that catalyze the hydrolysis of thiol esters and phosphoesters.
Example: NH 2 ).

Example: arginase(urea cycle).

4.Lyases - catalyze reactions of molecular splitting without adding water. These enzymes have a non-protein part in the form of thiamine pyrophosphate (B 1) and pyridoxal phosphate (B 6).

4.1. C-C bond lyases. They are usually called decarboxylases.

Example: pyruvate decarboxylase.

5.Isomerases - catalyze isomerization reactions.

Example: phosphopentose isomerase, pentose phosphate isomerase(enzymes of the non-oxidative branch of the pentose phosphate pathway).

6.Ligases catalyze reactions for the synthesis of more complex substances from simpler ones. Such reactions require the energy of ATP. “Synthetase” is added to the name of such enzymes.

REFERENCES FOR THE CHAPTER IV.3.

1. Byshevsky A. Sh., Tersenov O. A. Biochemistry for the doctor // Ekaterinburg: Uralsky Rabochiy, 1994, 384 pp.;

2. Knorre D. G., Myzina S. D. Biological chemistry. – M.: Higher. school 1998, 479 pp.;

3. Filippovich Yu. B., Egorova T. A., Sevastyanova G. A. Workshop on general biochemistry // M.: Enlightenment, 1982, 311 pp.;

4. Leninger A. Biochemistry. Molecular basis of cell structure and functions // M.: Mir, 1974, 956 pp.;

5. Pustovalova L.M. Workshop on biochemistry // Rostov-on-Don: Phoenix, 1999, 540 p.

Enzymes or enzymes(from Latin fermentum - leaven) - usually protein molecules or RNA molecules (ribozymes) or their complexes that accelerate (catalyze) chemical reactions in living organisms without undergoing any changes. Substances that have a similar effect also exist in inanimate nature and are called attenuators.

Enzymatic activity can be regulated by activators and inhibitors (activators increase, inhibitors decrease chemical reactions).

The terms “enzyme” and “enzyme” have long been used interchangeably. The science of enzymes is called enzymology.

The vital activity of any organism is not possible without the participation of enzymes. Enzymatic catalysis accelerates the passage of all biochemical reactions in the body and thus ensures the phenomenon of life. Without the presence of enzymes during biochemical reactions, food will not be broken down into five main compounds: carbohydrates, fats, proteins, vitamins and microelements - the food will remain useless for the body. Thus, without enzymes, life slows down.

Functions of enzymes and their role in the life of the body

1. stimulate the process of digestion and absorption of food;
2. activate metabolism, promote the removal of dead cells from the body;
3. regulate osmotic pressure, normalize the pH value of various environments;
4. ensure metabolism, support the body’s ability to resist inflammatory processes;
5. increase immunity and the body’s ability to self-heal and self-regulate;
6. promote detoxification of the body, cleanse lymph and blood.

Necessity of enzymes for healthy functioning of the body
Most scientists are now convinced that almost all diseases are caused by the absence or insufficient amount of enzymes in the body. Medical research shows that disturbances in the production of enzymes in the body are caused by genetic factors.

In particular, such a common disease as diabetes mellitus is due to the fact that the pancreas does not produce enough or does not produce the enzyme insulin. Leukemia and other types of cancer are caused by the absence or weakness of enzymatic barriers in the body. These facts are gradually being confirmed by scientific research. We can say that if the body contains required amount enzymes - there will be no hundred diseases.

With age, as the human body ages, the production of enzymes decreases. The body begins to experience a lack of them, which affects the course of metabolic processes, the efficiency of digestion and absorption of nutrients decreases, and it becomes more difficult to influence the body with medications, because they are not absorbed enough and cause more side effects. Additional intake of a large number of enzymes into the body will compensate for their deficiency and all the resulting consequences.

Thus, a sufficient amount of enzymes in the body is a necessary condition for its healthy state. Many diseases are caused by insufficient production of enzymes, which upsets the balance of metabolism in the body. If, in addition to the natural production of enzymes, we ensure their supply from the outside, then this will be the fastest and most the best way

treatment of diseases.

The human body exists due to the constant influence of enzymes. For example, in the process of digestion, with the help of enzymes, reactions occur that decompose food into nutrients - proteins, fats, carbohydrates, vitamins and microelements; which, with their help, are absorbed into the blood and distributed to all organs. Due to this, our muscles and bones, all organs and systems are nourished, receive energy and carry out the functions necessary to maintain the body in a healthy, active state.

Not only the human body, but also all living things, between heaven and earth, exist due to biochemical reactions carried out with the help of enzymes. The enzyme is the source of life and health of any living organism.

The role of enzymes in the human body

The role of enzymes in maintaining the vital functions of the body is surprising in its importance.

The presence of enzymes and the existence of all living things are inseparable concepts. If the amount of enzyme is not enough to support life, this means death. The appearance of green leaves on trees in the spring, the light of a firefly, any act of vital activity of the human body (be it eating, walking down the street, singing, laughing or crying) - all these processes are ensured by biochemical reactions and are not possible without the mandatory participation of enzymes.

All the food we consume goes through a complex process of breakdown into simple elements in the gastrointestinal tract under the influence of digestive enzymes. Only then can these nutrients enter the bloodstream and spread to all organs and tissues. Try chewing a piece of bread for 2-3 minutes, you will feel how it gradually becomes sweet - this is because under the influence of enzymes contained in saliva, starch is broken down and sweet maltose is released.

With the help of enzymes, the body not only breaks down substances, but also synthesizes them. For example, the synthesis of amino acids into protein molecules - the main building material for muscle cells, hair, etc., or the conversion of glucose into glycogen, which is deposited in the liver and, in case of lack of energy, with the help of the same enzymes, is again broken down into glucose molecules, which provides a rapid release of energy in the body.

The process of skin renewal also occurs due to enzymes involved in metabolic processes. If there are enough enzymes specific for this process, the skin will be soft, shiny and elastic. With enzyme deficiency, the skin becomes dry, flaky, and flaccid.

About 4,000 different types of enzymes function in the human body. Thousands of biochemical reactions take place in it, which together can be compared to a large chemical plant. But all these chemical reactions require enzymatic catalysis, otherwise they either do not proceed or proceed very slowly. Each enzyme participates in one chemical reaction. Some of the enzymes cannot be synthesized by the body. If the body lacks any enzymes, then there is a danger of developing a disease or the occurrence of a pre-disease state, which sooner or later will manifest itself in the disease.

Therefore, if you want to maintain your youth, beauty and health for many years, you need to ensure that your body contains a sufficient amount of enzymes. And if their level is low, then the main source of their replenishment is daily intake in the form of bioactive supplements.

Groups of people especially in need of additional sources of enzymes
Let's consider which groups of people especially need the use of additional enzymes.

Those who want to improve their physical fitness, improve their health or restore it after illness.

People with weakened immune systems, often susceptible to infections.

Those who experience constant fatigue complain of lack of energy and frequent weakness.

Prematurely aging, frail people.

People suffering from chronic diseases.

Cancer patients with various types of cancer, in the pre- and postoperative period.

People suffering from liver diseases.

People who prefer meat food.

People prone to neurasthenia and other neuropsychiatric diseases.

People suffering from sexual dysfunction.

Women in the prenatal and postpartum period.

People with digestive disorders.

Vegetarians (dietary supplements will promote cell stability).

People with insufficient physique, for improvement physical fitness(overweight and obesity, underweight).

People with disabilities and restrictions in movement.

Children during a period of intensive growth (since modern children, for the most part, almost do not consume foods containing digestive enzymes - lipase, amylase and protease; and this is one of the main reasons for childhood obesity, frequent allergies, constipation, and increased fatigue).

Elderly people (with age, the body’s ability to produce its own enzymes decreases, the amount of enzyme that stimulates the process of “inventory” in the body decreases, which is why the consumption of additional enzymes is the path to longevity for them).

Patients with established enzyme dysfunction (since their own enzyme reserves are depleted, they especially need additional enzyme intake).

Athletes especially need a large number of additional enzymes, since due to intense physical activity, their body undergoes an accelerated metabolism, which means that enzyme reserves are also consumed intensively (figuratively, they can be compared to a candle burning at both ends).