What Are Enzymes: How These Enzymes Could Change Your Life

Enzymes: Definition, History, Nature, Structure, Classification, Functions

Enzyme Definition:

  • Enzymes are defined as they are the biocatalyst which enhance the rate of reaction by decreasing activation energy.

  • Enzymes are protein-rich substances that catalyze or speed up biological reactions.

  • Enzyme (E) is a protein that has catalytic properties in the reaction of converting a substrate (S) into a product (P).

What are Enzymes?

  • Enzymes are the biocatalyst which enhance the rate of reaction by decreasing activation energy.
  • Biological enzymes refer to organic substances that have catalytic functions.
  • Generally enzymes are produced by living cells and have a certain catalytic effect. 
  • The term enzyme is coined by Kuhne.
  • Study of enzymes is known as enzymology.
  • All enzymes are proteinous in nature except ribonuclease enzymes.
  • On the basis of what types of body reactions catalyze by enzymes they are divided into digestive And metabolic enzymes.
  • Enzymes are classified into six groups are oxidoreductases, transferases, hydrolases, , lyases, isomerases and ligases.
  • Some common examples of enzymes are lysozyme, protease, pectinase, lipase, amylase and cellulase.
  • Biological enzymes can be used in textile, petroleum, and food and pharmaceutical industries.
  • Enzymes take part in almost all vital processes of the human body: they support the hematopoietic system, reduce thrombosis, normalize blood viscosity, improve microcirculation, as well as the supply of tissues with oxygen and nutrients, normalize lipid metabolism etc.

History of Enzymes:

  • In 1833, Payen and Persoz obtained a substance that hydrolyze starch into sugar and named it diastase, which is now called amylase.
  • In 1836, T. Schwann extracted substances for digesting protein from gastric juice and solved the mystery of digestion.
  • In 1878, Wilhelm Friedrich Kuhne coined the term "enzyme".
  • In 1913, American scientists Michaelis and Menten proposed the equation of enzyme catalysis based on the intermediate product theory.
  • In 1926, for the first time American scientist Sumner extracted the crystals of urease from the seeds of Jack bean (Canavalia ensiformis L.). (First crystalize enzyme - Urease)
  • In the 1930s, scientists successively extracted protein crystals of various enzymes, and pointed out that enzymes are a class of proteins with biological catalysis.
  • In 1982, American scientists Cech and Altman found that a few RNAs also have catalytic activity and named it ribozyme. (Non proteinous enzyme)
  • In 1986, Schultz and Lerner successfully developed the antibody enzyme (abzyme).

Why Enzymes are Important?

  • Human body is a complex highly organized biological system, hundreds of biochemical reactions take place in it at the same time. 
  • These processes are very complex and cannot take place by their own. 
  • This is when the enzymes begin to work. 
  • They help a particular reaction to proceed in the desired sequence, which is inherent in us by nature. 
  • Enzymes speed up almost all chemical reactions that occur in cells. They have vital importance for humans, facilitate digestion and speed up metabolism.
  • Enzymes are present in the various cells of our body.
  • In a healthy person, the enzymatic composition of the blood serum is relatively constant; with a disease, the level of enzymes increases significantly.

Chemical Nature of Enzymes

  • Almost all enzymes are proteinous in nature with molecular weights ranging from 15,000 to several million Da. 
  • Except some Ribozyme and Ribonuclease enzymes.
  • Keep in mind all enzymes are proteins, but not all proteins are enzymes. Like other proteins, enzymes are also made up of amino acids.
  • According to the chemical structure enzymes are of two types simple enzymes and conjugate (Complex) enzymes.
  • A simple enzyme consists of only a peptide chain consisting of amino acid residues. This protein part of enzyme known as apoenzyme.
  • Complex enzymes consist both protein part and non-protein part.
  • The non - protein part of an enzyme is a Prosthetic group, Coenzyme or Cofactor.
  • Protein part (Apoenzyme) and non protein part (Cofactor) they together form a holoenzyme. 
  • Only the holoenzyme has catalytic activity. and if the two are separated, the enzyme activity disappears . 

Characteristics of Enzymes:

  • Specificity: Specific enzyme can only catalyze one or a class of substrates, such as protease can only catalyze the hydrolysis of proteins into polypeptides, Cellulase only used for cellulose breakdown, Urease only used to hydrolyze urea to decompose it into carbon dioxide and ammonia

  • Enzyme Diversity: There are many types of enzymes, about 4,000 kinds of enzymes have been discovered so far, and these enzymes categories into six major types.

  • Enzyme Efficiency: The catalytic efficiency of enzymes is higher than that of inorganic or chemical catalysts, making the reaction rate faster;

  • Enzyme Activity adjustability: Enzyme activity can regulate by inhibitor and activator regulation, feedback inhibition regulation, covalent modification regulation and allosteric regulation etc.

  • Volatility: Most enzymes are proteins, so they will be destroyed by high temperature, strong acid , strong alkali, etc.

  • Reaction Speed: Enzymes can speed up the chemical reaction, but the enzyme cannot change the equilibrium point of the chemical reaction, that is to say, while promoting the forward reaction, the enzyme also promotes the reverse reaction in the same proportion, so the function of the enzyme is to shorten the time required to reach the equilibrium. time, but the equilibrium constant remains unchanged;

  • Activation Energy: Enzymes reduce the activation energy to speed up the chemical reaction rate.

Structure of enzymes: Active Site:

  • Enzymes are macromolecules whose molecular weight is generally more than 10,000 and are composed of hundreds of amino acids. 
  • The substrate of an enzyme is generally small, and only a small part of the enzyme molecule directly contacts the substrate and plays a catalytic role. 
  • Even though some enzymes have larger substrates, only a small area is in contact with the enzyme. 
  • Therefore, we call the site where the enzyme molecule binds to the substrate and catalyzes the reaction as the active site of the enzyme.
  • The active site is composed of a few residues in the enzyme molecule. 
  • The amino acids in the active site can be divided into substrate binding sites and catalytic sites according to their functions.
  • Generally monomeric enzymes have only one active site, but some multifunctional enzymes have multiple active sites. 
  • Methods such as ultraviolet, fluorescence, and circular dichroism spectroscopy can also be used in the study of active site.

Classification of Enzymes

Enzymes are classified on the basis of their location, their chemical composition, on the basis of their works and on the basis of nature of reactions.

1. According to Location of Enzymes

According to location of enzymes are of two types intracellular enzymes and extracellular enzymes.

a. Intracellular Enzymes: Humans and mammals contain at least 5,000 enzymes. They are either dissolved in the cytoplasm, or combined with various membrane structures, or located at specific positions in other structures in the cell, and are activated only when needed. These enzymes are collectively referred to as intracellular enzymes; in addition, they also 

b. Extracellular Enzymes: There are some enzymes that are synthesized in the cell and then secreted outside the cell such enzymes are called as extracellular enzymes

2. According to chemical composition

a. Simple Enzymes: Enzymes that only consists of protein part except protein, do not contain other substances are called as simple enzymes. Such as urease, protease, amylase, lipase and ribonuclease etc.

b. Conjugated Enzymes: Conjugated enzymes consist of  proteins parts and some non-protein part. The protein part is called apoenzyme, and the non protein is called a cofactor. The complex formed is called holoenzyme, i.e. apoenzyme + cofactor = holoenzyme.

3. According to enzymes works in the body:

Enzymes are divided into three types: digestive enzymes, metabolic enzymes, and food enzymes

a. Digestive enzyme: Digestive enzymes are enzymes that help break down the food you eat so that it can be absorbed. Major enzymes include proteases (proteolytic enzymes) that degrade proteins into amino acids, amylases (carbohydrate-degrading enzymes) that degrade carbohydrates into glucose, and lipases (lipolytic enzymes) that decompose fats into fatty acids. It is further subdivided by the organs it consumes and the nutrients it decomposes.

b. Metabolic enzyme: Metabolic enzymes actually put the nutrients absorbed into the body to work. Various metabolic enzymes are at work in all aspects of human life activities, such as breathing, exercising, healing injuries, cell division, and skin metabolism.

c. Food enzyme: Food enzymes are enzymes found in foods. It aids in digestive enzymes and aids in better digestion. Food enzymes, which are abundant in fresh foods such as raw vegetables and fruits, sashimi, and fermented foods such as miso and natto, help digestion and play a role in preventing wasteful use of digestive enzymes in the body.

4. According to the nature/type of the reaction

In 1961, the International Union of Biochemistry and Molecular Biology (IUBMB) unified all enzymes into six categories according to the type of reaction they catalyze. In August 2018, the classification of translocases was added, so there are now seven major enzymes, namely: oxidase-reductase (EC 1), transferase (EC 2), hydrolase (EC 3), lyase (EC 4), isomerase (EC 5), ligase (EC 6) and translocase (EC 7). Where as EC stands for Enzyme Commission.

  • Oxidoreductases:  are enzymes that promote redox reactions of substrates, and are a class of enzymes that catalyze redox reactions.

  • Transferases: are enzymes that catalyze the transfer or exchange of certain groups (such as acetyl , methyl, amino, phosphate , etc.) between substrates. For example, methyltransferases, aminotransferases, acetyltransferases , transsulfases, kinases, and polymerases, among others.

  • Hydrolases: are enzymes that catalyze the hydrolysis of substrates. For example, amylases, proteases , lipases , phosphatases, glycosidases, and the like.

  • Lyases: are enzymes that catalyze a reaction that removes a group from a substrate (non-hydrolytically) leaving a double bond, or its reverse reaction. For example, dehydratase, decarboxylase, carbonic anhydrase , aldolase , citrate synthase , and the like. Many lyases catalyze a reverse reaction that forms new chemical bonds between two substrates and eliminates a substrate's double bond. Synthases fall into this category.

  • Isomerases: are enzymes that catalyze the mutual conversion between various isomers, geometric isomers or optical isomers. For example, isomerase, epimerase, racemase and the like.

  • Ligase: is an enzyme that catalyzes the synthesis of two molecules of substrates into one molecule of compound, and at the same time, the phosphate bond coupled with ATP is broken to release energy. For example, glutamine synthase , DNA ligase , amino acid : tRNA ligase, and biotin- dependent carboxylase, among others.

Class of Enzyme Functions (Biochemical Properties)
Oxidoreductases Oxidoreductase enzymes catalyzes the oxidation and reduction reaction where the electrons tend to travel from one form of a molecule to the other.
Transferases Transferase enzymes that catalyze the transfer or exchange of certain groups (such as acetyl , methyl, amino, phosphate , etc.) between substrates. For example, methyltransferases, aminotransferases, acetyltransferases , transsulfases, kinases, and polymerases, among others.
Hydrolases Hydrolases are hydrolytic enzymes, which catalyze the hydrolysis reaction by adding water to cleave the bond and hydrolyze it.
Lyases Lyases are enzymes that catalyze a reaction that removes a group from a substrate (non-hydrolytically) leaving a double bond, or its reverse reaction. For example, dehydratase, decarboxylase, carbonic anhydrase , aldolase , citrate synthase
Isomerases Isomerases are enzymes that catalyze the mutual conversion between various isomers, geometric isomers or optical isomers. For example, isomerase, epimerase, racemase
Ligases The Ligases enzymes are known to charge the catalysis of a ligation process. For example, glutamine synthase , DNA ligase , amino acid : tRNA ligase, and biotin- dependent carboxylase

Examples of Enzymes:

1. Alpha amylase:

  • Alpha-amylase (α-amylase, alpha amylase) is a digestive enzyme that involved in digestion of food and accelerates the breakdown of complex carbohydrates like starch and glycogen into its monomers,  
  • Alpha amylase also ensures the maintenance of normal blood sugar levels.
  • Most amylase in the human body is found in the pancreas and salivary glands. 
  • Accordingly, two types of a-amylase are determined in human blood serum: pancreatic (P-type), which is synthesized by the pancreas, and salivary amylase (S-type) - by the salivary glands.
  • An increase in α-amylase activity by 2 or more times can be regarded as a symptom of damage to the pancreatic tissue. 

2. Aspartate aminotransferase (AST)

  • This enzyme is located in almost all cells of the body, however, its favorite place of localization is the heart and liver, less of it in the kidneys and muscles. 
  • In healthy people, the level of AST in the blood is negligible. When symptoms of a liver or heart disease appear, it enters the bloodstream, and therefore an increase in the serum of this enzyme is an excellent indicator of the pathology of these organs.
  • Increase in the concentration of AST can cause myocardial infarction, infectious viral hepatitis, liver cancer, metastases, cirrhosis, sepsis etc.
  • A decrease in the concentration of aspartate aminotransferase in the blood serum is rare and has no special diagnostic value.

3. Alanine aminotransferase (ALT)

  • This enzyme is found in many cells of our body, but its highest concentration is determined in the cells of the liver, kidneys, in smaller quantities - in the heart, pancreas and skeletal muscles.
  • The concentration of AST in the blood serum of healthy people is low, in men the level of the enzyme is slightly higher than in women. 
  • However, when cells that are rich in this enzyme, such as the liver or kidney, are damaged or die, there is a sharp increase, so to speak, “release” of ALT into the circulatory system. 

4. Lipase:

  • Lipase enzymes are present in gastric juice, in pancreatic secretions, as well as in dietary fats and is the most important enzyme in the process of digestion of fats.
  • This enzyme is synthesized in the pancreas and released into the intestine, where it breaks down fats from food and hydrolyzes fat molecules. 
  • Lipase activity is significantly altered in diseases of the pancreas, cancer and malnutrition.

5. Metabolic enzymes

  • Enzymes that catalyze biochemical processes inside cells are known as metabolic enzymes.
  • During which both energy production and detoxification of the body and the removal of waste decay products occur. 
  • Each system, organ and tissue of the body has its own network of enzymes.

6. Lactate dehydrogenase (LDH):

  • Lactate dehydrogenase (LDH) is a zinc-containing enzyme that is involved in the oxidation of lactic acid. 
  • This enzyme is quite common in our body, it can be found in the kidney tissue, in the heart, in the skeletal muscles and, of course, in the liver.
  • In the body of a healthy person, there are five different forms - isoenzymes. 
  • They differ in chemical structure, location in the body. 
  • An increase in the concentration of LDH in the blood serum can also be determined under certain physiological conditions: in newborns, pregnant women, as well as during active sports.

7. Alkaline phosphatase:

  • Alkaline phosphatase (AP) is a blood serum enzyme that is widely distributed in human tissues. 
  • Its largest amount is found in the intestinal mucosa, osteoblasts (young bone cells that form the intercellular substance or matrix), the walls of the bile ducts, in the placenta and in nursing mothers in the lactating mammary gland.
  • The enzyme is localized outside the cell, or rather on its membrane and is involved in the transport of phosphorus.
  • The activity of liver alkaline phosphatase is most often increased due to damage to liver cells (hepatocytes) or due to a violation of the outflow of bile.

Factors Affecting Enzyme Activity
The ability of an enzyme to catalyze a chemical reaction is called enzymatic activity or active unit and this enzyme activity can be regulated and controlled by a variety of physical and chemical factors. Without the involvement of enzymes, metabolism is almost impossible to maintain. The enzymatic reaction rate is affected by the concentration of the enzyme, substrate, temperature, pH, activators and inhibitors.

(1) Enzyme concentration
  • Enzymatic reaction rate is directaly proportional to the concentration of enzyme molecules present in a reaction. 
  • When the concentration of substrate molecules is sufficient, the more enzyme molecules required to faster the substrate conversion. 
  • And when the enzyme concentration is high, this relationship is not maintained, and the curve gradually flattens. 

(2) Substrate concentration
  • In biochemical reactions, if the concentration of the enzyme is a fixed and the initial concentration of the substrate is low, the enzymatic reaction rate is proportional to the substrate concentration, that is, it increases with the increase of the substrate concentration. 
  • When all the enzymes combine with the substrate to generate intermediate products, even if the concentration of substrate is increased, the concentration of intermediate products will not increase, and the rate of enzymatic reaction will not increase.

(3) pH:
  • Enzymes exhibit activity within the optimum pH range, and greater or less than the optimum pH will reduce enzyme activity. 
  • Too high or too low pH will affect the stability of the enzyme, thereby causing the enzyme to suffer irreversible damage. 
  • The closer the pH of most enzymes in the human body is to 7, the better the catalytic effect. 
  • However, pepsin in the human body is suitable in an environment with a pH value of 1~2, and the optimal pH of trypsin is about 8.

(4) Temperature:
  • Various enzymes have the strongest enzymatic activity and the highest enzymatic reaction speed within the optimum temperature range. 
  • Within a suitable temperature range, the rate of enzymatic reaction can be increased by 1-2 times for every 10°C increase in temperature. 
  • The optimum temperature of enzymes in different organisms is different.
  • Too high or too low temperature will reduce the catalytic efficiency of the enzyme and simultaneously the speed of enzymatic reaction also reduce.
  • When enzymes whose optimum temperature is below 50°C, when the temperature reaches 60-80°C, most of the enzymes are destroyed and irreversible denaturation occurs and when the temperature is close to 90°C, the catalysis of enzymes is completely lost. 

(5) Inhibitors
  • Substances that can weaken, inhibit or even destroy enzyme activity are called enzyme inhibitors. 
  • These inhibitors slows down enzymatic reactions. 
  • Enzyme inhibitors can be heavy metal ions, carbon monoxide, hydrogen sulfide, fluoride, dyes alkaloids, dyes and surface active agent, etc.
  • The inhibition of enzymatic reactions can be divided into competitive inhibition and non-competitive inhibition. 
  • Substances similar in structure to the substrate compete to bind to the active center of the enzyme, thereby reducing the speed of the enzymatic reaction. This effect is called competitive inhibition. Competitive inhibition is reversible inhibition and Substances that are structurally similar to their substrates are called competitive inhibitors.
  • Non-competitive inhibition is irreversible, and increasing the substrate concentration does not relieve the inhibition of enzyme activity. Inhibitors that bind to sites other than the active center of the enzyme are called noncompetitive inhibitors.
  • Some substances can act as both an inhibitor of an enzyme and an activator of another enzyme.

Functions of Enzymes
  1. Enzymes play a very wide range of functions in living organisms.
  2. Enzymes takes place in all biochemical processes such as metabolism, nutrition and energy conversion of organisms. 
  3. All life processes are enzyme-catalyzed reactions.
  4. Enzymes breakdown the complex molecules into simple molecules that can be easily absorbed by the human body.
  5. Energy production through metabolic processes is one of the important function of enzymes. ATP synthase is the enzyme involved in the synthesis of energy.
  6. Enzymes maintain all the functions of the internal organs of body.
  7. Enzymes helps in cell repair, anti-inflammatory and detoxification, improving immunity and promoting blood circulation.
  8. Number of enzymes are used for enzyme therapy to treat and diagnose diseases such as trypsin, chymotrypsin etc.
  9. Enzymes such as protein kinase helps in signal transduction.
  10. Number of enzymes are used in detergents, soap, leather industry.
  11. Enzymes like amylase and cellulase are used to improved nutritional value of food.
  12. Many enzymes used in fermentation process.
  13. In the treatment of thrombophlebitis, myocardial infarction and pulmonary infarction verious enzymes like plasmin, streptokinase, urokinase, etc, are used.
  14. Enzymes Protease used for protein breakdown, Lipase used for lipid breakdown, Cellulase used for cellulose breakdown, Urease used to hydrolyze urea to decompose it into carbon dioxide and ammonia
  15. Enzymes also takes place in movement, produce muscle contractions by catalyzing the hydrolysis of ATP on myosin , and are involved in the transport of intracellular substances as part of the cytoskeleton. 
  16. ATPases enzyme located on the cell membrane that are involved in active transport as ion pumps.

Frequently Asked Questions on Enzymes:

What is an enzyme?
Answer: Various chemical reactions take place in the body. Enzymes are proteins that act as catalysts for each reaction. Enzymes are essential for digestion, absorption, and metabolism of the food ingested by living organisms, including humans, and for most of the chemical reactions that occur in the body. However, each enzyme can only catalyze a specific reaction. For example, enzymes that break down proteins can only break down proteins, not starches or lipids. In order to decompose starch and lipids, another enzyme exists, and each can only decompose starch and lipids. This is called enzyme specificity. Therefore, it is said that there are about 5,000 types of enzymes in the human body.

Where are enzymes are produced?
Answer: Enzymes are proteins they are produced in the substrates of stroma and mitochondria in the cytoplasm and chloroplast. 

What enzymes do?
Answer: Enzymes are essential substances for health and beauty, as they work to digest, absorb, decompose, and excrete food, promote metabolism, and regulate hormone balance. An enzyme found in raw vegetables and fruits, fish and meat, and fermented foods. It aids digestion, prevents the decrease of digestive enzymes, activates the function of metabolic enzymes, and promotes metabolism.

What happens if you don't have enough enzymes?
Answer: A lack of enzymes slows down your metabolism. As a result, substances that have not been metabolized accumulate in the blood, and the blood flow may become poor. When the blood flow is poor, the heat cannot be carried to every corner of the hands and feet, resulting in a drop in body temperature. It is said that when the body temperature drops, the activity of the enzyme is halved.

What are the industrial applications of enzymes?
Answer: Due to the availability and fast growth rate enzymes have a wide range of industrial applications. Industries like cosmetics, leather, detergent, dairy, baking, beverage, animal feed, polymer and waste management highly use enzymes.

Why are enzymes good for the body?
Answer: If there are many enzymes in the body , the metabolism will be active, the digestion of the stomach and intestines will be aided, and the absorption and digestion of nutrients will be smooth. On the other hand, if there are not enough enzymes , the toxins in the body will not be discharged, which will put a burden on the internal organs and may cause various poor physical conditions due to the deterioration of the gastric and intestinal phases.

What are the health benefits of enzymes?
Answer: Enzymes are involved in almost all reactions that occur in the body, so if the amount of enzymes produced in the body is low, there is a possibility that the health of the body will deteriorate. Like other proteins, enzymes are synthesized in the body based on genetic information, but the ability to synthesize enzymes declines with age. As a result, the elderly are less able to digest and metabolize.

Although the use of food-derived enzymes to aid digestion is still controversial, digesting and absorbing what you eat requires a lot of energy, and excess food cannot be digested. It is true that the situation you have to do puts a strain on the digestive organs such as the stomach and intestines. Especially for the elderly, it is important for their health to eat meals that take care of their stomachs so as not to put a burden on the digestive system.

Related Posts

Subscribe Our Newsletter