Applications Of Enzymes

What are Enzymes?

With the exception of a few classes of catalytic RNA molecules, all enzymes are proteins. Their catalytic activity depends on their native protein conformation. If an enzyme is denatured or dissociated into its subunits, catalytic activity is usually lost. If an enzyme is broken down into its component amino acids, its catalytic activity is always destroyed. Thus the primary, secondary, tertiary, and quaternary structures of enzymes are essential to their catalytic activity. Some enzymes require no chemical groups for activity whereas others require an additional chemical component.

Types of Enzymes

Many enzymes have been named by adding the suffix “-ase” to the name of their substrate or to a word or phrase describing their activity. Enzymes are divided into six classes based on the type of reaction catalyzed.

• Lyases - Cleavage of C—C, C—O, C—N, or other bonds by elimination, leaving double bonds or rings, or addition of groups to double bonds

• Ligases - Formation of C—C, C—S, C—O, and C—N bonds by condensation reactions coupled to cleavage of ATP or similar cofactor

• Isomerases - Transfer of groups within molecules to yield isomeric forms

• Hydrolases - Hydrolysis reactions (transfer of functional groups to water)

• Transferases - Group transfer reactions

• Oxidoreductases - Transfer of electrons (hydride ions or H atoms)

The most crucial jobs that enzymes perform are many bodily processes, including digestion, respiration, excretion, reproduction, liver and kidney function, as well as many other biological processes.

Application of Enzymes

Enzymes are also known as biological catalysts that help in speeding up the chemical reactions which take place inside living organisms. They play a very important role in chemical reactions especially when it comes to the industrial application of enzymes. Some of the better points are discussed below regarding the application of enzymes:

• Enzymes are used in blood tests and the detection of diseases such as glucose oxidase in the case of diabetes.

• Enzymes like amylase and proteases are studying the fermentation process of baking and some dairy products.

• The application of enzymes in biochemistry also becomes important when we talk about medicines and their benefits to our bodies.

Enzymes in the Biochemistry and Industry

Enzymes play an important role in biochemistry where they act as catalysts in the biochemical reactions that take place. It is also used to recognise diseases and their therapeutic procedure.

There are also several applications of enzymes in biochemistry and industries for organic synthesis and production of essential compounds in medicines and research. Some of the basic application of enzymes in biochemistry is discussed below:

• Fibrinolytic enzymes like nattokinase are used in the treatment of thrombosis.

• Enzymes are also used in the treatment of diabetes while testing the disease and looking for its detection.

• Proteolytic enzymes help in the removal of dead tissues and treat burnt areas.

• Lipase is also used in producing active alcohols and acids.

• Tyrosinase and DOPA are important enzymes which are used in Neurotherapy for treating diseases like Parkinson's disease.

Some of the other major Applications of enzymes are discussed below:

• Enzymes are the organic instruments of nature and are necessary for every type of life on earth.

• In the production and improvement of 400 to 500 common consumer and commercial goods, enzymes are used.

• By creating environmentally benign goods, enzymes are effective tools that support a clean environment in many ways.

• They are also utilised in a wide range of technical processes, including the creation of dishwashing soaps and detergents, recycling paper and paper goods to remove ink, and laundering clothes to remove stains and lengthen the life of the fabric.

• Enzymes are used to make a wide range of food products, beverages, animal nutrition, household goods, biofuels and other types of car fuel, cleaning supplies, and energy production facilities.

Factors Affecting Enzyme Activity

• Temperature: Enzyme activity generally increases with rising temperature because molecules move faster and collide more frequently. However, beyond an optimum temperature, which sharply decreases activity.

• pH: Each enzyme has an optimum pH where it functions best. Deviations from this range alter the ionic bonds and hydrogen bonds holding the enzyme’s structure, leading to reduced efficiency or complete inactivation.

• Substrate concentration: At low substrate concentration, the reaction rate increases proportionally as more enzyme-substrate complexes form.

• Enzyme concentration: Higher enzyme concentration provides more active sites for substrates, increasing the reaction rate.

Enzymes in Exams (CBSE, NEET, Paramedical)

During exam preparation, different types of questions about the Application of Enzymes are asked. The table below contains the various patterns of questions asked in other exams.

Tips, Tricks & Mnemonics

It takes effort to remember everything in a single go. We made the entire problem easy. Some of the tricks regarding the application of enzymes are given below which you can use to memorise the important points.

Applications of Enzymes

TAME: Therapeutic, Analytical, Metabolic, Environmental

• T: Therapeutic applications (enzymes in medicine, e.g., proteases for burns, fibrinolytics for clots).

• A: Analytical tools (enzymes in diagnostic tests like ELISA and glucose oxidase for diabetes).

• M: Metabolic processes (enzymes in metabolic pathways, e.g., glycolysis, Krebs cycle).

• E: Environmental uses (enzymes in bioremediation to break down pollutants).

Enzyme Classes

HOPED: Hydrolases, Oxidoreductases, Transferases, Lyases, Isomerases

• H: Hydrolases (break down substrates with water, e.g., proteases).

• O: Oxidoreductases (catalyze oxidation-reduction reactions, e.g., dehydrogenases).

• P: Transferases (transfer functional groups, e.g., kinases).

• E: Lyases (add or remove groups without hydrolysis, e.g., decarboxylases).

• D: Isomerases (catalyze isomerization changes, e.g., racemases).

Enzyme Kinetics

MR.K: Michaelis-Menten, Rate, Km, Vmax

• M: Michaelis-Menten equation (describes rate of enzymatic reactions).

• R: Reaction rate (depends on substrate concentration and enzyme activity).

• K: Km (Michaelis constant, substrate concentration at half Vmax).

• V: Vmax (maximum reaction velocity when the enzyme is saturated).

Factors Affecting Enzyme Activity

T.P.H: Temperature, pH, Inhibitors

• T: Temperature (increased temperature generally increases activity until denaturation).

• P: pH (each enzyme has an optimal pH for activity).

• H: Inhibitors (competitive and non-competitive affect enzyme activity).

Enzymes NEET MCQs

Q1. The active site of the enzyme is present in which level of organization of proteins (enzymes)?

1. Primary

2. Secondary

3. Tertiary

4. Quaternary

Correct answer: 3) Tertiary

Explanation:

The active site of an enzyme is at the tertiary level of protein organization. The tertiary structure is the general three-dimensional shape of a protein, which is created through the folding of its polypeptide chain. An active site is a region within this structure where an enzyme interacts with its substrate to catalyze a chemical reaction.

Hence, the correct option is 3) Tertiary.

Q2. Consider the following statements A, B, and C. Which of the following options accurately represents the statements?

Statement A: All enzymes exhibit a proteinaceous nature.

Statement B: Certain competitive inhibitors are frequently employed to manage bacterial pathogens.

Statement C: The active site of an enzyme is formed through the intricate folding of the protein's tertiary structure.

1. Statements A and B are correct.

2. Statements B and C are correct.

3. Statements A and C are correct.

4. All of the above

Correct answer: 2) Statements B and C are correct

Explanation:

Statement B states that some competitive inhibitors are commonly used to control bacterial pathogens. This statement is accurate because competitive inhibitors can bind to the active site of an enzyme and compete with the substrate, effectively inhibiting the enzyme's activity. In the context of bacterial pathogens, competitive inhibitors can be employed to target specific enzymes necessary for bacterial survival or growth, providing a means of controlling the pathogens.

Statement C asserts that the active site of an enzyme is formed through the intricate folding of its protein's tertiary structure. This statement is also accurate. The active site of an enzyme is the region where substrate molecules bind and undergo catalysis. It is typically formed by specific amino acid residues that come together in the folded structure of the protein, which includes the tertiary structure. The precise folding of the protein is crucial for creating the functional active site and facilitating enzyme-substrate interactions.

Hence the correct answer is Option 2) Statements B and C are correct.

Q3. Select the correct statement

1. All enzymes are proteins

2. All proteins are enzymes

3. Enzymes and proteins are same molecule

4. Protein helps in building enzymes

Correct answer: 1) All enzymes are proteins

Explanation:

As we have learned

The enzymes are actually proteins with catalytic power which hastens the rate of a given metabolic reaction.

Hence the correct answer is Option 1) All enzymes are proteins.

Also Read:

• MCQs on Enzymes

• Biomolecules

• Cell Cycle And Cell Division

FAQs on Enzymes

Define enzymes.

Enzymes are biological catalysts made up of proteins (and sometimes RNA) that speed up chemical reactions in living organisms without being consumed in the process. They lower the activation energy required for reactions, making them proceed faster and under mild biological conditions. Each enzyme is highly specific for its substrate and plays a vital role in metabolism, digestion, respiration, and other cellular activities.

What are the types of enzymes?

Enzymes are classified into six major categories based on the type of reaction they catalyze:

1. Oxidoreductases – catalyze oxidation-reduction reactions (e.g., dehydrogenases).

2. Transferases – transfer functional groups from one molecule to another.

3. Hydrolases – break bonds using water (e.g., proteases, lipases).

4. Lyases – add or remove groups without hydrolysis (e.g., decarboxylases).

5. Isomerases – rearrange atoms within a molecule (e.g., isomerases, mutases).

6. Ligases (synthetases) – join two molecules using ATP (e.g., DNA ligase).
   
   

What are the applications of enzymes?

Enzymes have wide applications in biological, medical, and industrial fields. In medicine, they are used for diagnosis (e.g., liver function tests), as therapeutic agents (e.g., streptokinase for dissolving clots), and in drug manufacture. In industry, enzymes are used in food processing (amylase in brewing, proteases in detergents, lactase in dairy), textile processing, and biofuel production. In agriculture, they enhance soil fertility and crop protection.

What factors affect enzyme activity?

Enzyme activity is influenced by several factors:

• Temperature: activity increases with temperature up to an optimum, then decreases due to denaturation.

• pH: each enzyme has an optimum pH; deviations reduce activity.

• Substrate concentration: increasing substrate increases activity until saturation is reached.

• Enzyme concentration: more enzyme molecules increase reaction rate.

• Cofactors/coenzymes: some enzymes need additional molecules like vitamins or metal ions for activity.