ENZYMES

Enzyme, a substance that acts as a Catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process.

The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes. Without enzymes, many of these reactions would not take place at a perceptible rate. Enzymes catalyze all aspects of cell Metabolism.

Chemical nature of enzymes

All enzymes were once thought to be proteins, but since the 1980s the catalytic ability of certain nucleic acids, called ribozymes (or catalytic RNAs), has been demonstrated, refuting this axiom. Because so little is yet known about the enzymatic functioning of RNA, this discussion will focus primarily on protein enzymes.

A large protein enzyme molecule is composed of one or more amino acid chains called polypeptide chains. The amino acid sequence determines the characteristic folding patterns of the protein’s structure, which is essential to enzyme specificity. If the enzyme is subjected to changes, such as fluctuations in temperature or pH, the protein structure may lose its Integrity (denature) and its enzymatic ability. Denaturation is sometimes, but not always, reversible.

Bound to some enzymes is an additional chemical component called a cofactor, which is a direct participant in the catalytic event and thus is required for enzymatic activity. A cofactor may be either a coenzyme—an organic molecule, such as a vitamin—or an inorganic Metal ion; some enzymes require both. A cofactor may be either tightly or loosely bound to the enzyme. If tightly connected, the cofactor is referred to as a prosthetic group.

Impact of temperature on Enzymes

As the temperature increases, so does the rate of reaction. But very high temperatures denature enzymes. The graph shows the typical change in an enzyme’s activity with increasing temperature. The enzyme activity gradually increases with temperature until around 37ºC, or body temperature. Then, as the temperature continues to rise, the rate of reaction falls rapidly, as heat energy denatures the enzyme.

Industrial applications of Enzymes

Enzymes are used in the chemical Industry and other industrial applications when extremely specific catalysts are required. However, enzymes in general are limited in the number of reactions they have evolved to catalyze, and by their lack of stability in organic solvents and at high temperatures. As a consequence, protein engineering is an active area of research and involves attempts to create new enzymes with novel properties, either through rational design or in vitro evolution. These efforts have begun to be successful, and a few enzymes have now been designed “from scratch” to catalyze reactions that do not occur in nature.

In Food Processing, the enzymes used include amylases from Fungi and Plants. These enzymes are used in the production of sugars from starch, such as in making high-fructose corn syrup. In baking, they catalyze the breakdown of starch in the flour to sugar. Yeast Fermentation-2/”>Fermentation of sugar produces the carbon dioxide that raises the dough. Proteases are used by biscuit manufacturers to lower the protein level of flour. Trypsin is used to predigest baby foods. For the processing of fruit juices, cellulases and pectinases are used to clarify fruit juices. Papain is used to tenderize meat for cooking.

In the Dairy industry, rennin, derived from the stomachs of young ruminant animals (like calves and lambs) is used to manufacture of cheese, used to hydrolyze protein. Lipases are implemented during the production of Roquefort cheese to enhance the ripening of the blue-mold cheese. Lactases are used to break down lactose to glucose and galactose.

In the brewing industry, enzymes from barley are released during the mashing stage of beer production. They degrade starch and proteins to produce simple sugar, amino acids, and peptides that are used by yeast for fermentation. Industrially-produced barley enzymes are widely used in the brewing process to substitute for the natural enzymes found in barley. Amylase, glucanases, and proteases are used to split polysaccharides and proteins in the malt. Betaglucanases and arabinoxylanases are used to improve the wort and beer filtration characteristics. Amyloglucosidase and pullulanases are used for low-calorie beer and adjustment of fermentability. Proteases are used to remove Cloudiness produced during storage of beers.

In the starch industry, amylases, amyloglucosideases, and glucoamylases convert starch into glucose and various syrups. Glucose isomerase converts glucose into fructose in production of high-fructose syrups from starchy materials. In the paper industry, amylases, xylanases, cellulases, and ligninases are used to degrade starch to lower viscosity, aiding sizing and coating paper. In the biofuel industry, cellulases used to break down cellulose into sugars that can be fermented.

In the production of biological detergents, proteases, produced in an extracellular form from bacteria, are used in pre-soak conditions and direct liquid applications, helping with the removal of protein stains from clothes. In molecular biology, restriction enzymes, DNA ligase, and polymerases are used to manipulate DNA in Genetic engineering, important in pharmacology, agriculture and medicine, and are essential for restriction digestion and the polymerase chain reaction. Molecular biology is also important in forensic science.

Enzymes are proteins that catalyze, or speed up, chemical reactions. They are essential for life, as they are responsible for catalyzing the reactions that allow cells to function. Enzymes are highly specific, meaning that they only catalyze a certain type of reaction. This specificity is due to the shape of the enzyme’s active site, which is a pocket or groove on the surface of the enzyme where the reactants (substrates) bind. The active site is lined with amino acids that have specific shapes and charges that interact with the substrates in a way that promotes the reaction.

Enzymes can be regulated in a number of ways. One way is through allosteric regulation, which is when the binding of a molecule to a site on the enzyme other than the active site affects the activity of the enzyme. For example, the enzyme phosphofructokinase is regulated by the molecule fructose 2,6-bisphosphate. When fructose 2,6-bisphosphate binds to phosphofructokinase, it activates the enzyme, making it more likely to catalyze the reaction.

Another way that enzymes can be regulated is through the presence of cofactors. Cofactors are non-protein Molecules that are required for the activity of some enzymes. Cofactors can be either inorganic ions, such as magnesium ions, or organic molecules, such as VITAMINS.

Enzymes can also be inhibited by a number of different molecules. One type of inhibition is competitive inhibition, which is when a molecule that is similar in structure to the substrate binds to the active site of the enzyme and prevents the substrate from binding. For example, the drug aspirin inhibits the enzyme cyclooxygenase, which is responsible for the production of prostaglandins. Prostaglandins are involved in inflammation and pain, so by inhibiting cyclooxygenase, aspirin can reduce inflammation and pain.

Another type of inhibition is noncompetitive inhibition, which is when a molecule binds to the enzyme at a site other than the active site and changes the shape of the active site so that it can no longer bind to the substrate. For example, the drug cyanide inhibits the enzyme cytochrome oxidase, which is responsible for the final step in the electron transport chain. The electron transport chain is responsible for producing ATP, which is the cell’s energy currency. By inhibiting cytochrome oxidase, cyanide can prevent the cell from producing ATP, which can lead to cell death.

Enzymes are essential for life, and they play a role in almost every Chemical Reaction that takes place in the cell. Enzymes are highly specific and can be regulated in a number of ways. Enzymes can be inhibited by a number of different molecules, but they are also essential for the production of ATP, which is the cell’s energy currency.

Active site: The active site is a pocket or groove on the surface of an enzyme where the reactants (substrates) bind. The active site is lined with amino acids that have specific shapes and charges that interact with the substrates in a way that promotes the reaction.

Allosteric regulation: Allosteric regulation is when the binding of a molecule to a site on the enzyme other than the active site affects the activity of the enzyme.

Cofactor: A cofactor is a non-protein molecule that is required for the activity of some enzymes. Cofactors can be either inorganic ions, such as magnesium ions, or organic molecules, such as vitamins.

Competitive inhibition: Competitive inhibition is when a molecule that is similar in structure to the substrate binds to the active site of the enzyme and prevents the substrate from binding.

Enzyme kinetics: Enzyme kinetics is the study of how enzymes work. Enzyme kinetics can be used to determine the rate of a reaction, the affinity of an enzyme for its substrate, and the maximum rate that an enzyme can catalyze a reaction.

Enzyme regulation: Enzyme regulation is the process by which the activity of enzymes is controlled. Enzyme regulation can occur through a number of different mechanisms, including allosteric regulation, cofactor binding, and inhibition.

Induced fit: Induced fit is a model that describes how the active site of an enzyme changes shape when the substrate binds. The induced fit model suggests that the active site is initially in a relaxed state, but when the substrate binds, the active site changes shape to better accommodate the substrate.

Lock and key model: The lock and key model is a model that describes how the active site of an enzyme interacts with the substrate. The lock and key model suggests that the active site is a rigid structure that fits perfectly with the substrate, like a key fits into a lock.

MichaelisâMenten kinetics: MichaelisâMenten kinetics is a mathematical model that describes the rate of an enzyme-catalyzed reaction. The MichaelisâMenten equation can be used to determine the rate of a reaction, the affinity of an enzyme for its substrate, and the maximum rate that an enzyme can catalyze a reaction.

Noncompetitive inhibition: Noncompetitive inhibition is

What are proteins?

Proteins are large molecules that are essential for the structure and function of all living things. They are made up of amino acids, which are linked together in a chain. The sequence of amino acids determines the shape and function of the protein.

What are the different types of proteins?

There are many different types of proteins, each with its own unique function. Some proteins are structural, meaning they provide support and structure to cells and Tissues. Other proteins are enzymes, which are molecules that speed up chemical reactions. Still other proteins are HORMONES, which are molecules that regulate the activity of other cells.

What are the functions of proteins?

Proteins have many different functions in the body. Some of the most important functions of proteins include:

Structure: Proteins provide support and structure to cells and tissues.
Enzymes: Proteins are molecules that speed up chemical reactions.
Hormones: Proteins are molecules that regulate the activity of other cells.
Antibodies: Proteins that protect the body from infection.
Transport: Proteins transport molecules around the body.
Storage: Proteins store energy and other molecules.
Movement: Proteins help the body move.

What are the sources of proteins?

Proteins can be found in a variety of foods, including meat, Poultry, fish, eggs, dairy products, beans, nuts, and seeds. Some plant-based proteins are incomplete proteins, meaning they do not contain all of the essential amino acids that the body needs. However, by combining different plant-based proteins, you can create a complete protein.

How much protein do I need?

The amount of protein you need depends on your age, sex, activity level, and overall Health. The Recommended Dietary Allowance (RDA) for protein is 0.8 grams per kilogram of body weight. However, athletes and people who are trying to build muscle may need more protein.

How do I get enough protein?

There are many ways to get enough protein. You can include protein-rich foods in your meals and snacks, or you can take a protein supplement. If you are trying to lose weight, you may want to focus on lean protein sources, such as chicken, fish, beans, and lentils.

What are the benefits of getting enough protein?

Protein has many benefits for health. It can help you build and maintain muscle mass, repair tissue, and boost your immune system. Protein can also help you feel full and satisfied after meals, which can help you manage your weight.

What are the risks of not getting enough protein?

If you do not get enough protein, you may experience fatigue, muscle weakness, and hair loss. You may also be at increased risk for infection and other health problems.

What are the side effects of too much protein?

In general, it is not harmful to eat too much protein. However, if you eat a very high-protein diet, you may experience some side effects, such as:

Nausea
Vomiting
Diarrhea
Constipation
Kidney stones
Weight gain

If you experience any of these side effects, you should talk to your doctor.

What are some common myths about protein?

There are many common myths about protein. Some of these myths include:

You need to eat a lot of protein to build muscle.
You need to eat a lot of protein to lose weight.
Protein is bad for your kidneys.
Protein can make you fat.

These myths are not true. You do not need to eat a lot of protein to build muscle or lose weight. Protein is not bad for your kidneys. And protein can help you lose weight if you are trying to do so in a healthy way.

What is the best way to get protein?

The best way to get protein is to eat a variety of protein-rich foods. Some good sources of protein include:

Meat
Poultry
Fish
Eggs
Dairy products
Beans
Nuts
Seeds

You can also get protein from protein supplements. However, it is important to talk to your doctor before taking any supplements.

Which of the following is a type of enzyme?
(A) Lipase
(B) Amylase
(C) Pepsin
(D) All of the above
Enzymes are proteins that:
(A) Speed up chemical reactions
(B) Are not consumed in the reactions they catalyze
(C) Are specific for the reactions they catalyze
(D) All of the above
The active site of an enzyme is a:
(A) Pocket or groove on the surface of the enzyme where the substrate binds
(B) Region of the enzyme that is responsible for catalysis
(C) Both (A) and (B)
The rate of an enzyme-catalyzed reaction is affected by:
(A) The concentration of the enzyme
(B) The concentration of the substrate
(C) The temperature
(D) All of the above
The process of enzyme inhibition can be:
(A) Competitive
(B) Noncompetitive
(C) Both (A) and (B)
Competitive inhibition occurs when:
(A) A molecule that resembles the substrate binds to the active site of the enzyme
(B) The inhibitor binds to a site on the enzyme other than the active site
(C) Both (A) and (B)
Noncompetitive inhibition occurs when:
(A) A molecule that resembles the substrate binds to the active site of the enzyme
(B) The inhibitor binds to a site on the enzyme other than the active site
(C) The inhibitor changes the shape of the active site so that the substrate cannot bind
Which of the following is an example of a competitive inhibitor?
(A) Aspirin
(B) Cyanide
(C) Both (A) and (B)
Which of the following is an example of a noncompetitive inhibitor?
(A) Aspirin
(B) Cyanide
(C) Both (A) and (B)
Which of the following is true about the activity of enzymes?
(A) Enzymes are denatured by heat
(B) Enzymes are denatured by pH extremes
(C) Enzymes are denatured by organic solvents
(D) All of the above
Which of the following is a way to prevent enzyme denaturation?
(A) Use a buffer to maintain a constant pH
(B) Use a low temperature
(C) Use a non-denaturing organic solvent
(D) All of the above
Which of the following is a way to increase the activity of enzymes?
(A) Increase the concentration of the enzyme
(B) Increase the concentration of the substrate
(C) Increase the temperature
(D) All of the above
Which of the following is a way to decrease the activity of enzymes?
(A) Decrease the concentration of the enzyme
(B) Decrease the concentration of the substrate
(C) Decrease the temperature
(D) All of the above
Which of the following is true about the specificity of enzymes?
(A) Enzymes are specific for the type of reaction they catalyze
(B) Enzymes are specific for the type of substrate they bind to
(C) Enzymes are specific for the conformation of the substrate they bind to
(D) All of the above
Which of the following is an example of an enzyme that is specific for the type of reaction it catalyzes?
(A) Amylase
(B) Lipase
(C) Pepsin
(D) All of the above
Which of the following is an example of an enzyme that is specific for the type of substrate it binds to?
(A) Amylase
(B) Lipase
(C) Pepsin
(D) All of the above
Which of the following is an example of an enzyme that is specific for the conformation of the substrate it binds to?
(A) Amylase
(B) Lipase
(C) Pepsin
(D) None of the above
Which of the following is true about the active site of an enzyme?
(A) The active site is a pocket or groove on the surface of the enzyme where the substrate binds
(B) The active site is a region of the enzyme that is responsible for catalysis
(C) The active site is both a pocket or groove on the surface of the enzyme and a region of the enzyme that is responsible for catalysis
(D) None of the above
Which of the following is true about the mechanism of enzyme catalysis?
(A) Enzymes catalyze reactions by lowering the activation energy