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1 year ago (08/03/21) 281 Views

Enzyme Profile Details

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You can learn everything by reading this post:

What is an enzyme?

 

History of the discovery of enzymes!

 

The chemical nature of the enzyme!

 

How enzymes work!

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Enzyme effect process!

 

Enzyme control!

 

Enzyme naming!

 

Types of enzymes!

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Enzymes in the body!

 

Enzymes in the industry!

 

So let’s get started.

 

What is an enzyme?

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In a word, enzymes are biological agents or enzymes. Influencers are chemical compounds that can increase or decrease the speed of a chemical reaction. We need to know that there are two basic conditions of life:

* Every living thing must have the ability to make similar offspring.

* Organisms must have the ability to control and affect the biochemical reactions that take place in their bodies.

The reason for saying these conditions is that enzymes play an important role in both of these basic things in life. That is why enzymology can be called a central subject of life. Enzymes have a role to play in everything from the survival of the organism to the creation of offspring and the incorporation of its dead body into nature after death. You will agree with me only after reading the whole article about enzymes.

Think of food and digestion. If you notice a little, you will understand that most of the foods we eat are very complex, hard type. Because we have teeth, we can easily tear these hard foods to pieces. Then I press it on the palate with my tongue and send it to the stomach. Then? Then what are these complex complex food objects? We eat food to nourish our body cells. But we are not taking nutrition directly. How many pieces of hard food are we giving? Cells no longer have sharp teeth like ours, that they would break them down and separate the nutrients. In fact, the solid foods we send are converted into simple nutrients through a number of chemical reactions through a physiological process called digestion. Cells can then absorb them.

Each of these digestive reactions contains multiple different types of enzymes. One by one enzymes work on one type of food. Amylase, maltase on sugary foods. Trypsin, renin on protein foods. Lipase on fat. In addition to food intake, enzymes also play a role in our cell division. An important factor in cell division is the replication of cell DNA (the process by which exact copies of DNA are made). Different types of enzymes play a role in this replication process. Such as: DNA polymerase, helix, ligase, epimerase etc. And as cells divide, our bodies grow, we can produce our offspring. In this way enzymes are very important for almost all the physiological processes in our life.

Due to the enzymes, these biochemical reactions happen very fast. Without enzymes, these reactions would have been very slow. This can make our death impossible. Enzymes can increase the speed of a reaction by hundreds to millions
of times.

For example: orotidine 5-phosphate decarboxylase enzyme can cause its associated chemical reaction in a few milliseconds. But without the enzyme, the reaction would take millions of years to complete. This religion of enzymes is called its influence religion. Usually a specific enzyme acts on certain chemical compounds. This religion is called substrate specificity.

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The compound on which the enzyme works is called a substrate. Some chemical compounds that inhibit the activity of enzymes are called inhibitors. For example: various drugs, poisons. Some chemical compounds increase the activity of enzymes called activators. Such as hexokinase-1.

History of Enzyme Discovery

 

In the late seventeenth and early eighteenth centuries, people knew that meat was digested under the influence of a type of juice secreted in the stomach, and that saliva and a substance in the body of plants broke down starch into simple sugars. But there was no knowledge of how it happens in any process. The first digestive enzyme was discovered in 1833 by the French chemist Ansalme Payne. Decades later, Louis Pasteur studied the process of making alcohol from fermentation into sugars, saying that the fermentation process is caused by a biological force (fermentation force) inside the yeast fungus. And these ferments are found only inside the organism.

                     picture : Louis Pasteur

 

In 1877 the German physiologist Ulhem first used the term enzyme. The term enzyme was later used to refer to some of the external factors of the organism, such as pepsin, and the internal factors of the organism were called fermentes. Edward Bachner wrote a paper in 1897 on the research on the yeast fungus.

                picture : Edward Bachner

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After a series of experiments at the University of Berlin, he discovered that the fermentation process of sugar was possible by only a fraction of it, without living yeast cells. The enzyme that works in this process is called zymez. He was awarded the Nobel Prize in 1907 in recognition of his ability to carry out fermentation without living cells.The enzyme naming is done by adding ‘edge’ at the end of the name of the corresponding reaction substrate following Bakhnar. For example: Lactase enzyme works on lactose. Enzymes are also named according to the type of reaction. The enzyme in the DNA polymerization reaction is called DNA polymerase.

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The chemical nature of the Enzyme

 

The biochemical nature of the enzyme was not clear until the early 1900s. Many scientists have noticed that the properties of enzymes are similar to those of proteins. But some scientists, such as Nobel laureate Richard Wilstratt, believed that proteins could act as carriers of enzymes, but that proteins alone had no effect.In 1926, James B. Summer showed that the urease enzyme is a pure protein and he made a crystal of this enzyme.

               pictureJames B. Summer

 

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In 1937, he similarly worked with the catalase enzyme to show that it was also a protein. O’Dell Stanley and John Howard, working with the enzymes pepsin, trypsin, and chymotrypsin, theorized that there could be some pure protein enzymes. These two scientists won the Nobel Prize in Chemistry in 1946.Finally the lysozyme enzyme is crystallized using the X-ray crystallography method. Lysozyme enzyme is present in tears, saliva, egg whites. This enzyme breaks down the bacterial coat protein. Since then, enzymes have been thought of as proteins.But in the 1980s, it became known that some ribo nucleic acids (RNAs) had enzyme-like effects. These are called ribozymes. Ribozymes (ribonucleic acid enzymes) are RNA molecules that have the ability to affect certain biochemical reactions (especially RNA splicing).In 1982, Sidney Altman discovered ribozymes. He said that RNA molecules can exhibit both genetic material and dominant properties.

 

                               picture : Ribozyme

Since then all enzymes are proteins, this idea has to be overcome. These enzymes are called protein enzymes. These are basically polypeptide chains made up of many amino acids. The properties of enzymes depend on the sequence of amino acids. The effectiveness of the enzyme depends on the temperature and pH.Each enzyme has a specific optimal temperature and pH. At higher temperatures than the optimum temperature, the enzyme becomes denatured (the three-dimensional structure of the enzyme is lost and its effectiveness decreases).

Enzymes Optimal temperature Favorable pH
Pepsin 40° Celsius 1.5-2.0
Protease 50° Celsius 8-9
Lipase 40° Celsius 7.0
Alpha-amylase 40° Celsius 8.0
Ureas 60° Celsius 7.0
Sucrose 40°  Celsius 6.2

 

Optimal temperature and pH of some enzymes Some enzymes have some aprotein components in addition to their protein components. These are called cofactors. The cofactor may contain an inorganic metal ion or may contain an organic component (co-enzyme) such as a vitamin.The cofactor may be strongly or weakly associated with the enzyme. These are called prosthetic groups when tightly attached
 
How Enzymes work
 
The enzyme must be attached to the substrate to affect any chemical reaction. I have already said that the substrate is specific for a specific enzyme. Each enzyme has a separate substrate binding site. Only a substrate that has a site that complements the binding site of a particular enzyme can be attached to that enzyme.Much like a lock key. In addition, specific enzymes may be added to a specific substrate based on complementary charges or hydrophilic or hydrophobic properties. Thus the different types of enzyme binding to the substrate are chemoselective, regioselective and stereoselective.
 
Some enzymes have the capability of DNA proof reading. The process by which an enzyme DNA polymerization reaction is incorrectly identified is called a proof-reading process. The process of placing a complementary base according to the nucleotide base of the mold formula in the process of DNA replication is called polymerization reaction.DNA polymerase does the job of enzyme proof reading. RNA polymerase, amino acyl TRNA synthase enzyme also has proof reading ability. There are two models to explain how the enzyme binds to the substrate. E.g.
 
 
* Lock key model, and
 
* Induced fit model
 
Lock-key Model :
 

 

                                  picture  :  Emil Fisher

 
In 1894, Emile Fischer proposed this lock key to explain the specificity of the enzyme. According to him, specific enzymes and specific substrates have specific complementary binding sites to bind to each other. The substrate adheres to the binding site of the enzyme. Much like a lock key. In order for a specific enzyme to be attached, a substrate must have a complementary structure to the binding site of that enzyme.Otherwise that substrate cannot be added to that enzyme. The binding site of the enzyme is called its active site. In this case, a substrate is first added to the active site of an enzyme to form a substrate-enzyme compound. At the end of the reaction they separate and form a product. There is no change in the structure of the enzyme. A specific enzyme can have multiple active sites.The limitation of the lock key model is that it can explain the substrate specificity of the enzyme but cannot explain the transition state of the reaction. We will know about the transition state later.
 
picture : Lock key model

Induced Fit Model:

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According to this model, the active site of the enzyme and the substrate are not ready to stick together at all. As scientists thought in the lock key model. Rather the enzyme changes its structure slightly to attach to the substrate. As a result, the substrate becomes attached to the enzyme in a very smooth way. The process by which the substrate attaches to the enzyme is called induced fit.
 
picture : Induced Fit Model

Enzyme Effect Mechanism:

 
We know that enzymes can speed up a chemical reaction several million times. This religion of enzymes is called the religion of influence. If you want to know how an enzyme speeds up a chemical reaction, you first need to know the barrier force or activation force.According to the collision theory of chemical reactions, when a chemical reaction takes place, the reactant molecules collide with a certain minimum force. Only reactive molecules that can collide with this minimum energy can take part in a chemical reaction. This minimum energy is called the barrier energy of the reaction or the activation energy. Let me explain with an example. Suppose you want to push a car from one place to another. Then you must push the car with a minimum of energy. Otherwise you can’t move the car. The same is true of activation power. In a reaction, the reactant molecules gain activation energy and reach a temporary complex in the middle of the reaction.This is called the transition state of the reaction. The difference in energy between the transition state and the reactive molecules at the beginning of the reaction is the amount of activation energy of that reaction.
 
Now, if the activation power of a chemical reaction is higher, will the rate or speed of the reaction be less or more? Definitely less. Let’s say you have two picnic offers. Both will be in the same place. But if you want to go, you have to pay 50 dollar for one and 100 dollar for the other. You currently have 30 rupees in your pocket. Where do you plan to go? Of course, it will cost 50 rupees.Not only that, you will see that the number of people has also increased with the offer of 50 dollar. The same is true of activation power. The lower the amount of activation energy in a reaction, the more molecules in the reaction can easily acquire the barrier energy and participate in the reaction, and the speed of the reaction will be higher.
 
The activation energy of enzyme-reacted reactions is less than the activation energy of enzyme-free reactions.

Now what the enzyme does is it causes a reaction with less activation energy than before.

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That is, the enzyme reduces the barrier energy of any chemical reaction. As a result, a greater number of molecules in an enzyme-containing reaction than in a chemical reaction without an enzyme can acquire barrier energy and collide. And so when enzymes are used in the reaction, the speed of the reaction increases. Now the question is how does the enzyme reduce the amount of activation energy of a reaction?
One enzyme works in one process. Some enzyme reagents speed up the reaction by putting them together in the right format. Some enzymes create the right environment for the substrate to be added to its active site. As such it can be acidic or nonpolar.Some enzyme-substrate complexes make the substrate flexible in such a way that the chemical bonds between it can be easily broken and thus reach the transition state very quickly. Some enzymes take part in chemical reactions to reduce the barrier energy.For this the enzyme molecule forms a transient covalent bond with the reactant molecule. The word transient is important. All enzymes return to their previous state at the end of the chemical reaction. That is, there is no lasting change in the structure of the enzyme at the end of the reaction.After affecting a reaction, the enzyme product is released at the end of the reaction to create a new reaction.
 
Enzyme control :
 
It is possible to control its effect by changing the structure of the enzyme. This process is called enzyme regulation. The chemical compounds that are used to regulate the activity of enzymes are called regulatory compounds.They can increase the activity of any enzyme (activator) or decrease (inhibitor). Enzyme regulation can occur in a variety of ways. Such as allosteric regulation, proteolytic activation, reversible covalent modification, regulation using isoenzymes.
Allosteric control :
 
In this process, the effector molecule is added to any control site (or regulatory site) other than the active site of an enzyme to regulate the enzyme. The site to which the effect molecule is being added is called the regulatory site.An enzyme has multiple regulatory sites. Allosteric sites help an effector molecule to attach to an enzyme and change the structure of the enzyme. Allosteric regulation can be of two types:
 
Allosteric Inhibition and 
 
* Allosteric activation
 
In the first case, the inhibitor enzyme binds elastically to slow down its activity. For example, in the process of isoleucine (amino acid) synthesis, the product inhibits the threonine dehydrate enzyme used in isoleucine reaction. In the second case, binding to the enzyme accelerates the activity of the enzyme.In this case the activator molecule binds to the enzyme and accelerates the affinity of the substrate. For example, AMP (adenosine mono phosphate) acts as an activator of the glycogen phosphorylase enzyme.
picture : Allosteric Regulation

Enzymes that can be regulated allosterically are called allosteric enzymes. If any effect molecule is added to a regulatory site of these enzymes, it has an effect on other sites. This religion is called co-operative. It can be of two types. Positive and negative.If an effect is added to one site and the chances of it being added to other sites increase, it is called positive co-operative. On the contrary, it is called negative co-operative.

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There are two models for explaining the allosteric regulation process of enzymes.
 
* Concerted Models, and 
* Sequential Model
 
Concerted Models:
 
This model was proposed in 1965 by Jack Monod, Jeffreys Weimen. The picture contains two confirmations of the allosteric enzyme. R (relax) and T (tight). R conformation is active and binds tightly to the substrate. T conformation is inert and binds less tightly to the substrate.The key to this model is: Conformal or structural changes of all subunits of the enzyme occur simultaneously. This means that at the same time all the sub-units change from T to R conformation. Under normal conditions T and R conformation of an enzyme maintains an equilibrium. In this case the number of T conformation is greater than that of R. That is, it goes from inactive to active confirmation. According to this model, after the substrate is added to all the sub-units of T conformation, the conformational change of all the units takes place simultaneously.
 
Concerted model. When all the four sub-units are saturated with oxygen, all the units undergo conformational changes together.
Sequential Model: 
 
Daniel Koshland proposed this model. According to this model, enzymatic regulation processes do not occur simultaneously in all units of the enzyme. First the enzyme binds a substrate with a sub unit and causes its conformational change.And that’s from T to R confirmation. That is, only the unit to which the substrate is added has a conformational change.
 
Sequential model. Confirmation changes occur only in the sub-unit to which oxygen has been added.
Allosteric Modulation: 
 
Allosteric modulation is the change in the activity of enzymes. In this case an effect is added to the allosteric site of an enzyme which changes its activity. The effect molecules used in this process are called modulators.They attach to the regulatory site of an enzyme and cause a confirmatory change in the active site of the enzyme and change its activity. Enzyme modulation can be positive or negative. In the case of positive modulation, binding to a ligand or modulator enzyme causes a positive structural change in its active site and increases the level of attachment to the substrate.In the case of negative modulation, the exact opposite happens. An example of positive modulation is the addition of oxygen to hemoglobin. Here oxygen acts as a substrate and ligand. When oxygen is added to a subunit of hemoglobin, oxygen is added to the active site of other units.
 
Naming of Enzymes:
Enzymes are named based on three distinct properties. E.g .: 
 
01. Depending on the type of substrate,
 
02. Depending on the type of reaction,
 
03. According to the combined properties of the substrate-reaction.
 
By substrate type:
 
This method involves the systematic naming process. In 1898, Duclax proposed that the enzyme be named by adding the last three letters of the digestive enzyme (Edge) to the end of the substrate on which the enzyme works. Some examples:
 
 
Substrate Enzymes
Sucrose Sucrose
Urea Ureas
Arginine Arginase
Tyrosine Tyrosinase
Lipids Lipase
Protein Protease

 

By reaction type:
 
This method also includes systemic nomenclature. Enzyme nomenclature is also added to the end of the name of the type of enzyme that affects the reaction.
 
 
The name of the reaction Enzymes
Hydrolysis Hydrolase
Oxidation Oxidase
Reduction Reductage

 

According to the combined properties of the substrate-reaction:
 
Such enzymes are named by combining the name of the enzyme with the substrate. This is the name given to a specific reaction. As the substrate is hexose and the reaction is kinase, the name of its enzyme is hexokinase.The enzyme that makes pyruvic acid from phosphoenol pyruvic acid is called pyruvic acid kinase.
 
Types of Enzymes:
 
So far, many enzymes have been discovered for the benefit of genomic sequencing methods. In mid-2004, about 83,000 different enzymes were discovered from 9,800 different organisms.This number doubled in 2008. All enzymes are divided into 6 classes based on chemical reactions. The International Union of Biochemistry and Molecular Biology (IUBMB) introduced a number system consisting of 4 numbers for each enzyme. The first of these numbers indicates what kind of reaction the enzyme affects.The IUBMB number of the enzyme alcohol dehydrogenase to aldehyde by oxidizing alcohol is 1.1.1.1. The first number here indicates that this enzyme affects the zeron-bizarre reaction, the second number indicates that it removes a hydrogen using NAD +, the third number indicates that its substrate is primarily alcohol, and the fourth number refers to the same reaction on different substrates. All enzymes are used to mean different things.
 
Class-01: Oxydoridactase:
 
First class enzymes affect the oxidation reaction. Oxidation means electron donation and oxidation means electron acceptance. The one who donates electrons is oxidized and the one who receives electrons is oxidized. The term dehydrogenase is commonly used for these enzymes.For example: lactate dehydrogenase, glycerideldehyde-3-phosphate dehydrogenase. However, in some cases reductase is also used. E.g. pyruvate reductase.
 

Class-02: Transfer:

 
These classes of enzymes transfer a chemical group from one compound to another. This is why each of these enzymes works on two substrates and makes two products. For example, the hexokinase enzyme transfers a phosphate group from ATP to the glucose molecule.Again the acetyl transfer enzyme transfers from acetyl-CoA to the acetyl group to another molecule such as lysine. The amino transfer enzyme transfers amino groups from any amino acid and makes keto acids.
 

Class-3: Hydrolase :

 
These enzymes take part in the hydrolysis reaction by adding a water molecule to a chemical molecule. Usually the substrate of this group is an amide or ester molecule. Such as esters, lipase, phosphatase, glycosides, peptides, nucleosides.
 
 
Class-4: Liaison :
 
Usually enzymes in this group are used to break the carbon-carbon covalent bond. Others break the carbon-nitrogen bond of a keto acid and release one molecule of carbon-dioxide. For example, dopamine (dihydrophenyl alanine) dicarboxylase enzyme participates in dopamine production Dopamine is made by removing one molecule of carbon dioxide from dopamine.

Level-5: Isomarage

 
These enzymes transfer a chemical group of a chemical compound or a binding compound to another place. For example, the phosphate group of 2-phosphoglycerate 2 transfers to the phosphate group of 3 carbon to form 3-phosphoglyceride, a phosphoglyceride mutage enzyme.

Class-6: Luggage:

 
 Luggage is used to attach two carbon atoms. These enzymes need energy to affect the reaction. Energy usually comes from ATP (adenosine triphosphate). The enzymes that collect energy using a nucleotide are usually called synthetases. And those who do not need nucleotides are called synthase.So ligase enzymes are synthesized. The enzyme ligase (amino-acyl-tRNA-synthetase) affects the reaction of adding amino acids to the transfer RNA.
Under the influence of the enzyme amino-acyl-tRNA-synthesis, amino acids are added to tRNA.

Enzymes in the organism

 
The role of enzymes in the organism is not to be underestimated. However, it is not bad to talk about the work of two important enzymes. In that case the first thing to talk about is rubiscoenzyme.
 
Enzymes are called the most important enzymes in the world.
 
In general, plants can make their own food in the process of photosynthesis. In fact, plants play another important role in this process. That is, the plant can combine the first light energy with chemical energy. The earliest reaction of photosynthesis is when the carbon dioxide in the air reacts with riboflavin-1,5-bis phosphate in the leaves to form a temporary keto acid.It is through this reaction that solar energy is first integrated into chemical energy. Rubisco enzyme plays an influential role in this reaction. So without this enzyme, this reaction would not have taken place and it would not have been possible for plants to make food. And you can imagine what would have happened then. That’s why this enzyme is so expensive. In addition, many other enzymes play a role in this process.
 

Well think about it, when the seeds of a plant are under the ground, there is no chance of photosynthesis in the seeds. Because sunlight cannot reach there. Again, there is no chlorophyll in the seeds. So where does the seed get enough glucose to survive? Seeds contain lipids and proteins. So there is a glycosalate cycle from lipids and proteins to produce the necessary glucose from lipids and proteins.There are also two important enzyme roles. These are iso citrate lyase and malate synthase. These enzymes are not present in the bodies of two animals. So animals cannot produce glucose from lipids.

 
Respiration is a very important process for the body. Through this process, the organism breaks down the nutrients of the body and creates energy. There are many enzymes involved in this process. Such as hexokinase, phosphofructo kinase, aldolase, citrate synthase, fumarage etc.
 
 
Digestive Enzymes

Now let’s talk about the process of digestion. Digestion is an extremely important process in the animal body. At the beginning of the writing, I talked a little about digestion. In this process complex food is broken down into simple nutrients. And here is the role of many enzymes. Chemical digestion of food begins with saliva in the mouth.Saliva is secreted from three pairs of salivary glands inside the mouth. And saliva juice contains enzymes that analyze sugars. Such as Tylenol, Maltese. Tylenol breaks down complex sugars into maltose and converts maltase into glucose. Saliva contains no enzymes to break down lipids and proteins.

 
From the oral cavity, food enters the stomach through the esophagus. There is no enzyme in the stomach to analyze sugar. Gastric juice is secreted from the gastric glands in its wall. This juice contains pepsin, renin, lipase enzyme. Pepsin breaks down proteins into proteases and peptones. Renin converts casein protein to paracetamol. Lipase breaks down fats to form fatty acid glycerol.
 
The small intestine starts after the stomach. About one hundred percent of the semi-digested food is digested from the stomach. Here sugars, meats, fats are all digested. Here pancreatic juice, liver juice and bile juice come from the pancreas and mix with the food. Pancreatic juice contains amylase, lipase, trypsin, chymotrypsin, carboxy peptides, amino peptides, phospholipase enzymes.In addition, intestinal juice is secreted from the wall of the small intestine. Intestinal juices contain amylase, lecithinase, sucrose, maltase, lipase. Amylase converts complex sugars into glucose. Trypsin, chymotrypsin, carboxy peptides break down polypeptide molecules into amino acids. Lecithinase, lipase, fossolipase are enzymes that analyze fats.
 
Industrial Enzymes:
 
Enzymes are used in a variety of ways in industry. Enzymes are very important in industrial production. For example, in the textile industry, the use of enzymes in the manufacture of pharmaceuticals, detergents, biofuels is very common.
 
In the dairy industry :
 
For a long time in the dairy industry, rennet produced in the stomach of calves was used to make various dairy products such as cheese, yoghurt, whey. Renate is a fluid composed of a number of protease enzymes that are produced in the stomachs of herbivorous mammals. Renate contains renin, a pepsin enzyme that breaks down the milk protein casein.Currently microbial rennet is used instead of calf’s rennet. The acid aspartate in the microbial rennet contains the enzyme protease. Lactase enzyme is also used in making yogurt and whey. The sugars in lactase milk hydrolyze lactose. Also, lipase enzyme is used to keep the smell of cheese.

Enzymes in the dairy industry

 
In the Textile Industry:
 
 In the textile industry, enzymes like cellulose, catalase, lacase, amylase etc. are commonly used. Enzymes are mainly used to remove starch from yarn, to break down excess hydrogen peroxide, to bleach, to remove lignin.
 

Enzymes in textiles

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Enzymes used in textiles are used for this purpose :
 
Enzymatic desalination: 
 
Amylase enzyme is used to remove starch from fabric or yarn. The optimum temperature in this case is 30-40 degrees Celsius and the pH is 5.5-6.5. In this way the yarn can be disassembled without any damage.
 
Enzyme washing:
 
Enzyme washing is the process of softening, softening and removing various stains from the yarn using enzymes. In the case of ordinary washing, various proteins form stains by being deposited on dirty cloth or yarn. In this case, these stains can be easily removed by using proteolytic enzymes to make detergents.
 
Biofinishing:
 
Biofinishing is the use of enzymes to make the yarn smooth and comfortable. Cellulose enzymes are used in this process.
 
Enzymes to reduce plastics:

 

The PET Edge enzyme eats plastic

A team of researchers from Spain invented a new plan to remove plastics. The plan is basically two steps. At first some microorganisms will come in contact with the plastic. Then they will use plastic as their source of carbon. The microorganisms will make some enzymes (PET Edge) by which they break down plastic polymers.If the process takes place in the presence of oxygen then carbon dioxide and water will be formed at the end of the reaction. And if it happens in the absence of oxygen, biogas and water will be formed. PET Edge enzyme polyethylene terephthalate breaks down plastic. This enzyme was first discovered in 2016 at Salidionella saccinosis.

 
References:
 
01. Lehninger Principles of Biochemistry.
 
03. Text book of Biochemistry, Thomas M.Devlin.
 
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