1) Honey Helps in Healing Wounds and Burns:

There have been Several Instances Where people have reported Positive ramifications of using Honey in healing wounds.

The Cochrane Library stated that Pure Desi Honey (4Á/) may have the ability to help rapidly heal burns. The Famous writer “Fayaz Wali” stated that “topical Honey (4Á/) is less affordable than other interventions, especially oral antibiotics, which are normally used and may have other adverse effects.”

However, there is a lack of evidence to fully support this claim. In Fact, a study published in The Lancet Infectious Diseases suggested that taking medical-grade Honey (4Á/) into the consequences of patients has no advantage over standard antibiotics among patients undergoing dialysis.

Pure Desi Honey shouldn’t be taken to young it can cause botulism, few but different types of Food poisoning. (Aso Read: Benefits of Soft Almonds)

2) Pure Desi Honey Reducing the duration of diarrhea:

According to a Research, Pure Honey helps to reduce the intensity and duration of diarrhea. It also helps to increased potassium and water quantity, which can be very helpful when suffering from diarrhea. Researchers also indicate that Hunza Desi Honey has also indicated the capability to block the action of germs which frequently cause diarrhea.

3) Pure Desi Honey Preventing Acid Reflux:

A recent study has shown that Pure Honey (4Á/) can reduce the upward flow of stomach acid and undigested food by lining the esophagus and stomach.

Pure Honey also helps to decrease the risk of gastroesophageal reflux disorder. It may lead to inflammation, acid reflux, and heartburn.

4) Fighting infections:

In 2010, A Famous Research of Academic Medical Center reported that the Pure Desi Honey has the ability to kill the harmful germs which are lying in a protein known as defensin. (Also Read: Benefits of Pistachio Nuts)

More Recent Study in the European Journal of Clinical Microbiology and Infectious Diseases revealed a certain Kind of Honey, known as Manuka honey (4Á/), will assist in preventing the germs Clostridium difficile out of Settling within the body. C. Difficile is famous for causing acute nausea and illness.

5) Honey (4Á/) Relieving cold and cough symptoms:

Pure Honey is a 100% Natural Cough remedy (WHO). Honey is a cure for cough. Honey is the best remedy for cough symptoms. But some professionals stated that Honey Isn’t suitable for underage of one year. A 2007 research by the College of Medicine demonstrated that Pure Honey decreased hay coughing and also improved sleep quality in children with respiratory infection to a greater level than the cough medication dextromethorphan.

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The essence of most enzymes is protein, and only a few enzymes are RNA, so this article only discusses enzymes composed of proteins. These enzymes, like other proteins, are composed of amino acids and have primary, secondary, tertiary, and quaternary structures. Enzymes will also be denatured and lose vitality due to certain physical and chemical factors. Enzymes also have colloidal properties and cannot penetrate semi-permeable membranes.

Enzymes can also be hydrolyzed by proteases. Some people think that proteases cannot act on themselves. In fact, one enzyme molecule can cut another enzyme molecule as long as there is a corresponding enzyme cutting site. For example, when the zymogen of chymotrypsin is activated by trypsin, the direct product is π-chymotrypsin. π-chymotrypsin has high activity, but it will self-cleave to produce α-chymotrypsin which is less active but more stable.

Some enzymes are composed entirely of protein and are simple proteins, such as urease and trypsin. In addition to protein, some enzymes also contain non-protein components, which are binding proteins. The non-protein components are called cofactors, the protein part is called enzyme protein, and the complex is called holoenzyme. Cofactors generally play the role of carrying and transferring electrons or functional groups. Among them, those that are tightly bound to the enzyme protein by covalent bonds are called prosthetic groups, and those that are loosely bound by non-covalent bonds are called coenzymes.

Recently, there is a term “conjugated enzyme” used to refer to holoenzymes. However, there is no such name in biochemistry books, and conjugated enzyme is not available on Wikipedia. Conjugated protein does exist (translated as binding protein or conjugated protein). So this term should be derived by some people, not a professional term. The official name should be holoenzyme, and apoenzyme. Because Conjugated protein is actually just a classification, it is emphasized that such proteins can have cofactors, but it is not guaranteed to have cofactors. The search results on PubMed are all about coupling enzymes to carriers, so don’t use them indiscriminately.

In the process of catalysis, the prosthetic group is not separated from the enzyme protein, and only functions as the carrier in the enzyme. For example, the prosthetic group of FAD and FMN in the flavin protein enzyme molecule carries hydrogen, and the biotin prosthetic group of carboxylase carries carboxyl group, etc. Coenzymes are often used as inter-enzyme carriers to connect two enzymatic reactions. For example, NAD+ is reduced to NADH in one reaction, and then oxidized back to NAD+ in another reaction. It acts like a substrate in the reaction and is sometimes called a secondary substrate. Therefore, the systematic naming of dehydrogenase is often like “alcohol: NAD + oxidoreductase”.

More than 30% of enzymes require metal elements as cofactors. The metal ions of some enzymes are tightly bound to the enzyme protein and are not easily separated, which are called metalloenzymes; the metal ions of some enzymes are loosely bound and are called metal activating enzymes. The cofactors of metalloenzymes are generally transition metals, such as iron, zinc, copper, and manganese. The cofactors of metal activating enzymes are generally alkali metals or alkaline earth metals, such as potassium, calcium, and magnesium.

An enzyme composed of one peptide chain is called a monomeric enzyme, and an enzyme formed by multiple peptide chains joined by non-covalent bonds is called an oligomerase, which is an oligomeric protein. Sometimes some functionally related enzymes in the organism are organized to form a multi-enzyme system, which in turn catalyzes related reactions. The formation of a multi-enzyme system is a requirement of metabolism, which can reduce the diffusion limit of substrates and products, and improve the speed and efficiency of the overall reaction.

Sometimes there are multiple enzyme activities on a peptide chain, which is called a multi-enzyme fusion. For example, the debranching enzyme in glycogen decomposition has starch-1,6-glucosidase and 4-α-D-glucanotransferase activities on one peptide chain. The AROM multi-enzyme fusion from N. rubrum is a dimer, and each peptide chain contains five enzyme activities, which can catalyze the second to sixth steps of the shikimate pathway. Due to the intermediate product transfer channel, the catalytic efficiency is greatly improved.

What is the role of protease?

One of the main functions of proteases is to process proteins. Proteins in the body are difficult to digest and do not contain enzymes. Other types of proteases are involved in regulating the activities of blood clotting cells. These enzymes are also called proteolytic enzymes.

Proteins are held together by peptide bonds. Long-chain amino acids, small pieces of protein are called peptides, large pieces of protein are called peptides, and enzymes that break down peptides are called proteases. Proteases are types of proteins that accelerate degradation. γpeptidase cleaves terminal amino acids to break down peptide bonds and release amino acids produced due to residual protein.

What is protease?

Proteasomes are ubiquitous in eukaryotes and archaea, and a giant protein complex that also exists in some prokaryotes. In eukaryotes, the proteasome is located in the nucleus and cytoplasm. The main role of the proteasome is to degrade proteins that are not needed or damaged by the cell. This role is achieved by chemical reactions that break peptide bonds. Enzymes that can perform this role are called proteases.

The proteasome is the main mechanism used by cells to regulate specific proteins and remove misfolded proteins. After proteasome degradation, the protein is cleaved into peptides about 7-8 amino acids long; these peptides can be further degraded into single amino acid molecules, and then used to synthesize new proteins. The protein that needs to be degraded is first labeled (ie attached) by a small protein called ubiquitin. This labeling reaction is catalyzed by ubiquitin ligase. Once a protein is labeled with an ubiquitin molecule, it will trigger other ligases to add more ubiquitin molecules; this forms a “polyubiquitin chain” that can bind to the proteasome, thereby bringing the proteasome here. A labeled protein begins its degradation process.

From the structural point of view, the proteasome is a barrel-shaped complex, including a “core” composed of four stacked rings. The core is hollow to form a cavity. Among them, each ring is composed of seven protein molecules. The middle two loops each consist of seven β subunits and contain six active sites for proteases. These sites are located on the inner surface of the loop, so the protein must enter the “cavity” of the proteasome to be degraded.

The two outer rings each contain seven α subunits, which can function as a “gate” and are the only way for proteins to enter the “cavity”. These alpha subunits, or “gates”, are controlled by the “cap”-like structures (ie, regulatory particles) attached to them; the regulatory particles can recognize the polyubiquitin chain tag attached to the protein and initiate the degradation process. The entire system including ubiquitination and proteasome degradation is called the “ubiquitin-proteasome system”. The proteasome degradation pathway is essential for many cell processes, including the cell cycle, regulation of gene expression, and oxidative stress.

The winning themes of the Nobel Prize in Chemistry in 2004 were the importance of protein enzymolysis in cells and the role of ubiquitin in the enzymatic pathway. The three winners are Aaron Chehanovo, Avram Hershko and Owen Rose.

What is biological protease?

Biological protease is an abbreviation of enzyme that hydrolyzes protein peptide bond. This substance is generally widely distributed in plant stems and leaves, animal organs, microorganisms and fruits. The protease can accelerate the digestion of food after entering the human body, and has a relatively good help for indigestion that occurs in the human body. Protease also has a better recovery effect for some other types of diseases.

What is the role of pepsin?

Pepsin is a digestive protease whose main function is to break down the protein in food into small peptide fragments. Pepsin is mainly used to treat indigestion caused by eating too much protein food, or recovery period after serious illness, impaired digestion and chronic atrophic gastritis, as well as impaired digestive function of gastric cancer, and protease deficiency caused by pernicious anemia.

As biocatalysts, enzymes and general catalysts are the same in many respects. For example, the amount is small but the catalytic efficiency is high. Like general catalysts, enzymes can only change the speed of chemical reactions, not the equilibrium point of chemical reactions. The enzyme itself does not change before and after the reaction, so the relatively low content of the enzyme in the cell can catalyze the change of a large number of substrates in a short time, reflecting the high efficiency of enzyme catalysis. Enzymes can reduce the activation energy of the reaction, but do not change the free energy change (³G) during the reaction, thus speeding up the reaction and shortening the time for the reaction to reach equilibrium, but it does not change the equilibrium constant.

Compared with general catalysts, the catalysis of enzymes shows unique characteristics.

1. High efficiency of enzyme catalysis

The catalytic activity of enzymes is much higher than that of chemical catalysts. For example, catalase (containing Fe2+) and inorganic iron ions both catalyze the decomposition reaction of hydrogen peroxide as follows. 1 mol of catalase can catalyze the decomposition of 5×106 mol of H2O2 in 1 minute. Under the same conditions, 1 mol of the chemical catalyst Fe2+ can only catalyze the decomposition of 6×10-4 mol of H2O2. Compared with the two, the catalytic efficiency of catalase is about 1010 times that of Fe2+.

The level of enzyme catalytic efficiency can be expressed by the concept of turnover number. The conversion number refers to the number of molecules per enzyme molecule that can convert the substrate per minute when the substrate concentration is large enough, that is, the number of molecules that catalyze the chemical change of the substrate. According to the data introduced above, the conversion number of catalase can be calculated as 5×106. The conversion number of most enzymes is around 1,000, and the largest can reach over 106.

(2) High specificity of enzyme catalysis

An enzyme can only act on a certain type or a specific substance. This is the specificity of enzyme action. For example, glycosidic bonds, ester bonds, peptide bonds, etc. can be hydrolyzed by acid-base catalysis, but the enzymes that hydrolyze these chemical bonds are different. They are the corresponding glycosidases, esterases, and peptidases, that is, they are individually specific. It can be hydrolyzed by natural enzymes.

(3) Mild reaction conditions catalyzed by enzymes

Enzymatic reactions generally require mild conditions such as normal temperature, normal pressure, and neutral pH. Because enzymes are proteins, they are prone to lose their activity in environments such as high temperature, strong acid, and alkali. Since enzymes are more sensitive to changes in the external environment and are easily denatured and inactivated, the reaction conditions must be strictly controlled during application.

(4) Adjustability of enzyme activity

Compared with chemical catalysts, another feature of enzyme catalysis is that its catalytic activity can be automatically regulated. Although there are many kinds of chemical reactions in organisms, they are very coordinated and orderly. Changes in substrate concentration, product concentration and environmental conditions may affect enzyme catalytic activity, thereby controlling the coordinated and orderly progress of biochemical reactions. Any disorder and imbalance of the biochemical reaction will inevitably cause the organism to produce disease or even death in severe cases. In order to adapt to changes in the environment and maintain normal life activities, organisms have formed a system that automatically regulates enzyme activities during the long evolutionary process. There are many ways to regulate enzymes, including inhibitor regulation, feedback regulation, covalent modification regulation, zymogen activation, and hormone control.

(5) Enzyme catalytic activity is related to coenzyme, prosthetic group and metal ion

Some enzymes are complex proteins, and the small molecules of coenzymes, cofactor and metal ions are closely related to the catalytic activity of the enzyme. If they are removed, the enzyme loses its activity.