PRODUCTS

GLYCINE

Glycine is a colourless, sweet-tasting crystalline solid.
Glycine is very slightly soluble in alcohol and in ether.
Glycine may be prepared from chloroacetic acid and ammonia; from protein sources, such as gelatin and silk fibroin; from ammonium bicarbonate and sodium cyanide; by catalytic cleavage of serine; from hydrobromic acid and methyleneaminoacetonitrile.

CAS Number: 56-40-6
Molecular Formula: C2H5NO2
Molecular Weight: 75.07
EINECS Number: 200-272-2

Glycine (abbreviated as Gly or G) is an organic compound with the formula NH2CH2COOH.
Having a hydrogen substituent as its side-chain, glycine is the smallest of the 20 amino acids commonly found in proteins.
Glycine is codons are GGU, GGC, GGA, GGG of the genetic code.

Glycine is unique among the proteinogenic amino acids in that it is not chiral.
Glycine can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom.
Glycine is an amino acid, which is a building block of proteins.

Glycine is also the genus name of the Soybean plant (species name = Glycine max).
Glycine is a white, odorless, crystalline powder having a sweetish taste.
Its solution is acid to litmus.

Glycine is the simplest amino acid in terms of structure, as its side chain consists of just a hydrogen atom.
Glycine is a non-essential amino acid, meaning that the body can synthesize it on its own, and it doesn't necessarily need to be obtained through the diet.
Glycine (symbol Gly or G;[6] /ˈɡlaɪsiːn/ ⓘ) is an amino acid that has a single hydrogen atom as its side chain.

Glycine is the simplest stable amino acid (carbamic acid is unstable), with the chemical formula NH2‐CH2‐COOH.
Glycine is one of the proteinogenic amino acids.
Glycine is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG).

Glycine is integral to the formation of alpha-helices in secondary protein structure due to the "flexibility" caused by such a small R group.
Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited muscle contraction.
Glycine is the only achiral proteinogenic amino acid.

Glycine can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom.
Glycine is an amino acid that helps build proteins needed for tissue and hormone maintenance.
More glycine may help support heart and liver health, improve sleep, reduce diabetes risk, and reduce muscle loss.

Glycine is of the simplest structure in the 20 members of amino acid series, also known as amino acetate.
Glycine is a non-essential amino acid for the human body and contains both acidic and basic functional group inside its molecule.
Glycine exhibits as a strong electrolyte an aqueous solution, and has a large solubility in strong polar solvents but almost insoluble in non-polar solvents.

Glycine also has a relative high melting point and boiling point.
The adjustment of the pH of the aqueous solution can make glycine exhibit different molecular forms.
The side chain of glycine contains only a hydrogen atom.

Owing to another hydrogen atom connecting to the α-carbon atom, the glycine is not optical isomer.
Since the side bond of glycine is very small, it can occupy space which can’t be occupied by other amino acids, such as those amino acids located within the collagen helix.
At room temperature, it exhibits as white crystal or light yellow crystalline powder and has a unique sweet taste which can ease the taste of acid and alkaline taste, masking the bitter taste of saccharin in food and enhance the sweetness.

However, if an excessive amount of glycine is absorbed by body, they not only can’t be totally absorbed by the body, but will also break the balance of the body's absorption of amino acids as well as affect the absorption of other kinds of amino acids, leading to nutrient imbalances and negatively affected health.
The milk drink with glycine being the major raw material can easily does harm to the normal growth and development of young people and children.
Glycine has a density of 1.1607, melting point of 232~236 °C (decomposition).

Glycine is soluble in water but insoluble in alcohol and ether.
Glycine is capable of acting together with hydrochloric acid to form hydrochloride salt.
Glycine is presented in the muscles of animals.

Glycine can be produced from the reaction between monochloro acetate and ammonium hydroxide as well as from the hydrolysis of gelation with further refining.
As an amino acid, glycine is involved in the synthesis of proteins, which are essential for the structure and function of cells.
Glycine acts as an inhibitory neurotransmitter in the central nervous system.

Glycine plays a role in signal transmission in the brain and spinal cord.
Glycine is a component of collagen, the most abundant protein in the human body.
Collagen provides structure to connective tissues, such as skin, bones, and tendons.

Glycine is involved in the synthesis of glutathione, a powerful antioxidant that plays a role in the detoxification of certain substances in the liver.
Glycine is involved in the regulation of blood sugar levels and can be converted into glucose, providing a source of energy.
Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain.

Glycine can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom.
Glycine is acid–base properties are most important.
In aqueous solution, glycine is amphoteric: below pH = 2.4, it converts to the ammonium cation called glycinium.

Glycine functions as a bidentate ligand for many metal ions, forming amino acid complexes.
A typical complex is Cu(glycinate)2, i.e. Cu(H2NCH2CO2)2, which exists both in cis and trans isomers.
With acid chlorides, glycine converts to the amidocarboxylic acid, such as hippuric acid and acetylglycine.

With nitrous acid, one obtains glycolic acid (van Slyke determination).
With methyl iodide, the amine becomes quaternized to give trimethylglycine, a natural product:
H3N+CH2COO− + 3 CH3I → (CH3)3N+CH2COO− + 3HI

Glycine condenses with itself to give peptides, beginning with the formation of glycylglycine:
2 H3N+CH2COO− → H3N+ CH2CONHCH 2COO− + H2O
Pyrolysis of glycine or glycylglycine gives 2,5-diketopiperazine, the cyclic diamide.

Glycine forms esters with alcohols. They are often isolated as their hydrochloride, e.g., glycine methyl ester hydrochloride.
Otherwise the free ester tends to convert to diketopiperazine.
As a bifunctional molecule, glycine reacts with many reagents.

These can be classified into N-centered and carboxylate-center reactions.
Glycine has a pivotal role in lowering the plasma lipid levels in diabetic and obese patients by activating the CNS.
During brain hypoxia glycine can stabilize the energetics disturbances in brain mitochondria.

Glycine also increases the in vitro development of porcine blastocysts when used along with glucose.
Glycine is the simplest naturally occurring amino acid and is a constituent of most proteins. Its formula is H2N·CH2·COOH.
Glycine is routinely used as a cofreeze-dried excipient in protein formulations owing to its ability to form a strong, porous, and elegant cake structure in the final lyophilized product.

Glycine is one of the most frequently utilized excipients in freeze-dried injectable formulations owing to its advantageous freeze-drying properties.
Glycine has been investigated as a disintegration accelerant in fast-disintegrating formulations owing to its excellent wetting nature.
Glycine is also used as a buffering agent and conditioner in cosmetics.

Glycine may be used along with antacids in the treatment of gastric hyperacidity, and it may also be included in aspirin preparations to aid the reduction of gastric irritation.
Although glycine can be isolated from hydrolyzed protein, this route is not used for industrial production, as it can be manufactured more conveniently by chemical synthesis.
The two main processes are amination of chloroacetic acid with ammonia, giving glycine and ammonium chloride, and the Strecker amino acid synthesis, which is the main synthetic method in the United States and Japan.

About 15 thousand tonnes are produced annually in this way.
Glycine is the most plentiful amino acid within the body, it is considered a link to the forming of proteins.
Amino acids are used for a number of bodily functions including creating proteins and enzymes.

They are broken down into three different groups: essential, non-essential and conditional amino acids.
Glycine is a non-essential amino acid, meaning that it is produced naturally in the body.
Glycine can also be found in various high protein food sources such as fish, meat and eggs.

Glycine is recommended for any individual looking to increase their Glycine intake in a powder form.
Glycine is usually taken pre-workout, post workout or before bed.
Glycine is also cogenerated as an impurity in the synthesis of EDTA, arising from reactions of the ammonia coproduct.

Glycine is an amino acid.
The body can make glycine on its own, but it is also consumed in the diet.
Sources include meat, fish, dairy, and legumes.

Glycine is a building block for making proteins in the body.
Glycine is also involved in transmitting chemical signals in the brain, so there's interest in using it for schizophrenia and improving memory.
Glycine is an amino acid with a number of important functions in the body.

Glycine acts as a neurotransmitter, a component of collagen, and as a precursor to various biomolecules (e.g., creatine, heme), among other roles.
Glycine is often considered conditionally essential, meaning it can usually be produced in the body in sufficient amounts.
However, in certain contexts (e.g., pregnancy) more glycine may be needed from the diet.

Glycine is found in most protein sources, meaning common sources of glycine include meat, eggs, soybeans, lentils, and dairy products.
Classified as a “non-essential” (also called conditional) amino acid, glycine can be made in small amounts by the human body itself, but many people can benefit from consuming a lot more from their diets thanks to its numerous beneficial roles.
Glycine is the second most widespread amino acid found in human enzymes and proteins, which is why it has roles in nearly every part of the body.

Glycine’s one of 20 amino acids used to make protein in the body, which builds the tissue that forms organs, joints and muscles.
Of the proteins in the body, Glycine’s concentrated in collagen (the most abundant protein in humans and many mammals) and also gelatin (a substance made from collagen).
Some of the most attractive attributes include promoting better muscle growth, healing the lining of the GI tract, and slowing down the loss of cartilage in joints and skin.

While high-protein foods (like meat and dairy products) do contain some glycine, the best sources — collagen and gelatin — can be hard to get.
These proteins are not found in most cuts of meat and instead are obtained from consuming parts of animals that today most people throw away: skin, bones, connective tissue, tendons and ligaments.
People who are ill, recovering from surgery, taking medications that hinder certain metabolic processes or who are under a lot of stress can all use extra glycine for recovery.

According to some research, glycine can be used to help lower symptoms in people suffering from conditions like ulcers, arthritis, leaky gut syndrome, diabetes, kidney and heart failure, neurobehavioral disorders, chronic fatigue, sleep disorders, and even certain cancers.
Glycine, the simplest amino acid, obtainable by hydrolysis of proteins.
Sweet-tasting, it was among the earliest amino acids to be isolated from gelatin (1820).

Especially rich sources include gelatin and silk fibroin.
Glycine is one of several so-called nonessential amino acids for mammals; i.e., they can synthesize it from the amino acids serine and threonine and from other sources and do not require dietary sources.
Glycine is the smallest possible of the 20 amino acids that are essential for human life.

In a seeming contradiction, glycine is called a “nonessential” amino acid because it can be synthesized by the body and therefore does not have to be included in the diet.
Glycine is the only achiral amino acid in that the carbon atom bearing the carboxylate and amino groups is not a stereogenic center.
Glycine is considered a glucogenic amino acid, which means it helps supply the body with glucose needed for energy.

Glycine helps regulate blood sugar levels, and thus glycine supplementation may be useful for treating symptoms characterized by low energy and fatigue, such as hypoglycemia, anaemia, and Chronic Fatigue Syndrome (CFS).
Glycine encephalopathy (non – ketotic hyperglycinemia), is a rare autosomal recessive inherited metabolic disorder.
This disorder is characterized by abnormally high levels of the amino acid glycine in bodily fluids and tissues.

Glycine is the smallest of the 20 amino acids, and unlike the other amino acids, it does not have a significant side chain, allowing it to act as a flexible link for specific proteins by connecting protein domains together.
This makes glycine a common feature in amino acid motifs at protein active sites.
Glycine is prominence in protein structure explains why it represents 11.5% of total amino acid content in the human body.

Glycine biosynthesis can take place through three pathways.
The first occurs via the amino acid serine, which is produced from D-3-phosphoglycerate, a glycolysis intermediate.
Glycine can also be produced from threonine with threonine dehydrogenase and 2-amino-3-ketobutyrate lyase.

Oxidative degradation also helps synthesize glycine from choline.
Finally, glycine can be produced from glyoxylate through transamination with alanine.
Glycine metabolism also occurs through three distinctive mechanisms.

First, it can be metabolized through the glycine cleavage system, a complex enzyme system that conducts the reversible reaction at the last step of producing glycine from serine.
Serine hydroxymethyltransferase, the enzyme that catalyzes glycine synthesis from serine, also catalyzes serine formation from glycine.
Finally, D-amino acid oxidases can convert glycine into glyoxylate.

Although humans can synthesize glycine, still require dietary supplementation (usually from meat and dairy products) to support normal bodily functions, making it one of the conditionally essential amino acids.
Glycine is absorbed in the small intestine and enters the circulation, from whence it can provide a range of benefits.

Melting point: 240 °C (dec.) (lit.)
Boiling point: 233°C
Density: 1.595
vapor pressure: 0.0000171 Pa (25 °C)
FEMA. 3287 | GLYCINE
refractive index: 1.4264 (estimate)
Flash point: 176.67°C
storage temp.: 2-8°C
solubility: H2O: 100 mg/mL
form: powder
pka: 2.35(at 25℃)
color: <5 (200 mg/mL)(APHA)
PH: 4(0.2 molar aqueous solution)
Odor: Odorless
PH Range: 4
Odor Type: odorless
Water Solubility: 25 g/100 mL (25 ºC)
λmax: λ: 260 nm Amax: 0.05
λ: 280 nm Amax: 0.05
JECFA Number: 1421
Merck : 14,4491
BRN: 635782
LogP: -3.21

Glycine is a non-essential amino acid that is produced naturally by the body.
Glycine is one of 20 amino acids in the human body that synthesize proteins, and it plays a key role in the creation of several other important compounds and proteins.
Chemical synthesis is the most suitable method of preparation of glycine.

Amination of chloroacetic acid and the hydrolysis of aminoacetonitrile are the favored methods of production.
From chloroacetic acid and ammonia; from protein sources, such as gelatin and silk fbroin; from ammonium bicarbonate and sodium cyanide; by catalytic cleavage of serine; from hydrobromic acid and methyleneaminoacetonitrile.
Glycine is required for the synthesis of creatine, a chemical that provides energy to muscles and helps with increasing muscle strength and size.

Helps trigger the release of oxygen to the energy requiring cell-making process; Important in the manufacturing of hormones responsible for a strong immune system.
Glycine has been studied for its potential anti-inflammatory effects.
Glycine may help modulate the immune response and reduce inflammation in the body.

Due to its role in collagen synthesis, glycine is essential for wound healing and tissue repair.
Collagen provides structural support to tissues and is crucial for the formation of new skin during the healing process.
Collagen, containing glycine, is a major component of joints, contributing to their structure and function.

Some people use glycine supplements to support joint health, although more research is needed in this area.
Glycine receptors are found in the central nervous system, and glycine itself is involved in various neurological processes.
Some studies suggest that glycine may have a role in cognitive function and memory.

Glycine may have a protective effect on muscles, particularly during conditions that increase oxidative stress.
This could be relevant in situations like intense exercise or certain diseases.
Glycine is involved in the synthesis of heme, a component of hemoglobin, which is important for oxygen transport in the blood.

Glycine also plays a role in bile acid metabolism and may contribute to the regulation of fat metabolism.
Some research suggests that glycine may have potential benefits for cardiovascular health, including its role in reducing inflammation and supporting the health of blood vessels.
Glycine is not essential to the human diet, as it is biosynthesized in the body from the amino acid serine, which is in turn derived from 3-phospho glycerate.

In most organisms, the enzyme Serine hydroxy methyl transferase catalyses this transformation via the cofactor pyridoxal phosphate: serine + tetra hydro folate → glycine +N5,N10-Methylene tetrahydrofolate + H2O
In the liver of vertebrates, glycine synthesis is catalyzed by glycine synthase (also called glycine cleavage enzyme).

This conversion is readily reversible : CO2 + NH4+ + N5,N10-Methylene tetra hydro folate + NADH + H+→ Glycine + tetrahydrofolate +NAD+
Glycine is coded by codons GGU, GGC, GGA and GGG.
Most proteins incorporate only small quantities of glycine.

Glycine is manufactured exclusively by chemical synthesis, and two main processes are practiced today.
The direct amination of chloroacetic acid with a large excess of ammonia gives good yields of glycine without producing large amounts of di- and trialkylated products.
This process is widely used in China, where the main application of the glycine is as a raw material for the herbicide glyphosate.

The other main process is the Strecker synthesis.
The direct Strecker reaction of formaldehyde and ammonium cyanide produces methylene amino acetonitrile, which must be hydrolyzed in two stages to produce glycine.
A more efficient approach is to aminate the intermediate glycolonitrile, followed by hydrolysis].

An alternative method, which is more often applied for the homologous amino acids, is the Bucherer–Bergs reaction.
Reaction of formaldehyde and ammonium carbonate or bicarbonate gives the intermediate hydantoin, which can be hydrolyzed to glycine in a separate step.
Glycine is an amino acid, a building block for protein. It is not considered an “essential amino acid” because the body can make it from other chemicals.

A typical diet contains about 2 grams of glycine daily.
The primary sources are protein-rich foods including meat, fish, dairy, and legumes.
Glycine is used for treating schizophrenia, stroke, benign prostatic hyperplasia (BPH), and some rare inherited metabolic disorders.

Glycine is also used to protect kidneys from the harmful side effects of certain drugs used after organ transplantation as well as the liver from harmful effects of alcohol.
Other uses include cancer prevention and memory enhancement.
Some people apply glycine directly to the skin to treat leg ulcers and heal other wounds.

Glycine is another inhibitory CNS neurotransmitter.
Whereas GABA is located primarily in the brain, glycine is found predominantly in the ventral horn of the spinal cord.
Relatively few drugs are known to interact with glycine; the best-known example is the convulsant agent strychnine, which appears to be a relatively specific antagonist of glycine.

Glycine is degraded via three pathways.
The predominant pathway in animals and plants involves the glycine cleavage enzyme Glycine + tetra hydro folate + NAD+ → CO2 + NH4+ + N5,N10-Methylene tetra hydrofolate + NADH + H+ In the second pathway, glycine is degraded in two steps.
The first step is the reverse of glycine biosynthesis from serine with serine hydroxymethyl transferase.

Serine is then converted to pyruvate by serine dehydratase.
In the third pathway of glycine degradation, glycine is converted to glyoxylate by D-amino acid oxidase.
Glyoxylate is then oxidized by hepatic lactate dehydrogenase to oxalate in an NAD+-dependent reaction.

The half-life of glycine and its elimination from the body varies significantly based on dose.
In one study, the half-life was between 0.5 and 4.0 hours.
Glycine has been studied for its potential role in improving sleep quality.

Some research suggests that glycine supplementation may help promote relaxation and improve sleep patterns, making it a popular choice for individuals looking for natural sleep aids.
Glycine is involved in the synthesis of serotonin, a neurotransmitter that plays a key role in mood regulation.
Some studies have explored the potential antidepressant effects of glycine.

Glycine may play a role in regulating blood sugar levels.
Some research suggests that glycine supplementation could improve insulin sensitivity and help manage diabetes, although more studies are needed in this area.
Glycine is a component of gelatin, which is derived from collagen.

Gelatin has been studied for its potential benefits in supporting digestive health by promoting the integrity of the gut lining and aiding in the treatment of certain gastrointestinal conditions.
As a component of glutathione, glycine contributes to the body's antioxidant defense system.
Antioxidants help neutralize free radicals, which are molecules that can damage cells and contribute to aging and various diseases.

Glycine is involved in the detoxification process in the liver.
Glycine helps the liver remove toxins from the body and plays a role in the synthesis of various important molecules in the liver.
Collagen, which contains glycine, is crucial for maintaining the elasticity and hydration of the skin.

Some people use glycine supplements or collagen products to support skin health and reduce the signs of aging.
Glycine may undergo Maillard reactions with amino acids to produce yellowing or browning.
Reducing sugars will also interact with secondary amines to form an imine, but without any accompanying yellow-brown discoloration.

Glycine is not essential to the human diet, as it is biosynthesized in the body from the amino acid serine, which is in turn derived from 3-phosphoglycerate, but one publication made by supplements sellers seems to show that the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen synthesis.
In most organisms, the enzyme serine hydroxymethyltransferase catalyses this transformation via the cofactor pyridoxal phosphate:
serine + tetrahydrofolate → glycine + N5,N10-methylene tetrahydrofolate + H2O

In E. coli, glycine is sensitive to antibiotics that target folate.
In the liver of vertebrates, glycine synthesis is catalyzed by glycine synthase (also called glycine cleavage enzyme).
This conversion is readily reversible:

CO2 + NH+4 + N5,N10-methylene tetrahydrofolate + NADH + H+ ⇌ Glycine + tetrahydrofolate + NAD+
In addition to being synthesized from serine, glycine can also be derived from threonine, choline or hydroxyproline via inter-organ metabolism of the liver and kidneys.

History of Glycine:
Amino acids are organic acids containing an amino group and are the basic units of protein.
They are generally colorless crystals with a relative high melting point (over 200 °C).
Glycine is soluble in water with amphiprotic ionization characteristics and can have sensitive colorimetric reaction with ninhydrin reagent.

In 1820, glycine with the simplest structure was first discovered in a protein hydrolysis product.
Until 1940, it has been found that there were about 20 kinds of amino acids in nature.
They are necessary for the protein synthesis of both human and animal.

They are mostly α-L-type amino acids. According to the different number of amino groups and carboxyl groups contained in amino acids, we classify amino acids into neutral amino acids (glycine, alanine, leucine, isoleucine, valine, cystine, cysteine, A methionine, threonine, serine, phenylalanine, tyrosine, tryptophan, proline and hydroxyproline, etc.) with the amino acid molecules containing only one amino group and a carboxyl group; acidic amino acid (glutamate, aspartate) which contains two carboxyl and one amino group; alkaline amino acids (lysine, arginine) which molecularly contains one carboxyl group and two amino groups; Histidine contains a nitrogen ring which exhibits weakly alkaline and thus also belonging to alkaline amino acids.

Amino acids can be obtained both from protein hydrolysis and from chemical synthesis.
Since the 1960s, industrial production mainly applied microbial fermentation, such as monosodium glutamate factory has been widely applied fermentation method for production of glutamate.
In recent years, people has also applied petroleum hydrocarbons and other chemical products as raw materials of fermentation for production of amino acids.

Glycine was discovered in 1820 by French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid.
He originally called it "sugar of gelatin", but French chemist Jean-Baptiste Boussingault showed in 1838 that it contained nitrogen.

In 1847 American scientist Eben Norton Horsford, then a student of the German chemist Justus von Liebig, proposed the name "glycocoll"; however, the Swedish chemist Berzelius suggested the simpler current name a year later.
The name comes from the Greek word γλυκύς "sweet tasting" (which is also related to the prefixes glyco- and gluco-, as in glycoprotein and glucose).

In 1858, the French chemist Auguste Cahours determined that glycine was an amine of acetic acid.
Glycine is an essential component in the synthesis of proteins.
Proteins are crucial for the structure and function of cells, tissues, enzymes, and various other biological molecules.

Uses Of Glycine:
Glycine is used for the pharmaceutical industry, organic synthesis and biochemical analysis.
Glycine is used as a buffer for the preparation of tissue culture media and the testing of copper, gold and silver.
In medicine, Glycine is used for the treatment of myasthenia gravis and progressive muscular atrophy, hyperacidity, chronic enteritis, and children hyperprolinemia diseases.

Glycine is used for the treatment of myasthenia gravis and progressive muscular atrophy; treatment of excess stomach acid ester disease, chronic enteritis (often in combination antacid); using in combination with aspirin can reduce the irritation of the stomach; treatment of children hyperprolinemia; as the nitrogen source for generating non-essential amino acid and can be added to a mixed amino acid injection.
Glycine is primarily used as a nutritional additive in chicken feed.

Glycine is used as a kind of nutritional supplement which is mainly used for flavoring.
Glycine is used for alcoholic beverage in combination with alanine; the addition amount: grape wine: 0.4%, whiskey: 0.2%, champagne: 1.0%.
Others such as powder soup: 2%; lees marinated foods: 1%.

Because Glycine is tasted like shrimp and cuttlefish, and thus can be used in sauces.
Glycine has some certain inhibitory effects on the Bacillus subtilis and E. coli and thus can be used as the preservatives of surimi products and peanut butter with the added amount being 1% to 2%.
Because glycine is amphiprotic ions containing both amino and carboxyl groups, it has a strong buffering property on the taste feeling of salt and vinegar.

The added amount is: salted products: 0.3% to 0.7%, acid stain product: 0.05% to 0.5%. Antioxidant effect (with its metal chelation): being added to butter, cheese, and margarine extend the storage duration by 3 to 4 times.
To make the lard oil in baked food be stable, we can add 2.5% glucose and 0.5% glycine.
Adding 0.1% to 0.5% glycine to the wheat flour for making convenient noodles can play a role of flavoring.

In pharmacy, Glycine is used as antacids (hyperacidity), therapeutic agent for muscle nutritional disorder as well as antidotes.
Moreover, glycine can also be used as the raw material for synthesizing amino acids like threonine.
Glycine can be used as a spice according to the provisions of GB 2760-96.

Glycine is also known as aminoacetic acid.
In the field of pesticide production, Glycine is used for synthesizing the glycine ethyl ester hydrochloride which is the intermediate for the synthesis of pyrethroid insecticides.
Moreover, Glycine can also be used for synthesizing fungicides iprodione and solid glyphosate herbicide; in addition it is also used in various kinds of other industries such as fertilizer, medicine, food additives, and spices.

Glycinev is used as a solvent to remove carbon dioxide in the fertilizer industry.
In the pharmaceutical industry, Glycine can be used as amino acid preparations, the buffer of chlortetracycline buffer and as the raw material for synthesizing the anti-Parkinson's disease drugs L-dopa.
Moreover, Glycine is also the intermediate for producing ethyl imidazole.

Glycine is also an adjunct therapy medicine for treating neural hyperacidity and effectively suppressing excess amount of gastric ulcer acid.
In the food industry, Glycine is used for the synthesis of alcohol, brewing products, meat processing and cold drinks formula.
As a food additive, glycine can be used alone as a condiment and also used in combination with sodium glutamate, DL-alanine acid, and citric acid.

In other industries, Glycine can be used as a pH adjusting agent, being added to the plating solution, or used as the raw material for making other amino acids.
Glycine can further be used as biochemical reagents and solvent in organic synthesis and biochemistry.
Glycine is used as the intermediates of pharmaceutical and pesticide, decarbonation solvents of fertilizers, plating fluid, etc.

Glycine is used as a solvent for removing carbon dioxide in the fertilizer industry.
In pharmaceutical industry, it is used as the buffer of chlortetracycline, amino antacids, and used for the preparation of L-dopa.
In food industry, Glycine can be used as flavoring agents, agent for removing saccharine bitter taste, for brewing, meat processing, and preparation of soft drinks.

In addition, Glycine can also be used as a pH adjusting agent and used in the preparation of the plating solution.
Glycine is used as biochemical reagents for the pharmaceutical, food and feed additives; it can also be used as a non-toxic decarbonization agent in the field of fertilizer industry.
Glycine is an amino acid used as a texturizer in cosmetic formulations.

Glycine makes up approximately 30 percent of the collagen molecule.
Glycine is one of the non-essential amino acids and is used to help create muscle tissue and convert glucose into energy.
Glycine is also essential to maintaining healthy central nervous and digestive systems.

Glycine is used in the body to help construct normal DNA and RNA strands – the genetic material needed for proper cellular function and formation.
Without glycine the body would not be able to repair damaged tissues; the skin would become slack as it succumbed to UV rays, oxidation, and free radical damage, and wounds would never heal.
Glycine may have a protective effect on muscles, especially during conditions that increase oxidative stress.

This could be relevant in situations like intense exercise or certain diseases.
Glycine has been studied for its potential anti-inflammatory effects, making it a candidate for conditions involving chronic inflammation.
Glycine is involved in various metabolic processes.

Glycine plays a role in the synthesis of heme, a component of hemoglobin, and contributes to the regulation of blood sugar levels and fat metabolism.
As a component of glutathione, glycine contributes to the body's antioxidant defense system.
Antioxidants help neutralize free radicals, which can damage cells and contribute to aging and various diseases.

Glycine is involved in the synthesis of serotonin, a neurotransmitter that plays a role in mood regulation.
Some studies have explored the potential antidepressant effects of glycine.
Glycine is involved in the detoxification process in the liver.

Glycine helps the liver remove toxins from the body and plays a role in the synthesis of various important molecules in the liver.
Collagen, which contains glycine, is crucial for maintaining the elasticity and hydration of the skin.
Some people use glycine supplements or collagen products to support skin health and reduce the signs of aging.

Glycine receptors are found in various tissues throughout the body, and glycine itself plays a role in cell signaling processes.
Some studies suggest that glycine may have protective effects on the cardiovascular system, including its potential to reduce blood pressure and improve lipid profiles.
Glycine is not widely used in foods for its nutritional value, except in infusions. Instead, glycine's role in food chemistry is as a flavorant.

Glycine is mildly sweet, and it counters the aftertaste of saccharine.
Glycine also has preservative properties, perhaps owing to its complexation to metal ions.
Metal glycinate complexes, e.g. copper(II) glycinate are used as supplements for animal feeds.

Glycine is a significant component of some solutions used in the SDS-PAGE method of protein analysis.
Glycine serves as a buffering agent, maintaining pH and preventing sample damage during electrophoresis.
Glycine is also used to remove protein-labeling antibodies from Western blot membranes to enable the probing of numerous proteins of interest from SDS-PAGE gel.

This allows more data to be drawn from the same specimen, increasing the reliability of the data, reducing the amount of sample processing, and number of samples required.
This process is known as stripping.
Glycine acts as an inhibitory neurotransmitter in the central nervous system.

Glycine plays a role in signal transmission in the brain and spinal cord, contributing to the regulation of motor and sensory functions.
As a constituent of collagen, glycine is vital for maintaining the integrity and strength of connective tissues, such as skin, bones, cartilage, and tendons.
Glycine is involved in the synthesis of glutathione, a powerful antioxidant that plays a crucial role in the detoxification of harmful substances in the liver.

Some people use glycine supplements to improve sleep quality.
Research suggests that glycine may have a calming effect on the brain, potentially aiding in relaxation and sleep initiation.
Due to its role in collagen synthesis, glycine is essential for wound healing and tissue repair.

Collagen provides structural support to tissues, contributing to the healing process.
Glycine receptors are found in the central nervous system, and glycine itself is involved in various neurological processes.
Some studies suggest that glycine may have a role in cognitive function and memory.

Glycine, as a component of collagen, supports the health and structure of joints.
This is why some people use glycine supplements to promote joint health, although more research is needed in this area.
Glycine may play a role in regulating blood sugar levels and improving insulin sensitivity, making it a subject of interest in diabetes research.

Some research suggests that glycine may have potential benefits for cardiovascular health, including its anti-inflammatory effects and potential to support blood vessel health.
Glycine, as part of gelatin derived from collagen, may contribute to the health of the gut lining and aid in the treatment of certain gastrointestinal conditions.
Glycine may also improve liver health and function.

In male Wistar rat models of alcohol-induced liver damage, glycine supplementation alleviated damage from alcohol-induced liver injury.
Another study demonstrated increased fatty acid oxidation and increased glutathione synthesis in the livers of mice with non-alcohol-induced liver injury.
These results demonstrate that glycine acts on the liver, protecting it from long-term damage.

Safety Profile Of Glycine:
While rare, some individuals may be allergic to glycine.
Allergic reactions can range from mild symptoms such as itching and hives to severe reactions like difficulty breathing.
High doses of glycine may cause gastrointestinal discomfort, including nausea, vomiting, and diarrhea.

Glycine's essential to adhere to recommended dosage guidelines to minimize the risk of these side effects.
Glycine supplements may interact with certain medications.
For example, glycine can affect blood sugar levels, so individuals taking medications for diabetes should consult their healthcare provider before using glycine supplements.

Additionally, glycine may have additive effects when taken with certain medications that influence the central nervous system.
Some studies suggest that glycine supplementation may have a mild blood pressure-lowering effect.
Individuals with low blood pressure or those taking medications to lower blood pressure should use glycine supplements with caution and under the guidance of a healthcare professional.

Synonyms Of Glycine:
glycine
2-Aminoacetic acid
56-40-6
aminoacetic acid
Glycocoll
Aminoethanoic acid
Glycolixir
H-Gly-OH
Glycosthene
Glicoamin
Aciport
Padil
Hampshire glycine
L-Glycine
Amitone
Leimzucker
Aminoazijnzuur
Acetic acid, amino-
Glycine, non-medical
Sucre de gelatine
Glycinum
GLY (IUPAC abbrev)
Gyn-hydralin
Corilin
Glicina
Glycine [INN]
Glyzin
FEMA No. 3287
Acido aminoacetico
Glycinum [INN-Latin]
Acide aminoacetique
Glicina [INN-Spanish]
Acidum aminoaceticum
gly
Glykokoll
Aminoessigsaeure
Hgly
CCRIS 5915
HSDB 495
Acide aminoacetique [INN-French]
Acido aminoacetico [INN-Spanish]
Acidum aminoaceticum [INN-Latin]
AI3-04085
NSC 25936
25718-94-9
GLYCINE 1.5% IN PLASTIC CONTAINER
H2N-CH2-COOH
amino-Acetic acid
EINECS 200-272-2
UNII-TE7660XO1C
MFCD00008131
NSC-25936
[14C]glycine
TE7660XO1C
DTXSID9020667
CHEBI:15428
Glycine [USP:INN]
NSC25936
CHEMBL773
DTXCID90667
Glycine iron sulphate (1:1)
GLYCINE-1-13C-15N
GLYCINE-2-13C-15N
EC 200-272-2
aminoacetate
Athenon
Glycine (USP:INN)
NCGC00024503-01
Glycinum (INN-Latin)
Glicina (INN-Spanish)
GLYCINE (II)
GLYCINE [II]
GLYCINE (MART.)
GLYCINE [MART.]
Glycine, free base
GLYCINE (USP-RS)
GLYCINE [USP-RS]
GLYCINE (EP MONOGRAPH)
GLYCINE [EP MONOGRAPH]
GLYCINE (USP MONOGRAPH)
GLYCINE [USP MONOGRAPH]
Acide aminoacetique (INN-French)
Acido aminoacetico (INN-Spanish)
Acidum aminoaceticum (INN-Latin)
CAS-56-40-6
Glycine, labeled with carbon-14
AMINOACETIC ACID 1.5% IN PLASTIC CONTAINER
Aminoessigsaure
Aminoethanoate
18875-39-3
amino-Acetate
2-aminoacetate
Glycine;
[3H]glycine
Glycine USP grade
H-Gly
L-Gly
Gly-CO
Gly-OH
L-Glycine,(S)
[14C]-glycine
Corilin (Salt/Mix)
Tocris-0219
Glycine (H-Gly-OH)
GLYCINE [VANDF]
NH2CH2COOH
GLYCINE [FHFI]
GLYCINE [HSDB]
GLYCINE [INCI]
Glycine, >=99%
GLYCINE [FCC]
GLYCINE [JAN]
GLYCINE [MI]
Glycine (JP17/USP)
Glycine, 99%, FCC
GLYCINE [WHO-DD]
Biomol-NT_000195
bmse000089
bmse000977
WLN: Z1VQ
Gly-253
GLYCINE [GREEN BOOK]
GTPL727
AB-131/40217813
GLYCINE [ORANGE BOOK]
Treating Gingivitis Toothpaste
Glycine, Electrophoresis Grade
BPBio1_001222
GTPL4084
GTPL4635
Repair Cracked Teeth Toothpaste
BDBM18133
AZD4282
Glycine, >=99.0% (NT)
Glycine, 98.5-101.5%
Pharmakon1600-01300021
Glycine 1000 microg/mL in Water
2-Aminoacetic acid;Aminoacetic acid
BCP25965
CS-B1641
HY-Y0966
Glycine, ACS reagent, >=98.5%
Tox21_113575
Glycine, 99%, natural, FCC, FG
HB0299
NSC760120
s4821
STL194276
Glycine, purum, >=98.5% (NT)
Glycine, tested according to Ph.Eur.
AKOS000119626
Glycine, for electrophoresis, >=99%
Tox21_113575_1
AM81781
CAREDO Treating Gingivitis Toothpastes
CCG-266010
DB00145
NSC-760120
Glycine - Absolute carbon isotope ratio
Glycine, BioUltra, >=99.0% (NT)
Glycine, BioXtra, >=99% (titration)
SERINE IMPURITY B [EP IMPURITY]
CAREDO Repair Cracked Teeth Toothpastes
Glycine, SAJ special grade, >=99.0%
NCGC00024503-02
NCGC00024503-03
BP-31024
Glycine, Vetec(TM) reagent grade, 98%
CAREDO Treating Gingivitis Toothpastes100g
FT-0600491
FT-0669038
G0099
G0317
Glycine, ReagentPlus(R), >=99% (HPLC)
CAREDO Repair Cracked Teeth Toothpastes100g
EN300-19731
A20662
C00037
D00011
D70890
M03001
L001246
Q620730
SR-01000597729
Glycine, certified reference material, TraceCERT(R)
Q-201300
SR-01000597729-1
Q27115084
B72BA06C-60E9-4A83-A24A-A2D7F465BB65
F2191-0197
Glycine, European Pharmacopoeia (EP) Reference Standard
Z955123660
Glycine, BioUltra, for molecular biology, >=99.0% (NT)
InChI=1/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5
Glycine, United States Pharmacopeia (USP) Reference Standard
Glycine, Pharmaceutical Secondary Standard; Certified Reference Material
Glycine, analytical standard, for nitrogen determination according to Kjeldahl method
Glycine, from non-animal source, meets EP, JP, USP testing specifications, suitable for cell culture, >=98.5%
Glycine, meets analytical specification of Ph. Eur., BP, USP, 99-101% (based on anhydrous substance)