Category Archives: health care materials

Ethoxyquin Msds

1, Ethoxyquin Ethoxyquin
Alias ​​tiger spirit, antioxidant quinoline
Coding GB 17.010; INS 324
Light yellow to amber viscous liquid, long-term placement in light and air gradually becomes dark brown liquid, but does not affect its antioxidant effect, the boiling point of 134 ~ 136 ℃ (13.33Pa), the refractive index of 1.569 ~ 1.672, the relative density 1.029 ~ 1.031, insoluble in water, miscible with ethanol arbitrary.
Method of on – phenetidine iodine and acetone in the reaction catalyzed by ring closure system.
Identification of the product was dissolved in 10mL 1mg acetonitrile, which was strong fluorescence under short-wave UV light.
1. Mouse oral LD50 1680 ~ 18080mg/kg weight.
1470mg oral rat; kg body weight.
2. GRAS FDA-21CFR 172.140.
The use of preservatives, fruit preservative.
2 Precautions
(1) This product is mainly used for apples, pears Storage tiger prevention of disease. This product can be made ​​of latex dipped fruit, liquid concentration 2 ~ 4g/kg, this product can also be applied to the wrapping paper made ​​from fruit bag, add a plastic film bags made ​​of fruit, or fruit boxes such as binding by its nature and fumigation work.
With effect (2) This product is also available with other preservatives.
2. Scope and usage
(1) China’s “food additives health standards” (GB 2760-1996) states: Fresh apple production may need to use the right amount of residual amount of 1mg/kg.
(2) Other countries: as antioxidants food, beverage, oil and pharmaceuticals, such as vitamin A, or be used in carotene allows stable performance. Applications can be maintained in food freshness and nutritional value of food, oil can not rancidity deterioration, preservation and storage of feed has a significant advantage, as the red hot pink color protection is also effective antioxidant amount of 0.1g / kg.

Uridine (UR) msds

Basic Information
Product Code: SHG018
Chinese name: uridine (uridine)
Chinese alias: uridine, uridine, uridine
Name: Uridine
English Name: 1-β-D-Ribofuranosyluracil; Uracil-1-β-D-ribofuranoside
Linear Formula:
Purity: ≥ 99% (HPLC)
CAS: 58-96-8
Molecular formula: C9H12N2O6
Molecular Weight: 244.20
2 Performance description
Appearance Description: White needle crystal or powder; odorless. Slightly sweet and slightly acrid taste. Soluble, slightly soluble in dilute alcohol, insoluble in ethanol. Constitute a relevant component of animal cell nucleic acids.
Three physical parameters
Melting point: 162.0 ~ 171.0 ℃
Specific rotation: +6.0 ° ~ +10.0 °
Loss on drying: ≤ 0.5%
Residue on ignition: ≤ 0.1%
Heavy metal: ≤ 10ppm
Purity (HPLC): ≥ 99.0%
Content (UV): 98.0 ~ 102.0%
4 Use Description
Uridine is a drug, such as anti-giant red blood cell anemia, treatment of liver; cerebrovascular; cardiovascular and other diseases, but also the manufacturing fluorouracil (S-FC); nucleoside; idoxuridine (IDUR); bromine glycosides (BUDR); fluorine the main raw materials glycosides (FUDR) and other drugs.
Storage conditions: room temperature sealed dry preservation
5 Dangerous Description
Dangerous code: Xi
Hazard Class: R36/37/38
Security Level: S24/25-36-26

N-acetyl-L-tyrosine (ACETYLTYROSINE) Basic Information

Chinese name: N-acetyl-L-tyrosine
Chinese alias: acetyl tyrosine
English name: N-acetyl-L-tyrosine
English Name: L-TYROSINE, N-ACETYL-; [1] ACETYLTYROSINE; ACETYL-L-TYROSINE; AC-TYR-OH; AC-TYROSINE; N-AC-L-TYR; N-ACEYL-L-TYROSINE; (2S) -2 – (acetylamino) -3 – (4-hydroxyphenyl) propanoate
CAS :537-55-3
EINECS :208-671-3
MF: C11H12NO4
MW: 222.2178
Melting point: 149-152 ℃
Boiling Point: 531.3 ° C at 760 mmHg
Flash Point: 275.1 ° C
Vapor Pressure: 4.07E-12mmHg at 25 ° C
Specific rotation of 47.5 ° (c = 2, water)
N-acetyl-L-tyrosine is important fine organic chemical intermediates, widely used in medicine, pesticides, chemical industry and other fields

L-tryptophan Production Method

L-tryptophan produced mainly by chemical synthesis of the first method and the method of manufacture of a protein hydrolyzate. With the continuous development of microbial production of tryptophan research, people began using microbial fermentation method tryptophan. Now to practical and dominant. Microbiological method can be roughly divided into microbial fermentation and enzymatic conversion method. In recent years, there was even a direct fermentation and chemical synthesis, research and production of tryptophan direct fermentation and transformation Combination. Another technology, genetic engineering, enzyme immobilization and high density cultivation on microorganisms and enzymes breeding industry has greatly promoted the industrialization process of direct fermentation and enzymatic production of tryptophan.
Protein hydrolysis
L-tryptophan produced mainly by proteolysis first and chemical synthesis method. Protein hydrolysis method is based on hair, blood meal and waste as raw silk and other protein families, by alkaline hydrolysis and enzymatic hydrolysis method for producing L-tryptophan. With the development of amino acid production technology, it is now rarely used in the production of L-tryptophan.
Chemical synthesis
Chemical synthesis method is to use production methods of organic synthesis and chemical engineering technology or a combination of amino acids was prepared. DL-tryptophan chemical synthesis method can be broadly divided into two synthesis of indole synthesis as raw material and as raw material with phenylhydrazine. Snydcr and MacDonald developed a simple synthesis of DL-tryptophan
Method, i.e. the use of indole acrylic acid and α-acetamido direct condensation in the presence of acetic acid and acetic anhydride to give N-acetyl-DL-tryptophan, the substance can be hydrolyzed in a solution of sodium hydroxide to give DL-tryptophan, the yield was 57.7%. Moe with phenylhydrazine and MacDonald reported for the synthesis of tryptophan, i.e., in the presence of sodium acetate, and acrolein diethyl acetamido malonate condensation condensate is then reacted with hydrazine to produce phenylhydrazone in phenylhydrazone BF3 refluxing aqueous H2S04 or hydrolyzed cyclized compound 3 – indolyl – methyl – acetamido – malonate, hydrolysis of this compound can be obtained decarboxylation DL-tryptophan.
The biggest advantage is that the chemical synthesis method is not limited in the variety of amino acids, prepared either natural amino acids, unnatural amino acids can be prepared in a variety of special structure. This does not mean having a value of production industry, because the amino acid is synthesized racemic DL-type, must be split in order to obtain L-amino acids can be utilized. Therefore, when produced by chemical synthesis DL-tryptophan, synthesis conditions should be considered in addition to, but also consider the use of splitting with racemic isomer D-tryptophan isomers, three are indispensable. Thus, the chemical synthesis of L-tryptophan in industrial applications are also subject to certain restrictions.
Enzymatic conversion method
Enzymatic catalytic function is the use of microorganisms to produce L-tryptophan, L-tryptophan biosynthetic enzymes are able to use chemical precursors for the synthesis of raw materials, give full play to the advantages of both organic synthesis techniques, but also has the product high concentration, high yield, high purity, less byproducts, easy purification operation, etc., is a low-cost method for the production of industrial production of tryptophan. Currently in production of L-tryptophan is widely used. These enzymes include enzymes tryptophan, tryptophan, serine racemic enzymes. According to these enzymes provide the number of microbial species can be divided into double and single bacterial enzyme bacterial enzyme types.
Dual enzyme is using two strains of bacteria are needed to provide the enzymatic reaction of tryptophan synthase (TS), serine racemase (SR), indole and DL-serine as a substrate enzymatic conversion of L-color histidine. This method can be of high activity with different enzymes required for the enzymatic conversion of tryptophan together to achieve the advantages of complementary species, improve the conversion rate of the substrate. Makiguchi like E. coli tryptophan synthase and serine racemase from Pseudomonas putida, with DL-serine and indole as a substrate, the reaction in the reaction tank 200L 24h, L-tryptophan production can be achieved 110g / L, the absorption rate of 100% indole (molar ratio, the same below), the yield of DL-serine was 91%. Using a single strain of bacteria is provided by enzymatic synthesis of the desired enzyme tryptophan Trp, tryptophan, serine enzymes and enzymatic conversion of racemic tryptophan enzymes. Won-giBang bacteria and other single enzyme tryptophan production were studied using high-Ts activity of E. coli B10 conversion indole and DL-serine, adding non-ionic surfactant Triton X-100, 37 ℃ reaction 60h, tryptophan acid yield up to 141.4g / L, for a yield of 93.2% indole, the DL-serine yield of 93.6%.
Since the substrate tryptophan indole synthesis inhibitory strong and weak inhibition of the enzyme tryptophan, so in recent years tend to be more enzymes for tryptophan L-tryptophan biosynthesis. Normally tryptophanase degrades tryptophan, L-pyruvate, indole and ammonia, but at high concentrations of pyruvate and ammonia conditions effective to pyruvate, indole and ammonia synthesizing L-tryptophan acid. The enzyme can catalyze L-serine or L-cysteine ​​and L-tryptophan indole synthesis. Nakazawa, such as indole to 20g, 30g sodium pyruvate, 50g ammonium acetate and 4gProteus rettgeri (Proteus Reye) bacterial enzyme tryptophan as a source, 37 ℃ reaction 48h could accumulate 23gL-tryptophan. Ujimaru other enzymatic tryptophan and L-serine with indole synthesis Achromabacterliquidum (Achromobacter liquid form) L-tryptophan, L-serine conversion was 82.4%, conversion of indole was 92.4%.
There are also a study of L-cysteine ​​and indole as raw enzymatic production of L-tryptophan. Wei et tryptophan levels and gene engineering strain WWW-4 L-cysteine ​​and the catalytic synthesis of L-tryptophan indole, 80mL reaction solution (L-cysteine ​​0.75g, 0.75g indole ) 37 ℃ reaction 48h, can accumulate L-tryptophan 1.18g, L-cysteine ​​conversion was 93.2% and 90.1% conversion of indole, the recovery rate of 70% of total product. In addition, the strain has also been reported using enzymatic conversion of L-tryptophan in high yield and with a high activity of pyruvate enzyme tryptophan.
The enzymatic conversion method using a high activity can be either a tryptophan synthase, tryptophanase, or the catalytic activity of a synthetic cell tryptophan synthase enzyme L tryptophan or tryptophan, or the enzyme may synthesis of L-tryptophan or the immobilized cells. After the bacteria and enzyme immobilization of enzymes with improved stability to facilitate re-use, easy to implement continuous and automated production advantages. Won-Bang et polyacrylamide fixed tryptophan synthase having a high activity of Escherichia coli B10 E. coli bacterial cells, in a continuous stirred tank reactor 50 days of continuous use, a tryptophan synthase activity The 80% maximum acidogenic 0.12gL-1h-1. There immobilization techniques using other enzymatic conversion of L-tryptophan. Eggers et al reported a use of organic lipid membrane systems utilize tryptophan enzymatic conversion of L-tryptophan. It is cyclohexane as the organic phase, the organic resin film to two separate aqueous phase and an organic phase, wherein the aqueous phase having an enzymatic reaction system, constituting the aqueous phase was back-extracted another system, using bis-tris-propane as two water maintaining the two-phase buffers the pH of the aqueous phase difference, thus affecting the substances in the reaction system constant distribution of the two aqueous phases, the aqueous phase is then exchanged two L pyruvate and the organic phase through an anion exchanger Aliquat-336 – tryptophan. Such a system is conducive to the transport of L-tryptophan in the aqueous phase was back-extracted, and help reduce the extraction of L-tryptophan and the inhibition of the enzyme tryptophan; Moreover, the organic phase may also store indole, the concentration of indole in the enzyme reaction system is lower than the level of inhibition of the enzyme. Eggers et also established a reaction system of reverse micelles of the enzymatic conversion of L-tryptophan, it is dissolved in water containing tryptophanase reverse micelles of the surfactant Brij56 composed of cyclohexane and water phase , the use of indole and serine as a substrate in the organic phase was added Aliquat-336 anion exchanger and transfer the aqueous phase to the organic phase L-tryptophan. To buffer bis-tris-propane as a two-aqueous phase, select the appropriate parameters such as moisture content and pH conditions, results within 1dm reaction volume per g of tryptophan can produce the enzyme reaction after lh acid 10g. The advantage of the above system in addition to the lipid membrane of the reaction system, but also can improve the stability of the enzyme tryptophan. So, has broad application prospects in the enzymatic conversion of L-tryptophan.
Microbial fermentation
Microbial fermentation method including direct fermentation and added precursor fermentation.
A direct fermentation
Direct fermentation is glucose, cane molasses as carbon source of cheap raw materials, the use of tryptophan-producing excellent strain under suitable fermentation conditions, the direct fermentation of tryptophan. Strain tryptophan excellent high and stable yield is central direct fermentation studies. In breeding technology, the traditional mutation breeding and abroad have done a lot of research. Shiio etc. Brevibacterium tyrosine deficient for fluorophenylalanine (4FP) as the starting strains resistant mutants, breeding 5 – fluoro-tryptophan (5-FT) resistant mutant strain No. 187, the strain can produce L-tryptophan, 8.0 g / L. Continue to be No. 187 for the parent strain breeding with anthranilate structurally similar heavy chlorine serine (AsaSer) resistant mutant A100, its acid production rate increased to lO. 3 g / L, then from A-100 breeding sulfaguanidine (SG) resistant mutant strain S-225, which further improves the ratio of acid to 19g / L. Zhang Suzhen and others to domestic nitrosoguanidine Beijing Corynebacterium AS1.299, mutants obtained CG45. This strain has 5MT, 6FT, 4MP resistance marker, and the arginine and uracil as essential growth factors, in a medium containing 12% glucose, 30 ℃ shaking for 5 days. Can accumulate tryptophan 8g / L. The method of earlier studies, but not for a long time to reach the industrial production. The main reason is the biosynthetic pathway from glucose to tryptophan is relatively long, the metabolic flux is relatively weak and requires a variety of synthetic tryptophan precursor (PRPP, glutamine, L-serine). To further improve the yield of L-tryptophan must also increase production of these precursors. Tryptophan biosynthetic pathway hand adjustment mechanism is relatively complex, in addition to the presence of multiple feedback regulation, there also exists a weakening subsystem. This makes the amino acid tryptophan, an amino acid fermentation industry to become one of the most difficult fermentation. With the application of recombinant DNA technology in microbial breeding, for the excellent tryptophan Strains provide a reliable technical guarantee. Making acid levels gradually reached the industrial production requirement. Katsumata. The recombinant plasmid with R, DAHP synthase (DS) and tryptophan synthase (TS) gene introduced into the production of L-tryptophan 43g / L glutamicum KY10-894, allowing the engineering strain L-tryptophan production reached 66g / L acid levels increased by 54%.
2 Add the precursor fermentation
This method is also known tryptophan microbial conversion method, which is the use of glucose as a carbon source, while adding the required synthesis of tryptophan precursors (e.g., anthranilic acid, indole, L-serine, etc.), the use of microbial acid synthesis enzymes in the body prior to conversion to synthesize L-tryptophan. This method is very early into the industrial production, the world’s largest manufacturer of tryptophan Japan Showa Denko company is using anthranilic acid as precursors using Hansenula (Hansenula) or Bacillus (Bacillus coli) strains to convert tryptophan production methods, Yokozcnki like to DL-5-indole – methyl hydantoin as raw materials, the use of Flavobacterium T-523 which is the decomposition of tryptophan, L-tryptophan can produce acid 7.1 g / L. Breeding the Bacillus subtilis Fukui et 5 – fluoro-tryptophan (5-FT) resistant mutant strains, containing l% soluble starch and 5% glucose medium, the continuous fed-anthranilic acid, can accumulate L-color acid 9.6g / L. Nakayarna further transform this mutant such, it has a 5-FT and 8 – azaguanine (8-AG) double resistance in medium containing 10% glucose, the continuous fed-anthranilic acid, can accumulate L-tryptophan 15.6g / L.
The inadequacies of the microbial transformation is higher when converted precursor solution concentration, the conversion rate has dropped, but can be fed through a small batches to reduce its precursor inhibition. In addition, the precursors are expensive, is not conducive to reducing costs. Therefore, some studies use fermentation to provide a low-cost precursors, combined with the advantages of other methods were tryptophan production. Hajimu MOrikota other P390 Brevibacterium flavum using direct fermentation of L-glutamic acid-β-semialdehyde (GSA) was 13.2g / L, and after appropriate dilution of the broth was added phenylhydrazine 1mol/LH2S04 solution was heated at reflux for 1 hour after GSA 48% L-tryptophan can be converted to. SMgeru oita such dual use of lipoic acid and thiamine deficient strain Enterobacter aetogene LT-94, production of pyruvic acid 30g / L glucose in the medium containing 5%, then by adding ammonium chloride and indole using bacteria color neuraminidase enzymatic conversion of L-tryptophan 16.7%.

L-threonine Use

1 is mainly used as nutritional supplements. Easy generation of heat and glucose caramel and chocolate flavor, there flavoring effect. Can also be used for biochemical studies.
2 for nutritional supplements, threonine is an essential amino acid. Threonine often added to minors piglets and poultry feed, is the second limiting amino acids and third limiting amino acid in poultry feed, pig feed. Add in wheat, barley and other grain-based feed.
3 nutritional supplements, also for the preparation of amino acid infusion and comprehensive amino acid preparations.
4 for the adjuvant treatment of peptic ulcer. Also can cure anemia and angina, aortic inflammation, heart failure and other cardiovascular disorders.
5 Threonine (L-threonine) is W. C. Rose 1935 Isolation and Identification of a protein hydrolyzate from the fiber, essential amino acids has been shown to be the last to be found, it is the second or third limiting amino acid in livestock, which has extremely important physiological role in the animal . Such as to promote growth, improve immune function, etc.; dietary amino acid balance, the ratio closer to the ideal of an amino acid protein, thereby reducing the protein content of animal feed requirements. Lack threonine, can lead to lower animal feed intake, growth retardation, decreased feed efficiency, suppress immune function and other symptoms. In recent years, lysine, methionine synthetics been widely used in animal feed, threonine becoming affect animal performance limiting factor, further study of threonine help effectively guide the livestock and poultry production .
Threonine (L-threonine) animals can not synthesize itself, but the amino acid is required, can be used to accurately balance the amino acid composition of the feed to meet the need to maintain animal growth, improve weight gain and lean, reduce the meat material ratio; may improve the nutritional value of feed ingredients amino acid digestion rate and improve the performance of low-energy feed production; may reduce feed crude protein levels, improve feed nitrogen utilization, reduce feed costs; can be used for pigs, chickens, ducks and senior aquatic feeding and breeding. L-threonine is the use of bio-engineering principles, corn starch and other raw materials through submerged fermentation, refining and production out of the feed additive. Adjust the balance of amino acids in feed to promote growth and improve meat quality, improve the nutritional value of feed ingredients amino acids digest low, low protein feed production, contribute to conservation of protein resources, reduce the cost of feed ingredients, reduce animal manure and urine the nitrogen content, ammonia concentration and release of animal building speed. Widely used to add piglet feed, pig feed, chicken feed, shrimp feed and eel feed.
6 threonine (L-threonine) in vivo metabolism in the decomposition, not only after deamination and transamination effect, but directly through the threonine dehydratase, threonine and threonine dehydrogenase acid aldolase catalytic conversion of an amino acid other substances, e.g. threonine can be converted to butyryl coenzyme a, succinyl coenzyme a, serine, glycine and the like. Also threonine excess can increase the lysine-α-keto reductase activity gluconate, adding the right amount of threonine eliminate lysine in the diet due to excessive weight gain caused by decreased liver and muscle tissue protein / deoxyribonucleic acid (DNA), ribonucleic acid (RNA) / DNA ratio decreased. Add threonine tryptophan or methionine also reduce the growth inhibition caused by excessive. According to reports, the chicken to absorb most of threonine in the duodenum, crop Mang and glandular stomach quickly absorbed into the liver threonine protein deposition in the body.

L-glutamic acid Instructions for use

1, in the food industry: as a salt substitute, nutritional supplements, flavor enhancer (mainly for meat, soups and poultry). Broth and soups such as for convenience foods, 10g/kg. Used in beverages, bakery products, meat, meat, sausages, milk and dairy products, flavorings, cereal products, the amount of 400mg/kg. Used as a nutritional supplement, limit of 12.4% (based on the total protein in foods meter). Can be used as shrimp, crabs and other aquatic canned produce magnesium ammonium phosphate crystals preventing agent, the amount of 0.3% to 1.6%. L – monosodium glutamate (MSG commonly known as “MSG”) has a strong flavor of meat, sugar and salt is in addition to the world’s consumption of up to a flavoring agent. In particular, the PH value of 6 to 7, MSG all dissociated strongest flavor. Is widely used for cooking and food processing. The general dosage is 0.2% to 0.5%. Per capita daily intake does not exceed 6g / d. L-Glutamic acid salt for improving the bitterness of beer, but also useful as salt substitutes, nutritional supplements, flavoring agent.
2, in the pharmaceutical industry: L – Glutamic acid is non-essential amino acids, it is metabolized in the body. Easy to lose amino, and keto transfer reaction occurs, to the synthesis of other amino acids. After eating, there is 96% L – glutamic acid can be absorbed by the body, and therefore can be used as raw nutritional supplements “elemental diet” is used in clinical practice.

L-Cystine check

Acidity take this product 1.0g, add water 100ml, fully shaking determination (Appendix Ⅵ H) according to the law, pH value should be 5.0 to 6.5. Transmittance solution to take the product 1.0g, plus 1mol / L hydrochloric acid solution 20ml dissolved, according to spectrophotometry (Appendix Ⅳ A), measured at a wavelength of 430nm light transmittance of not less than 98.0%. Chloride take the goods 0.50g, after adding dilute nitric acid to dissolve 10ml, add water to make into a 50ml, dispensing 25ml, check (Appendix Ⅷ A) according to the law, compared with standard control solution made ​​of sodium chloride solution 5.0ml, not thicker (0.02%). Sulfate take the goods 0.70g, add dilute hydrochloric acid and shake to dissolve 5ml, add water to make into a 40ml, according to inspection (Appendix Ⅷ B), 5ml compared with standard potassium sulfate solution 1.4ml dilute hydrochloric acid control solution made not more concentration (0.02%). Other amino acids take the goods, plus 1mol L hydrochloric acid solution / solution made ​​from 10mg per 1ml, thin layer chromatography (Appendix Ⅴ B) test, learn the solution 2μl, points on silica gel G plate to positive butanol – water – acetic acid (5:2:1) as the agent, after the commencement of dried, sprayed with acetone solution (1 → 50) ninhydrin, dried at 80 ℃ 10 minutes and immediately view, in addition to the main spots, shall not significant other spots. Drying of the product, dried at 105 ℃ 3 hours, less weight loss should not exceed 0.2% (Appendix Ⅷ L). Residue on ignition to take this product 1.0g, according to inspection (Appendix Ⅷ N), no residue left over 0.1%. Iron salt residue on ignition key under the residue left over, add 1ml of nitric acid, evaporated on a water bath, add dilute hydrochloric acid 4ml, after tepid dissolved, moved to 50ml of Nessler tube, according to inspection (Appendix Ⅷ G), compare and contrast 1.0ml solution made with standard iron solution, not deeper (0.001%). Heavy metals in the product 1.0g, according to inspection (Appendix Ⅷ H Third Law), containing heavy metals should not exceed ten parts per million. Arsenic take this product 2.0g, dissolved in 23ml water, add 5ml of hydrochloric acid, check (Appendix Ⅷ J First Act) law, shall comply with the provisions of (0.0001%).

Hyaluronic acid Details

Glycosaminoglycans (formerly called mucopolysaccharides, glycosaminoglycans and acidic polysaccharides) in the structure of the simplest kind, it is by repeating disaccharide units
GlcUA-β (1 → 3)-GlcNAc, with β-1, 4 glycosidic bond together. In the body, often in free form or covalently (proteoglycan complexes) in the form of complexes present.
Surface molecules which contain a lot of hydrophilic groups, the body itself can absorb 1,000 to 10,000 times the product water, the water for maintaining the loose connective tissue is important; HA while a strong viscosity of the vitreous humor and joint having Run wet and protection; still promote wound healing.
HA is present in the extracellular matrix of connective tissue of animals. Among them, the cattle vitreous, human umbilical cord and rooster combs are commonly used material extracted HA. HA is widely used in cosmetics, artificial joint, surgical lubricants and other products. The U.S. Food and Drug Administration (FDA) approved in 2003 through the use of injection repair fine lines.

Glycine Physical and chemical properties

White monoclinic or hexagonal crystals or white crystalline powder. Odorless, has a special sweetness. The relative density of 1.1607. Melting point 248 ℃ (decomposition). pK’1 (COOH) is 2.34, pK’2 (N + H3) is 9.60. Soluble in water, solubility in water: 25 ℃ when 25g/100ml; 50 ℃ when 39.1g/100ml; was 54.4g/100ml 75 ℃ while; 100 ℃ when 67.2g/100ml. Extremely difficult to dissolve in ethanol, at approximately 100g of anhydrous ethanol to dissolve 0.06g. Almost insoluble in acetone and ether. Reaction of the hydrochloride salt with hydrochloric acid. pH (50g / L solution, 25 ℃) = 5.8 ~ 6.4
Quality standards HGB 3075-79
Molecular weight 75.07
Simple structure NH2CH2COOH
Specification consumption of raw materials consumption quota, kg / t
1, TCA TCA 95% of France 1600
880 industrial grade ammonia
Methenamine 98% 350
Ethanol 95% 1100
2, Strecker Formaldehyde 70% 114
Sodium cyanide 70% 930
Ammonium chloride 70% 1020
Barium hydroxide 80% 1430
Sulfuric acid 90% 725
Glycine has a unique sweet taste, can ease acid, alkaline taste, masking the bitter taste of saccharin in food and enhance the sweetness. If an excessive amount of human intake of glycine, not only can not be absorbed by the body, and will break the balance of the body’s absorption of amino acids affect the absorption of other amino acids, leading to nutrient imbalances and affect health. Glycine as the main raw materials to produce milk drinks, normal growth and development of young people and children can easily adversely affected.(Supplies:

Glutathione Application

Glutathione has a broad spectrum detoxification, not only for drugs, but also can be used as functional food base in the anti-aging, enhance immunity, anti-tumor and other functional foods widely used.
Clinical drug
Has developed a human glutathione drug widely used in clinical, in addition to the mercapto group using its chelate heavy metals, fluorides, mustard gas poisoning, etc., but also for use in hepatitis, hemolytic disease and keratitis, cataract and retinal diseases such as drug therapy or adjuvant therapy. In recent years, Western scientists, especially Japanese researchers found that glutathione inhibit HIV function.
New research also shows that, GSH can correct acetylcholine, cholinesterase imbalance, played anti-allergic effects, but also to prevent skin aging and pigmentation, reduce the formation of melanin, the skin antioxidant capacity and to improve skin luster, in addition , GSH is also a very good effect in the treatment of diseases of the cornea and improve sexual function.
And vitamin C in combination with
In addition, vitamin C is also an important in vivo antioxidant. Since vitamin C can reversibly hydrogenation or dehydrogenation, the vitamin C has many important roles in vivo redox reaction. For example, many enzymes reactive group is a thiol group (-SH),-SH vitamin C can be maintained in the reduced state to maintain enzyme activity; vitamin C allow oxidized glutathione into reduced glutathione (GSH ), so that hydrogen peroxide (H2O2) to restore the body’s metabolism; Vitamin C also protects vitamin A, E and some B vitamins from oxidation. Therefore, the use of glutathione, vitamin C and used, to improve their effectiveness.
Adding glutathione may play an unexpected role
1, added to pasta, you can play a role in the reduction. Not only shorten the manufacturing time for the bread to the original half or one-third, a significant improvement in labor conditions and serve to strengthen the role of food and nutrition, and other functions.
2, add it to yogurt and infant foods, the equivalent of vitamin C, can play a role in stabilizing agent.
3, which was mixed into the fish cake, and prevents the color deepened.
4, add the meat and cheese and other foods with enhanced flavor effect.