Lysine Acetylsalicylate

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The Form of Existence

According to optical activity, lysine has l-type (left-handed), d-type (right-handed) and dl-type (de-rotation) three configurations. Only the l type can be used by living things.

The active content of l-lysine is generally 77%-79%. Monopyrate animals can not synthesize lysine on their own, do not participate in transamino act. D-amino acids and l-amino acids of amino acids after acetylation, can be by the d-amino acid oxidase or l-amino acid oxidase action and deaminogen, deaminogenic ketoacids no longer play the role of amino, that is, the deamino reaction is irreversible, therefore, often in animal nutrition is insufficient.

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Physical and Chemical Properties

The commonly referred to as lysine refers to type l. L-type lysine is a needle-like crystal, darkened at 210 degrees c, decomposed at 224.5 degrees c, soluble in water, slightly soluble in alcohol, insoluble in ether.

Biochemical Metabolism

Lysine is absorbed only by organisms in the l-type. Free lysine easily absorbs carbon dioxide from the air, crystallization is difficult, and general commodities exist in the form of lysine. Lysine is soluble in water and is one of the easiest to absorb by mouth compared to other amino acids. Ingestion of lysine in the body, first by active transport from the small intestine cavity into the small intestine mucosa cells, and then through the door vein into the liver; the decomposition and metabolism of lysine is also carried out in the liver, it is condensed with ketotrec acid to form yeast amino acids, yeast amino acids are then converted tol-α-aminohexic acid semi-aldehyde, and eventually converted to produce acetyl coenzyme a. Unlike other amino acids, lysine does not participate in transamino act, and the deamino reaction is irreversible, so the decomposition and metabolism of lysine is very special. Lysine is a sugary and ketogenic amino acid, so it can participate in the formation of d-glucose, glycogen, lipids, and ultimately produce energy.

Human absorption experiments show that the absorption rate of lysine supplements is the same as that of lysine in food proteins, indicating that lysine supplements are an effective way to improve dietary lysine deficiency. The study found that within 5-7 hours of eating, lysine is quickly transferred to muscle tissue. Unlike other essential amino acids, lysine accumulates more in cells of muscle tissue, suggesting that muscle tissue is a repository of free lysine in the body. Of all the essential amino acids, lysine is stored in the body the most.

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Biosynthetic Pathways

The biosynthesis pathway of lysine has been gradually clarified since 1950. The biosynthesis pathway of lysine is different from other amino acids and varies according to the type of microorganism. Bacteria' lysine biosynthesis pathways require the synthesis of lysine through diaminoquine diacid (dap). The biosynthesis pathway of lysine in yeast and mold needs to be synthesized by α-aminohexic acid. The same is the diamino-diacid synthesis lysine pathway, different bacteria, lysine biosynthesis regulation mechanism is different.

Asparticine Pathway

Aspartic acid is reacted to synthesize diaminoic acid (dap), which in turn synthesizes lysine. The lysine synthesis pathway in yeast requires the reaction of aspartame to synthesize α-amino acetylate, α-amino acetylate by lysx,lysz,lysy,lysj,argd,lysk, and arge gene products catalyze the production of acetylation intermediates n-acetyl-l-α-aminoacetic acid, etc. To produce lysine.

The aspartame pathway, also known as the diaminoic acid pathway, is mostly present in bacteria, green algae, protozoa and higher plants, and can also be synthesized with sulphine, methionine and isolyuctamate.

α-aminohexic Acid Pathway

Synthesis by 2-ketone diacid and acetyl coenzyme a via α-aminoacetic acid pathway. The five-step reaction is catalyzed by isocirate synthase, ute acid synthase/shun-head acid synthase, utrexate dehydrogenase, 2-ketone diacid and acetyl coenzyme a α-amino acetylase. In the second reaction, α-aminoacetic acid is catalyzed to produce lysine by α-amino acetylase, yeast amino acid reductase, and yeast amino dehydrogenase.

α-aminoacetic acid pathways are present in higher fungi and paleobacteria.

E-mail: lilyoo@bbcapharma.com

Food Source

Lysine is one of the components of protein, and protein-rich foods generally contain lysine, which is found in animal foods such as lean meat, fish, shrimp, crab, shellfish, eggs and dairy products for livestock and poultry, and legumes (including soy, beans, and their products). In addition, almonds, hazelnuts, peanut kernels, pumpkin kernels and other tree nuts in the lysine content is also relatively high. Cereals are the first restrictive amino acid because of their low lysine content and easy to be destroyed during processing.

The Amount the Human Body Needs

The amount of lysine required varies from group of people (infants, adolescents, adults). In 2005, the u.S. Food and nutrition commission set the adult lysine requirement at 31 mg.Kg, based on the results of the study at the time-1·d-1.

In 2007, the who/fao/unu committee of experts determined that lysine requirements were 30 mg.Kg based on the results of relevant human trials-1·d-1, this value is currently generally accepted. The lysine needs of infants and adolescents identified by who/fao are (mg.Kg).-1·d-1: 1 month (119), 2 months (87), 3 months (75), 4 months (68), 6 months (65), 1-2 years (45), 3-10 years (35), 11-14 years (35), 15-18 years (33). At present, CHINA has not yet formulated the recommended intake standard of dietary lysine for people who conform to the dietary habits of chinese residents.

E-mail: lilyoo@bbcapharma.com

Digestion Rate and Utilization Rate

The absorption efficiency of d-leigh and l-type lysine is different,d-lysine can hardly be absorbed and utilized, and the main biological activity is l-lysine. The ε-amino acid of lysine is very active and easily binds to the active carbula group in the feed to produce compounds that are difficult to absorb and utilize.

Nutritional Physiological Function

Lysine regulates the body's metabolic balance, and lysine provides structural components for the synthesis of carnitine, which promotes the synthesis of fatty acids in cells. Adding a small amount of lysine to food can stimulate the secretion of gastric proteases and stomach acids, improve the secretion of stomach fluid, and play an important role in enhancing appetite to promote the growth and development of young children. Lysine can also improve the absorption of calcium and its accumulation in the body, speeding up bone growth. If the lack of lysine, will cause insufficient secretion of stomach fluid and anorexia, nutritional anemia, resulting in central nerve obstruction, stunting. Lysine can also be used as an auxiliary drug for diuretics in medicine, to treat lead poisoning caused by the reduction of chlorides in the blood, but also with acidic drugs (such as salicylic acid, etc.) To produce salts to reduce adverse reactions, in combination with methionine can inhibit severe hypertension, and studies have shown that lysine supplementation can accelerate the recovery of herpes infection and inhibit its recurrence.

Participate in the Synthesis of the Body's Proteins

Lysine, as an essential amino acid in the body, is involved in the synthesis of various proteins such as skeletal muscle, enzymes, serum proteins, peptide hormones and so on.

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Participate in Energy Metabolism

Lysine is involved in the biosynthesis of carnitine in the body. Carnitine plays an important role in fat metabolism and is an essential cofactor of fat metabolism. Lysine is one of the precursor substances of synthetic carnitine, so supplementing lysine can speed up fat metabolism in the body. Lysine has a strong function through the blood-brain barrier, can directly into brain tissue, affect the respiratory chain, for the repair of nerve cells and normal physiological activities to provide the necessary energy source.

Promotes the Absorption of Minerals and Bone Growth

Lysine can be chelated with calcium, iron and other mineral elements to form a soluble small molecular monomer, promoting the absorption of these mineral elements.

Enhances Immune Function

Lysine is considered a nonspecific bridge molecule that connects antigens to t cells, causing them to produce specific effects on antigens.

Treatment of Herpes Simplex Virus Infection

The study also found that supplementation with lysine can treat herpes simplex virus infection.

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Fermentation Process

Lysine fermentation can be divided into two-step fermentation method (also known as precursor addition method) and direct fermentation method.

Two-step Fermentation Method

The two-step fermentation method was developed in the early 1950s, and the two-step fermentation method is based on the precursor diaminoquine diacid acid of lysine, which is converted into lysine after deoxygenation by microbial production of enzymes (diamino-diazepam). Because diaminoic acid is also produced by fermentation, it is called step fermentation. After the 1970s, japan improved the process by using a fixed diamino acid deglutase or a bacterium containing this enzyme to continuously produce lysine. Despite this, the process is still complex and has been replaced by direct fermentation.

Direct Fermentation Method

Direct fermentation is a widely used lysine production method. Commonly used raw materials for sugar cane or beet sugar after waste molasses, starch hydrolysate and other cheap sugar raw materials. In addition, acetic acid, ethanol and so on are also available as raw materials. The main microorganisms that produce lysine by direct fermentation method are the mutant strains of lollipop glutamate, yellow short bacillus, and lactobacillus fermented short bacillus. This method was developed in the late 1950s, and since the 1970s, due to the development of breeding technology, some mutant strains with multiple genetic markers have been selected, making the process more mature and the yield of lysine multiply. The highest acid yield in industrial production has been raised to 100-120g per liter fermentation, and the extraction rate has reached about 80%-90%.

E-mail: lilyoo@bbcapharma.com

The Status Quo of Production

L-lysine was originally isolated from protein hydrolysis, protein hydrolysis is generally based on animal blood powder as raw material, this method is characterized by simple process, but limited raw material sources, only suitable for small-scale production. Then there is the chemical synthesis method, enzyme method, the use of synthesis method mainly has the dutch dms method and japan's toray method, the biggest disadvantage of this method is the use of highly toxic raw materials photogas, may residual catalysts, poor product safety, there are serious environmental problems. In 1960, japan first adopted microbial fermentation. Microbial fermentation produces amino acids, which artificially relieve the metabolic control mechanism of amino acid biosynthesis, causing them to accumulate a large number of required amino acids. The l-type stereoscopic specificity of amino acids determines that the process of producing amino acids by fermentation is simpler and faster than that of chemical synthesis. In the mid-1960s, CHINA began to carry out research on the selection and fermentation of lysine strains, but it is difficult to industrialize due to low yield. It was not until the late 1970s and early 1980s that CHINA's research made a breakthrough after the industrialization of lysine in the world. At present, most of the world's enterprises producing lysine use fermentation method, the production of l-type lysine, production process has been basically mature.

The strains used for industrial fermentation to produce lysine are mainly fine mutant strains such as bacillus and bacillus, which have high economic value, of which glutamate bacillus is the most widely used. In addition, lysine production has also been reported for the use of e. Coli, yellow short bacteria, brewing yeast, lactate fermentation short bacteria, false silk yeast, etc.

There are four main types of microorganisms producing lysine: wild type, nutritional mutation type, regulatory mutation type and nutritional regulation mutant type. Industrially, fermentation conditions (mixing speed, ph, dissolved oxygen, temperature and co) are modified by optimizing fermented strains (mutagenic and genetically engineered).2to increase lysine production. The methods of obtaining high-yielding microbial strains are traditional mutagenic methods (ultraviolet, x-ray, nitrogen mustard and nitrosylsters, etc.), Protoplasm fusion and genetic engineering methods. Lysine produced by mutagenic strains is reported to increase by 40%-50%. Mutagenic strains to low-cost carbon sources as fermentation raw materials, such as a variety of starch hydrolytic sugar, honey, acetic acid and ethanol, fermentation production of lysine, through separation, concentration, evaporation, crystallization, drying production process to obtain feed-grade lysine, refinement can be obtained food-grade, pharmaceutical-grade products.

E-mail: lilyoo@bbcapharma.com

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