Vitamix Premium BR: full spectrum of limited amino acids in one premix
The use of Vitamix Premium BR premixes in feeding broiler chickens allows poultry farms to independently produce ready-made feeds using their own protein and grain raw materials, controlling all critical points. Vitamix Premium BR premixes are individually developed based on the client’s existing raw material base and the parameters of broiler chicken growing.
One of the components of the premixes is synthetic amino acids, which constitute the main part of the cost of these products.
Amino acids are organic compounds whose physical and chemical properties and various reactions are determined by the presence of the main amino group and the acidic carboxyl group in the molecule.
Amino acids, as the basic components of proteins, participate in all vital processes. In addition to the amino acids that make up proteins, living organisms have a constant reserve of “free” amino acids in the blood, tissues, and cells. They are in dynamic equilibrium in numerous exchange reactions and are necessary for performing specific functions.
Amino acids that are constantly found in proteins along the carbon chain skeleton are classified as aliphatic, aromatic, and heterocyclic. In turn, aliphatic amino acids, based on the content of amino and carboxyl groups, are divided into monoaminocarboxylic and sulfur-containing amino acids.
It is now known that amino acids found in protein hydrolysates (excluding glycine) are optically active, and typically all have the same α-carbon atom configuration, namely L-configuration. The optical activity of amino acids is denoted by symbols (+) and (-) in round brackets. To standardize the nomenclature of amino acids, a system was proposed according to which uppercase Latin letters L and D are used to denote the configuration of the α-carbon atom. Natural amino acids, which are components of all proteins, as well as those found in free form, belong to the L-series. The physical and chemical properties of D- and L-forms of amino acids are practically the same. It should be noted that D- and L-amino acids can be distinguished by taste, with the former usually being sweet, while the latter are bitter or tasteless. In the production of amino acids, it is often easier to synthesize DL- rather than L-forms of amino acids. Mixtures of natural and unnatural isomers can be separated by chemical or enzymatic means, but this process is very laborious and time-consuming.
It has been established that D-forms of amino acids participate less effectively in metabolism than L-forms. L-amino acids can participate in various metabolic processes, including those not related to their deamination (protein biosynthesis, peptide synthesis, synthesis of various physiologically active compounds).
Protein metabolism scheme.
Main Stages of Protein Metabolism.
First stage. In the gastrointestinal tract, processes of protein breakdown into amino acids occur due to the functioning of enzymatic systems, as well as their further absorption into the blood. Amino acids are transported through the epithelial lining of the intestine and enter the liver through the portal vein, where some of them are retained and transformed, while others are transferred to various organs and tissues. The absorption of amino acids in the intestine is an energy-dependent process that requires ATP.
Second stage. Intermediate metabolism of proteins begins in the liver, where amino acids absorbed in the gastrointestinal tract are delivered. Here, their transformation occurs – deamination, transamination, decarboxylation with the detachment of amino and keto groups involving specific enzymes, and the formation of new amino acids. Nitrogen-free residues of amino acids are used in the synthesis of fats, carbohydrates, and other compounds. During intermediate metabolism, amino acids also form biologically active compounds: amines and gamma-aminobutyric acid during decarboxylation. The initial step in protein biosynthesis is the transport of amino acids from the blood into the cell, where free amino acids form complex compounds with ATP and tRNA and are delivered to the ribosomes. The structural components of the cell ribosomes “sew” amino acids into a specific sequence, forming a primary polypeptide chain. Subsequent intracellular transformations of the polypeptide chain, acquisition of secondary and tertiary structures, and incorporation of non-protein groups determine the final result of protein synthesis – the appearance of a specific protein with a certain molecular weight and characteristic properties.
Third stage. The end products of protein metabolism are carbon dioxide, water, and nitrogenous substances such as urea, uric acid, ammonia, creatinine, hippuric acid, and indican. These products must be excreted from the body or neutralized in subsequent metabolic reactions. For instance, some ammonia is neutralized by forming glutamic acid and glutamine, or converted into a less toxic product – urea. Uric acid, which is the end product of the metabolism of purine bases – adenine and guanine, constituents of nucleic acids, like urea, is excreted from the body through the kidneys. Some amount of ammonia can directly bind in the kidneys, forming ammonium salts.
Regulation of Protein Metabolism.
Somatotropic hormone (somatotropin) – STH, participates in the regulation of protein-synthetic processes. The effects of STH are manifested in the intensification of amino acid transport through cell membranes, stimulation of RNA synthesis in the cell nucleus, and the formation of polysomes, where the synthesis of polypeptide chains occurs.
Insulin – a hormone that directly influences transcription and translation processes, indirectly through intensification of transport processes. On the cell membrane, insulin enhances the transport of amino acids and affects the level of substrates for protein synthesis. Thyroid hormones thyroxine and triiodothyronine affect protein metabolism differently. Normally, the presence of thyroid hormones is necessary for stimulating protein synthesis, organism development, cell differentiation, and tissue formation. If thyroidectomy significantly disrupts growth and development, hyperthyroidism leads to excessive stimulation of oxidative phosphorylation, resulting in rapid “burning” of carbohydrate and lipid metabolites, followed by expenditure of tissue proteins. In this case, the action of thyroid hormones is manifested catabolically.
Sex hormones. Female sex hormones (estrogens) stimulate protein synthesis primarily in tissues and organs closely associated with reproductive function, such as the uterus, ovaries, mammary gland, and vagina. The influence of estrogen on other organs is insignificant. Male sex hormones (androgens) have anabolic effects not only on the reproductive system organs but also on the protein-synthetic activity of skeletal muscles, leading to muscle mass increase.
Among the catabolic hormones, along with thyroid hormones produced during thyroid gland hyperfunction, adrenocorticotropic hormone of the pituitary gland can be attributed, which affects the adrenal cortex, stimulating the synthesis and secretion of glucocorticoids. ACTH causes intensive conversion of tissue proteins into glucose. The action of glucocorticoids is associated with the induction of the synthesis of a number of enzymes that ensure the deamination of amino acids during glucose formation. However, in the liver, glucocorticoids stimulate the synthesis of blood plasma proteins.
Out of the 20 amino acids – constituting parts of feed and tissue proteins, 12 are considered indispensable for birds. They are not synthesized in the bird’s body or synthesized in small quantities. In the absence or deficiency of one or more essential amino acids in the feed, the synthesis of complete proteins in the body becomes impossible, metabolic processes are disrupted, productivity decreases, and the growth of young animals slows down. High poultry productivity can only be maintained by balancing diets based on the amino acid composition. For birds, indispensable amino acids include lysine, methionine, cystine, tryptophan, arginine, histidine. Leucine and isoleucine, phenylalanine, threonine, valine, and for young animals – also glycine are indispensable. When regulating amino acid nutrition for poultry, it is necessary to know its amino acid requirements and the amino acid composition of feeds.
Conclusion
Many scientists have studied the amino acid composition in the blood plasma of birds. In particular, it has been established that in chicks, the amino acid composition of blood largely depends on the protein composition of the diet and the rate of their growth. The observed decrease in the total level of free amino acids in the blood, according to researchers, indicates their active utilization for tissue protein synthesis. A relationship has been established between the amino acid composition of the diet and the amino acid composition of blood plasma.
Research data indicate that fluctuations in the amino acid composition of blood and cells largely depend on the quality of nutrition and the level of metabolism. It should be noted that feed imbalance in terms of amino acid composition adversely affects animal productivity, worsens their physiological condition, and disrupts metabolism, significantly reducing the efficiency of feed utilization.
One of the characteristic signs of amino acid imbalance is a disruption in the normal ratio of free amino acids in the blood. The deficiency of an essential amino acid in the diet usually accompanies a decrease in its content in the blood, leading to a significant increase in the level of other amino acids.
The mechanism of breakdown and excretion of excess amino acids is not strictly specific. In most cases, it is characteristic for a group of amino acids in the body, and both excess and deficient amino acids of the same group are intensively broken down and excreted. For example, when studying the relationship between lysine and arginine metabolism in chicks, it was found that excess lysine is eliminated by excretion through the kidneys, which is associated with a decrease in lysine reabsorption in the renal tubules. Along with lysine, the reabsorption of arginine in the renal tubules decreases, and its excretion with urine increases.
Thus, the use of premixes for broilers Vitamix Premium BR, containing proven availability of all essential amino acids for broiler chicks, tested on experimental farms, allows achieving maximum growth results.
