What is the principle of complementarity of amino acids, can anyone tell me

There are no enzymes in the digestive system to break down amino acids, so they are not broken down after eating, and are transported to the corresponding cells for transamination or protein synthesis! It is directly used by the human body! It is the principle of complementarity without amino acids!

Proteins in the body's tissues are both constantly broken down into amino acids and synthesized from amino acids provided by food and amino acids broken down by proteins. The degree of physiological activity of each tissue and organ is different, and the rate of protein synthesis and decomposition is also different. Intrahepatic protein metabolism is extremely vigorous, protein is renewed once every 10 days, and muscle protein is renewed once every 80 days.

Normally, protein synthesis and breakdown are always in a dynamic equilibrium.

Due to the different amino acids contained in various foods, the amino acids in several food proteins can make up for each other when reasonably matched with various foods in the daily diet, so that the physiological value of protein can be improved, and this phenomenon is called the complementary effect of protein. For example, eggs and roasted potatoes can achieve a high protein utilization. In order to better play the complementary role of protein, the following three principles can be followed when pairing food:

First, the more varieties of food that are matched, the better, the more varieties, and the more types of amino acids; Second, the farther away the food species are matched, the better, such as the combination between animals and plants, which is more conducive to improving the physiological value of protein than the simple combination of plants; The third is to eat the food at the same time, because the amino acids required by the human body can only form tissue proteins when they reach the body tissues at the same time.

<> Peptide residue slip number number bond number The number of water molecules removed = the number of amino acids (straight chain) The number of peptide chains = the number of amino acids (cyclic peptides).

Contains at least free amino groups orCarboxylNumber = number of peptide chains as first

Contains the number of free amino groups (carboxyl number) The number of peptide chains + the number of amino groups (carboxyl groups) on the R group

ProteinsRelative molecular weightNumber of amino acids Mean relative molecular weight of amino acids (128) Number of water molecules lost 18 - 2 Number of disulfide bonds).

Binding method: The ammonia blind silver group of one amino acid molecule and the carboxyl group of another amino acid molecule are combined to form water at the same time.

What is lost is water.

Method: Dehydration condensation.

Ammonia base acids are linked by peptide bonds to form peptide chains, which are then folded to form proteins with specific spatial structures. Abscisic acid combined with aminamitosic acid affects the activity of proteins. In general, it reduces the activity of the corresponding enzyme in the body, but when the amino acid is separated from the abscisic acid, the activity of the protease can still be restored.

The combination of amino acids is a compound formed by the condensation of two amino acid molecules, called a dipeptide. The hydrogen in the water molecules produced in it comes from amino and carboxyl groups. The way amino acid molecules bind is by the carboxyl group (-COOH) of one amino acid molecule and the amino group (-NH2) of another amino acid molecule, and at the same time remove a molecule of water, this combination method is called dehydration condensation.

The chemical bond (-nh-co-) that connects two amino acid molecules is called a peptide bond. The hydrogen in the water molecules generated comes from amino and carboxyl groups, and so on, and there are multiple amino acid molecules condensed to form compounds containing multiple peptide bonds, which are called polypeptides. Polypeptides usually have a chain-like structure called a peptide chain.

Peptide chains can coil and fold to form protein molecules with a certain spatial structure. Many protein molecules contain several peptide chains that are bound together by a chemical bond. These peptide bonds are not straight and are not in the same plane, forming a more complex spatial structure.

Proline is special in that it does not have a free -amino group. During dehydration condensation, although two H atoms and one O atom are also removed, there is no -NH- in the peptide bond formed, and its N atom is not directly connected to the H atom, but to three C atoms. For example, insulin is a protein that contains two peptide chains.

The chemical bond that connects two amino acid molecules is called a peptide bond. A compound made by the condensation of two amino acid molecules, called a dipeptide (containing a peptide bond). By analogy, compounds that are formed by the condensation of multiple amino acid molecules and contain multiple peptide bonds are called polypeptides.

In the cell, the number of each amino acid is hundreds of hundreds, when amino acids form peptide chains, the order of different types of amino acids is ever-changing, the coiling, folding methods and the spatial structure formed by peptide chains are very different, therefore, the structure of protein molecules is extremely diverse. This is the reason why there are so many types of proteins in cells.

The mutual combination of amino acids, that is, the dehydration and condensation of amino acids, is the removal of a molecule of water between two amino acid molecules, and the remaining part together forms a condensation reaction of compounds, and the compounds formed are called dipeptides. The water molecules formed are derived from the amino and carboxyl groups in the two amino acid molecules, respectively. The newly formed chemical bonds in a dipeptide are called "peptide bonds".

In this way, many amino acids, in a certain type and order, can be linked into a very long macromolecular compound, called a polypeptide or peptide chain. Peptides are modified by enzymes, twisted and coiled, and become macromolecular clusters with specific functions, which are certain proteins. The dehydration condensation reaction of amino acid dehydration condensation is the basis of protein formation.

The way amino acid molecules combine with each other is: dehydration and condensation. The carboxyl group of one amino acid molecule is attached to the amino group (-NH2) of another amino acid molecule.

At the same time, a molecule of water is removed. This type of bonding is called dehydration condensation. The chemical bond that binds two amino acid molecules together is called a peptide bond.

The structure of the peptide bond is: -nh-co- (or) method to dial the calculation problem with the protein. Just remember the following two equations:

1) Number of peptide bonds = number of water loss = number of amino acids - number of peptide chains, (2) molecular weight of protein = number of amino acids average molecular weight of amino acids - 18 number of water loss. You can also refer to the following table: number of amino acids, number of peptide bonds, number of dehydrated molecules, number of amino acids, number of carboxyl bases, one peptide chain nn-1n-1, at least 1 at least 1 m peptide chain, nn-mn-m at least m, at least m when calculating the number of amino and carboxyl groups contained in the peptide molecule.

The number of amino and carboxyl groups in the R group needs to be added. The formula for calculating the relative molecular weight of proteins is: n·a-(n-m)·18 (where n is the total number of amino acids.

a is the average relative molecular weight of amino acids. m is the number of peptide chains).

1) The complementary effect of protein refers to the mixing of two or more protein foods with different amino acid limits, which can learn from each other's strengths and weaknesses, improve the proportion of amino acids, and improve the nutritional value of protein. Generally speaking, although the nutritional value of most plant proteins is very low, due to the different amino acid composition ratios of various food proteins, they still have their own advantages and disadvantages from the perspective of nutritional value. For example, the general legume protein lacks sulfur-containing spine amino acids, but is rich in lysine, while most cereal proteins are the opposite, the above two foods can be mixed to eat, can improve the protein utilization rate by 10% 30%, the complementary effect of different proteins is actually the result of the complementary amino acid components contained in each other.

Chinese folk have long had the habit of mixed food, such as heterozygous noodles (cornmeal and bean noodles), laba porridge (rice, millet, sorghum rice, soybeans, adzuki beans, dates, etc.) all have the advantages of protein complementarity.

2) The following principles should be followed when using the principle of protein complementation for protein complementation:

The more variety of food, the better. Advocate a diversified diet, and the more varieties of food that are paired with land, the better the complementary effect of protein.

The farther away the food species, the better. The combination of animal and plant foods is more conducive to improving the biological value of protein than the combination of plant foods alone. Because some plant foods limit the same amino acids, the complementary effect of protein is not obvious, and when the food species is far away, the amino acid composition of food protein is quite different, which is conducive to the mutual complementarity of amino acid composition.

Serve at the same time. Because amino acids are easily degraded in the body and cannot be stored, if the uptake time is long (more than 5 hours), their complementary effect will be affected.

In a certain protein, there is a deficiency or insufficient quantity of one or several essential amino acids, resulting in the inconsistency of the ratio between essential amino acids, affecting the utilization of protein by the human body, limiting the nutritional value of this protein, and the lack or insufficient amount of amino acids is called limiting amino acids. It is divided into sections according to the degree of amino acid deficiency in a certain food.

I. Second ......Limit amino acids. If the cereal protein contains the least lysine, followed by phenylalanine, then lysine is the first limiting amino acid and phenylalanine is the second limiting amino acid of cereal protein. Legumes contain the least amount of methionine in protein, and methionine is the first limiting amino acid for legume protein.

Mixing the above two foods or a variety of foods, because the types and quantities of ammonyl acid complement each other, improve the biological value of the white matter of the egg, this phenomenon is called the complementary effect of Xiangyu protein.

First of all, you need to know the concept of ideal protein, which means that the amino acids of this protein are consistent with the composition and proportion of amino acids of the protein required by animals, including the composition and proportion between essential amino acids and between essential amino acids and non-essential amino acids, and the utilization rate of this protein by animals should be 100%.

However, there is no balance between the proportions of various AAs in general protein raw materials. The lowest amount of AA reduces the overall protein utilization level, which is known as restrictive AA. At this time, we need to add another protein raw material containing this AA.

The ratio between the various AAs should be as good as possible to meet the requirements of the ideal protein.

In this way, the utilization rate of several proteins used together is much higher than that of a single protein.

The complementary role of protein The content and composition ratio of various amino acids in plant-based proteins are always somewhat insufficient compared with the needs of the human body. Since the amino acid content and composition of various plant proteins are different, they can be matched with plant foods to complement each other's strengths and weaknesses to make them close to the needs of the human body and improve their nutritional value. The effect of this food combination is called the complementary effect of protein.

In practice, we often mix multiple foods, and now we know that this not only modifies the taste, but also conforms to the principles of nutritional science. For example, rice is deficient in lysine, soy protein is rich in lysine and relatively insufficient in tryptophan, and corn is rich in tryptophan.

When soybean, corn and rice are eaten separately, the biovalue of their protein is respectively, but when the three are mixed and eaten in the ratio of 20%:40%:40%, the biological value of their protein can be increased to 73%, which is equivalent to * meat.

This greatly improves the utilization rate of protein and avoids the adverse effects of eating more meat, such as excessive cholesterol and fat intake. Therefore, in our daily life, we should pay attention to the complementary effects of proteins to improve the quality of life. Three Principles of Protein Complementation:

1.Food biology species are as distant as possible 2The more types of combinations, the better 3