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Egg white is the common name for naming the clear liquid inside the egg. Egg whites are surrounded by impregnated, non-fertile egg yolks. Whiteness is necessary to protect the yolk, as well as nutrition and growth of the embryo. 90% of the egg is composed of water and 10% contains proteins such as albumin. Unlike yolks that are rich in lipid or fat, egg white is almost free of fat and carbohydrate accounts for less than 1% of it. Egg whites are used in many foods such as mice, and there are many other uses like making a vaccine.
Although egg white is considered as a low-fat source, and has high protein in nutrition, a percentage of people are not able to eat it. Eggs are one of the most common causes of food allergies. Eggs are made from various proteins, some of which are susceptible. Most people with egg allergy react to proteins in egg whites, and others are allergic to yolk.
Egg white is one of the best quality protein sources to make muscle tissue of interest to bodybuilders and is also a rich source of vitamins.
Bodybuilders who do not use egg whites in their diet will actually lose sight of their excellent status, since egg whites are rich in pure protein, low in carbohydrates, fat and cholesterol. Is.
The egg white protein is easily absorbed into the muscle and each yolk whites contain about 3.6 grams of pure protein containing all of the 8 essential amino acids required for the body including valine, leucine, isoleucine, lysine, methionine, phenylalanine , Threonine and tryptophan, and vitamins A, E, K, B12, riboflavin and folic acid are also found in abundance in egg whites that play a major role in muscle building.
The benefits to bodybuilders include only egg whites, and it's best to avoid eating yolk while taking it.
Biochemical Properties of White:
The liquid albumin is a clear, thick liquid that fills all the spaces located between the membranes of the shell and yolk. Egg white or egg albumin contains approximately 60% of the total egg weight, 78% of which is made up of water, and the remainder consists of albuminous substances, the most important of which is α-albumin.
Immediately after the egg is released by the bird, albumin has a jelly-like structure. But this jelly is gradually converted into liquid.
The egg white egg pH is about 4.7 and increases to 9 over a period of about 3 days, and then changes slightly, and this increase leads to harmful results.
In dry matter, egg white has about 85 percent protein, the most important of which are:
Ovalbumin:
This protein forms 60% of the total white protein and is similar to the serum albumin present in the blood plasma and can be compared with this compound. It has been found in blood of laying hens. However, α-albumin is not a pure protein; in fact, it is a phosphoprotein. It should be noted that α-albumin has some mannose and glucosamine in each individual unit, but it lacks noraminic acid. In terms of amino acid composition, it has a very good balance. Acid glutamate is present in excess of 10%, and other amino acids are also found to be less in it. It has gelatinous properties. These properties and properties depend on the protein state, so that the higher the amount of S-alpha-albumin increases, this property is reduced.
Conalbumin:
Conalbumin is also referred to as ototransferin. Its molecular mass is roughly twice the molecular mass of α-albumin. It is similar in amino acid composition and its ability to combine with bivalent cations close to that of sydurophilin (the blood serum glycosartin beta group). The difference is in carbohydrates and does not contain noraminic acid and consists of equal parts of mannose and glenalbumin. This protein has a deterrent effect on certain bacteria.
Compared with ovalbumin, cannabumbene makes it easier and more readily replaced by the heat of molecular building, and coagulates at about 63 ° C. This is almost the temperature that the egg white coals at that level because it finds a gelatine or quasi-solid state at the point where the insoluble canalubin is present.
Ovomucoid:
Oumocoids are a glucose-rich glucosamine protein of about 14%. It also contains 7% mannose and a portion of galactose and some nitaminic acid. The connection between these monosaccharides is carried out by a peptide chain on asparagine. This protein is comparable to the two previous compounds, namely, α-albumin and con can-bubble, with 13% nitrogen but 2% sulfur. This compound is easily removed from other egg white proteins due to its solubility properties in trichloroacetic acid.
Oumocoids, due to the heat, change the molecular structure of the molecule, although it has much greater resistance than ovalbumin and cannabumbina.
Oumocoids have biological activity and this is due to the antitrypsin agent.
The hardened coagulated white egg is digested quickly in the intestine because its molecular structure has been changed. In contrast, raw egg whites are partially resistant to the digestive process.
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