Can alcohol denature protein?

Protein is an essential substance in the human body. Protein is very important for human health. There are many foods in life that contain protein. Regular consumption of foods with high protein content has many benefits for human health. However, protein is very easy to denature in life. If not handled properly, protein will lose its original activity and will not be digested and absorbed by the human body.

Can alcohol denature proteins?

Alcohol can deform proteins because its structure contains -OH, which has similar and compatible properties. It can combine with the groups of proteins and thus change the properties of proteins.

Denaturation of proteins

Protein denaturation refers to the destruction of the specific spatial conformation of a protein under the action of certain physical and chemical factors such as heat, organic solvents, heavy metal ions, and bioalkali reagents, that is, the ordered spatial structure becomes a disordered spatial structure, which leads to changes in its physical and chemical properties and loss of biological activity. Denaturation does not change the primary structure of the protein, only the secondary, tertiary and quaternary structures, that is, the higher-level structures, change.

What can cause degeneration?

Protein precipitation with heavy metal salts

Proteins can combine with heavy metal ions such as mercury, lead, copper, silver, etc. to form salt precipitation. The precipitation conditions should be slightly higher than the isoelectric point. Because at this time the protein molecules have more negative ions that are easy to combine with heavy metal ions to form salts. Proteins precipitated by heavy metals are often denatured, but if under low temperature conditions and the concentration of heavy metal ions is controlled, they can also be used to separate and prepare non-denatured proteins.

In clinical practice, the property of protein to bind to heavy metal salts is used to rescue patients who have been poisoned by accidentally ingesting heavy metal salts. The patients are given a large amount of protein orally, and then emetics are used to make them vomit out the bound heavy metal salts to detoxify.

Protein precipitation with organic solvents

Organic solvents that can be mixed with water, such as alcohol, methanol, acetone, etc., have a strong affinity for water and can destroy the hydration membrane of protein particles, causing protein precipitation at the isoelectric point. At room temperature, precipitation of proteins by organic solvents often causes denaturation. This is the case with alcohol disinfection and sterilization, for example. However, at low temperatures, denaturation proceeds more slowly and can be used to separate and prepare various plasma proteins.

Heating and solidification

Heating a protein solution close to its isoelectric point can cause the protein to coagulate and precipitate. Heating first denatures the protein. The regular peptide chain structure is opened up to become a loose, irregular structure, the asymmetry of the molecules increases, and the hydrophobic groups are exposed, which then condense into gelatinous protein masses. For example, in a cooked egg, both the yolk and the egg white coagulate.

Characteristics of Transgender

The most important characteristic of denatured protein is the loss of its biological activity, such as the disappearance of the catalytic function of the enzyme and the change of the immune properties of the protein; in addition, the physical and chemical properties are changed, such as the solubility is decreased; the biochemical properties are changed, the peptide bonds are exposed, the sensitivity to the enzyme is increased, and it is easy to be hydrolyzed by proteases.