Enzyme therapy in cosmetology

Galina Krinskaya , cosmetologist, clinical pharmacologist, brand trainer PBSerum, BioRePeelCI3, IBSA

What is enzyme therapy?

Enzyme therapy (syn. enzyme therapy) is the use of enzymes for therapeutic purposes. And since we are considering the use of enzymes in cosmetology, the goals will be both therapeutic and aesthetic.

Enzymes (they are also called enzymes) are substances of protein origin that accelerate (catalyze) biochemical reactions in living systems, without themselves undergoing chemical transformations. Almost every biochemical reaction in a living cell requires the presence of a certain enzyme or will proceed much more slowly if its quantity is insufficient.

Enzymes have existed as long as humanity has existed. And their study began with the study of fermentation processes. The theoretical confrontation between the theories of L. Pasteur and J. Liebig on the nature of alcoholic fermentation led to the appearance of the work of E. Buchner, in which he proved that cell-free yeast juice carries out alcoholic fermentation in the same way as undestroyed yeast cells, for which he received the Nobel Prize. The crystalline enzyme urease was first isolated in 1926 by J. Sumner, and over the next 10 years the protein nature of the enzymes was finally proven.

Mechanism of action of enzymes

Each enzyme, assembled into a specific structure, speeds up the corresponding chemical reaction. An enzyme and a corresponding protein take part in the reaction, and the result is a specific reaction product. Enzymes are specific to their substrates. Enzyme activity can be increased by activators and decreased by inhibitors.

Enzymes are present in all living cells and help convert one substance into another; act as catalysts in almost all biochemical reactions occurring in living organisms. By 2013, more than 5,000 different enzymes had been described. They play a vital role in all life processes, directing and regulating the body’s metabolism.

Like all catalysts, enzymes speed up both forward and reverse reactions, lowering the activation energy of the process. In this case, the chemical equilibrium does not shift either forward or backward. Each enzyme molecule is capable of performing from several thousand to several million “operations” per second.

Moreover, the efficiency of enzymes is much higher than the efficiency of non-protein catalysts: enzymes speed up reactions by millions and billions of times, non-protein catalysts by hundreds and thousands of times. Enzymes are usually named by the type of reaction they catalyze, adding the suffix -ase to the name of the substrate, for example, collagen - collagenAZA.

Classification of enzymes

Based on the type of reactions they catalyze, enzymes are divided into six classes according to the hierarchical classification of enzymes (Enzyme Commission code). The classification was proposed by the International Union of Biochemistry and Molecular Biology.

Oxyreductases , which catalyze electron transfer, that is, oxidation or reduction. Example: catalase , alcohol dehydrogenase .

Transferases that catalyze the transfer of chemical groups from one substrate molecule to another. Among transferases, kinases that transfer a phosphate group, usually from an ATP molecule, are especially distinguished.

Hydrolases that catalyze the hydrolysis of chemical bonds. Example: esterase , pepsin , trypsin , amylase, hyaluronidase.

Lyases that catalyze the breaking of chemical bonds without hydrolysis with the formation of a double bond in one of the products, as well as reverse reactions.

Isomerases , which catalyze structural or geometric changes in a substrate molecule to produce isomeric forms.

Ligases that catalyze the formation of chemical bonds C–C, C–S, C–O and C–N between substrates due to condensation reactions coupled with ATP hydrolysis. Example: ligase .

Translocases , which catalyze the transport of ions or molecules across membranes or their separation in membranes.

Enzyme model

The specificity of enzymes was initially determined by the “key-lock” model (E. Fischer 1890), which is based on the exact correspondence between the shape of the enzyme and the substrate. As a result, a short-acting enzyme-substrate complex is formed. This model explains the high specificity, but does not explain the stabilization of the transition state. In 1958, D. Koshland proposed a modification of the “hand-glove” model. Enzymes are generally not rigid molecules, but flexible molecules. The active site of an enzyme can change conformation after binding a substrate.

The amino acid side groups of the active site assume a position that allows the enzyme to perform its catalytic function. In some cases, the substrate molecule also changes conformation after binding at the active site. Unlike the key-lock model, the induced-fit model explains not only the specificity of enzymes, but also the stabilization of the transition state.

Hydrolytic enzymes, or hydrolases, are widely used in cosmetology. Esterases (lipase) hydrolyze the ester bond. Glycosidases (amylase, hyaluronidase) hydrolyze bonds in sugars. Proteases (trypsin, chymotrypsin) hydrolyze the peptide bond.

Where to look for enzymes?

Enzymes in cosmetology can also be divided into plant, animal, bacterial and recombinant.

Plant enzymes (papain, bromelain, ficin, sorbain, actinidin, arbutin). Contained in berries, fruits, nuts.

Animal enzymes (pepsin, trypsin, chymotrypsin, pancreatin) are obtained from the pancreas of large and small cattle and pigs. Lysozyme is extracted from chicken egg white. Testicular hyaluronidase is extracted from bovine testes.

Bacterial enzymes – subtilisin and travase.

Recombinant enzymes – keratinase, lipase, hyaluronidase, collagenase. Produced from bacterial cultures using genetic modification technologies.