Biological accelerators |
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They are called enzymes. The first pure enzymes isolated in the 30s of the twentieth century in the form of crystals turned out to be proteins, and all obtained later (now there are about two thousand of them) are also special types of proteins. We now know that enzymes are immeasurably superior to artificial catalysts in many ways. First of all, by the strength of the action. Thousands of chemical reactions occur in living organisms with the participation of enzymes without high temperatures and pressures millions and billions of times faster than in the presence of the best chemical catalysts. Enzymes have another advantage - the most important one. They differ from artificial catalysts in the striking rationality of their actions, strictly directed and most effective. Each enzyme works optimally, without looking for "optimal technological solutions", converting only one or a group of closely related compounds. Moreover, it transforms in a strictly defined direction. These are the amazing abilities that enzymes have found. However, knowing a lot about their properties, researchers, even on the threshold of our century, could not answer the question of what they are. True, even then such prominent scientists as I. Pavlov, A. Bach, E. Fischer, F. Hopkins were convinced that the vital activity of any organism, metabolism is nothing more than a set of countless chemical reactions occurring in living cells strictly ordered. And enzymes are the kind of “law enforcement officers” (or rather, its organizers). Hence it is clear what an important role they play in metabolism. And he, in turn, is the basis of all biological functions: nutrition, reproduction, development, heredity, irritability, mobility.
This idea was fully confirmed. Moreover, it turned out that the extremely important organs of cells, associated with the synthesis of proteins, the transfer of substances, cellular respiration, are each built mainly from special enzymatic proteins. In other words, enzymes are placed exactly where they are needed as a subtle instrument of chemical transformation. The reader may ask: is it so important, where is which enzyme is "registered"? The main thing is to know how it works. It turns out that "topography" in this case is extremely important not only for science, but also for practice. After all, enzymes not only speed up reactions.They themselves, in turn, are targeted by the action of most biologically active compounds - vitamins, hormones, antibiotics, medicinal substances and poisons. Do I need to explain what prospects are fraught with the exact definition of the "coordinates" of certain enzymes, and the ability to influence their action. For example, complex organic compounds that attack one of the enzymes essential for the functioning of nerve centers have proven to be a powerful treatment for several severe eye and nervous diseases. Elucidating the structure and functions of enzymes, science is looking for ways of practical control of physiological processes and new ways to protect living organisms from harmful effects.
The unsurpassed selectivity of the action of enzymes makes them invaluable reagents for biochemical analysis - measuring the content of a certain sugar, amino acid, etc. in a complex mixture of similar, related compounds, as well as for the purposes of fine organic synthesis. Thus, the use of enzyme preparations (or microbial cells rich in them) in industry has reduced the cost of such important biochemical preparations as ascorbic acid and steroid hormones many times over. Today, in most of the technically developed countries, specialized enterprises have been created that produce enzyme preparations. These drugs are used in many areas of the light, food and pharmaceutical industries, intensify and reduce the cost of production. For example, their use can increase the nutritional value of feed in animal husbandry. It would seem that the possibilities of using such drugs are endless. But in fact, despite the remarkable catalytic properties of enzymes, their practical use until recently was relatively limited. Cause? The instability of enzymes and the difficulty of separating them from the reaction products. This eliminated the reuse of enzymes and made this method unprofitable in many cases. Recently, these shortcomings have been largely overcome. The method of the so-called immobilization of enzymes helped here. What if an unstable enzyme is attached using strong chemical bonds or by other means to polymeric insoluble carriers of various natures - cellulose derivatives, ion-exchange plastics, porous glasses, organosilicate gels? This principle is somewhat reminiscent of the grafting of southern varieties of apple trees to frost-resistant northern varieties. But, of course, it only reminds me from a distance. Here are different scales, different, much more subtle mechanisms. And the question is quite natural here: are the valuable qualities of enzymes preserved at all after such operations are carried out on them? And it turned out: yes, they are. Moreover, immobilized enzymes, while retaining a significant part of the catalytic activity, in many cases have a significantly increased stability.
It is no coincidence that great hopes are now being pinned on this new branch of research - the so-called "engineering fermentology". It promises to significantly simplify many industries and create fundamentally new ones. Despite the additional costs for the production of immobilized enzymes, the possibility of their repeated use makes the new technology economically justified. Scientists expect that with the use of immobilized enzymes in the future it will be possible to solve a number of complex problems not only of fine organic synthesis, but also of chemical energy, for example, to the creation of biocatalytic systems for fixing atmospheric nitrogen, synthesis of liquid organic fuel from carbon dioxide and natural gas. It goes without saying that the solution of these and other applied problems related to biological catalysis is possible only with a sufficiently high level of fundamental research on the structure and function of enzymes. The chemistry and biochemistry of enzymes are involved in many research institutes and higher educational institutions. Domestic scientists have made a number of major, internationally recognized contributions to this field of science. Man entered into competition with nature in areas that seemed fundamentally inaccessible only yesterday. Mastering the secrets of enzymes, forcing them to serve themselves, to increase their well-being, to protect their health, he writes a new page in the great book of our knowledge about the world. A. Braunstein |
As the legends and folk tales of antiquity testify, people from time immemorial have prepared wine from grape juice, made cheese from sour milk, struck enemies and wild animals with arrows, the tips of which were saturated with deadly poison. Man has observed and used many amazing transformations taking place in living organisms and materials taken from them, such as blood coagulation, ripening (and decomposition) of meat, fish and plant products. But why all this is happening, he could not explain for a long time. It was only at the beginning of the 19th century that active substances causing such transformations were discovered in biological objects.
After all, what are these "mysterious strangers" - enzymes for? It took years of work, reflection, and experimentation before it became clear that in organisms they not only accelerate metabolic reactions, but also serve as important tools for the "working" parts of cells. This was first shown in the 30s of the last century by V. Engelhardt and M. Lyubimova. They found that the muscle contractile protein and the enzyme that releases energy for contraction are identical. Engelhardt suggested that enzymes constitute an essential part of the entire mass of cellular proteins.
Nowadays, more than five hundred congenital metabolic defects in humans are known, the cause of which is a hereditary, genetically determined violation of the synthesis of a certain enzyme. So, for example, the congenital absence of an enzyme that accelerates the last stage of the biosynthesis of the amino acid tyrosine leads to a sharp disruption in the physical and mental development of children. Defects in the formation of certain enzymes of sugar metabolism result in dangerous disturbances in the stability of blood cells.
You understand what can be done if the place of today's catalysts, rather coarse, "inflexible" in comparison with enzymes, are taken in industry, agriculture, medicine by new accelerators and reaction retarders possessing all the best qualities of enzymes, but at the same time the resistance of artificial catalysts. If such “centaurs” are properly “harnessed” into the economy, forced to work for its needs with full dedication, this can lead to a serious increase in production efficiency.
| To the secrets of the living (perspectives of genetics) | Stepan Petrovich Krasheninnikov |
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