4.1 A Question Answered
“Wouldn’t it be wonderful if our scientists could come up with a substance which could assure digestion of our foods, clean our dirty sores, reduce inflammations, promote healing, liquefy the thick mucous discharges emanating from our many diverse serous and other membranes within the body cavity; in short, work all manner of miracles?” Well, they haven’t, but Nature has! In fact, Nature has produced a whole family of such miracle workers and they are known as enzymes.
The human organism contains countless millions of enzymes. They are contained in the food we eat and in every cell of the body. Enzymes are very specialized organic compounds of polymers of amino acids. A polymer is a larger molecule or compound formed by the union of two or more smaller identical molecules. Enzymes are formulated when two or more identical amino acids are united in a chemical union.
Polymers are never found in the inorganic world. Therefore, enzymes are found only in living plants and animals. They are proteinaceous catalysts of biological activities. Since this statement is quite a mouthful, let us probe a little further to get a greater understanding of the specific role played by enzymes.
4.2 A Catalyst
The word catalyst is defined in the Thorndyke-Barnhart Advanced Junior Dictionary as “a substance that causes catalysis” with catalysis then being interpreted to mean “the causing or speeding up of a chemical reaction by the presence of a substance that itself remains practically unchanged,” this last in our frame of reference referring, of course, to an enzyme.
The New American Encyclopedia (1939 Revised Edition) defines catalysis as a “chemical process by which the reaction of substances is quickened by an added substance which does not itself undergo a change. The added substance is called a catalytic agent or a catalyst. An example is platinum, the catalyst used in mfg. sulphuric acid.”
4.3 Enzymes as Catalysts
Enzymes serve as catalysts to metabolic activity. They act to assist the speed of the many chemical actions and reactions involved in the metabolic process and also help these activities to be brought to a successful conclusion. As catalysts, enzymes are capable of increasing the rate and effectiveness of a reaction without being consumed in the process.
Many of the processes which go on in the human body at normal temperatures would require in a laboratory situation hundreds and even perhaps thousands of degrees of temperature and perhaps even the presence of a strong violent reagent for their accomplishment. These same reactions are accomplished by means of the enzymatic presence almost instantaneously in the calm peaceful environment of a healthy body.
4.4 Classifying Enzymes
Enzymes come in many sizes and vary as to their specific duties. At present over 700 different enzymes have been identified but so many millions of these miracle workers are known to exist that they have simply been grouped in three general categories, as follows:
- hydrolytic (water-absorbing);
- oxidizing (uniting with oxygen to supply heat and/or energy; as in a combustion);
- Reducing (subtracting from a particular complex molecule certain elements, groups of elements or electrical charge).
These names are applied according to the type of process the enzymes control.
Individual enzymes are named by adding “ase” to the name of the substance on which they work, scientifically referred to as the substrate as, for example, the starch-digesting enzyme ptyalin or amylase. Trypsin is sometimes referred to as Trypsinogenase or proteinase because it assists in the resolution of protein (splitting the complex protein molecule into smaller chemical units or molecules). Lactase assists in the resolution of lactose, or milk sugar. And so on.
4.5 Enzyme Activation
Most enzymes actually exist in an inactive form until such time as their catalytic talents are called upon by the organisms. It is interesting in light of the fact that many people are taking enzymes regularly as supplements to realize that, in order to initiate the action by an enzyme, that is, to activate it, some metal ion (an electrically charged particle) or some simpler organic molecule or co-enzyme(s) must also be present.
As we have previously noted, vitamins serve as activators as well as regulators. They can serve as activators of enzymes and, at the same time, as regulators of enzymatic activity; again, a very good example of synergism within the system and, also, a very good reason taking isolated enzyme factors may be disruptive of normal enzymatic activity causing fluctuations of precise temperature ranges necessary to conclude successfully an important metabolic process.
Enzymes act only within very limited temperature ranges, this being true also of catalysts used in certain laboratory situations and industrial processes. At about 94 degrees, food enzymes start to lose their effectiveness, their ability to fulfill their catalytic duties and at about 118 degrees, they are no longer of any use. At the other end of the scale, they start to become inactive at about 32 degrees and seem to be totally destroyed at minus 104 degrees Fahrenheit. Thus it is that baking, boiling, frying, stewing, roasting, heating of any kind, dehydrating and freezing will either reduce or completely destroy the enzymatic presence in food.
When it became known that some enzymes were contained in food and that they probably helped in the digestion thereof, many people began talking about “live” food, but this was a misnomer since enzymes are in no sense “alive,” as we think of the meaning of this word. However, the concept of “life” in food led to many foolish ideas and fads in eating, some persons going so far as to eat nothing except what they were able to pull off a tree or pick from a vine or bush and pop immediately into their mouths, as if to catch the life element before it escaped. By this practice they hoped to live forever.
Certain supplement-happy practitioners go so far as to have blood tests made in order to evaluate the adequacy of pancreatic enzyme production, the same pancreatic enzyme which functions in the disorganization of carbohydrates in the small intestine. Since some of these enzymes are known to be absorbed from the GI tract into the blood stream, it is postulated that we can assess the amount of enzyme production by noting their presence in the blood.
Other methods are also used, such as the indican test which measures the amount of unused breakdown
products which result in the absence of sufficient pancreatic enzyme to digest protein, these being directed to and collected in the urine. When such deficiencies are found to exist, supplements of pancreatic enzymes and perhaps even of hydrochloric acid are given to correct the situation instead of either reducing drastically the protein intake of the patient to one more in balance with normal enzyme production or fasting him to remove the toxic wastes that now burden his body preventing efficiency of production at the cellular level, a condition which probably exists throughout the body. In other words, an attempt to restore the enervated system to a condition capable of more efficient production on all levels, including the synthesis and utilization of enzymes, would be a more sensible way to approach the problem.
The enzyme ribonuclease was first discovered in 1938 by the bacteriologist Rene Dubos. (Ribonuclease acts as a catalyst in the hydrolysis of ribonucleic acid.) Eight years later Moses Kunitz, an American chemist, isolated this same enzyme and 23 years after that, in 1969, by two teams of researchers from Merck, Sharp and Dohme, the pharmaceutical company, and from Rockefeller University, this enzyme was finally synthesized. Since that time research has continued in many areas with the hope that enzymes can be manufactured and adminstered in the form of pills or by injection as agents in the prevention of disease or as a curative agent should disease exist.
Researchers are persistent. They have been hard at work learning about the chemistry of enzymes and how they work, trying to solve the mystery of how they can accomplish so much at such low temperatures. There is no doubt that much will be revealed in future years but, to date, we work on the fringes and have failed to solve the mystery.
4.7 Other Roles
Enzymes not only help to affect the marvelous processes of life but they also assist in death. Every minute millions of our body cells conclude their duties and die. Whenever cells die within the living body, they must be disposed of very quickly else the metabolic processes might soon be overwhelmed by the dead and dying cells and all life would necessarily come to a halt. This is where enzymes function in another capacity.
The dead cells are immediately set upon by the enzymes assigned to this specific type of cleanup duty. They are lysosomes. They disintegrate the clutter before it can obstruct normal function. Interestingly enough, there are no enzymes other than rigidly controlled lysosomes that can digest a living cell! Since enzymes lack this power, life is protected from destructive catalytic action and living cells just go on about their business.
Enzymes usually work at their point of synthesis within the cell where they are formulated. Their chief duty appears to be the building of proteins which are suitable for the particular host cell where they reside. Man is truly “fearsomely and wondrously made.” And we labor under the delusion that supplementary enzymes can substitute for innate intelligence.