The second natural electromagnetic field which is known on earth is the one found in most living organisms. The human body also produces a field which is extremely weak and could hardly be measured. Nerve impulses are electrical messages caused by an action potential across the nerve membrane. The movement of a muscle by the action of a nerve also requires a complex movement of ions, and consequently an electric current. Cell division has now been discovered to be electrical and so is the heartbeat. The initiation of wound healing and bone growth is electrically stimulated. In fact all chemical changes are electrically based because they involve the transfer, sharing, or alteration of electrons at the molecular level. All of this electrical activity in the human body is therefore producing an electromagnetic field which could easily be disturbed by an external field acting on the body. A wide range of frequencies, according to recent experiments, caused numerous behavior problems, such as depression, anxiety and confusion. Also according to some tests on humans, we absorb energy most efficiently at around 85 megahertz, which is the frequency range used by many FM devices, but we resonate, and therefore respond as an antenna, right in the middle of the ultra high frequencies or television band. In some experiments, weak extremely low frequencies fields were found to affect a specific enzyme needed for the synthesis of melatonin, a very important hormone which is also needed in the production of seratonin, an essential neurotransmitter to the nervous system. Another enzyme on which they did some research was ODC (ornithine decarboxylase). This enzyme is always present during cell growth, but increased levels of ODC are considered a marker for the kind of increased cell activity common in cancers. It has been found that EMFs at 60 hertz turned on ODC production when combined with certain chemicals known to be carcinogenic. Blake Levitt, in her book “Electromagnetic Fields”, dedicates a chapter to the secret electrical life of cells and in the introductory paragraph states the fact that cells are packed with highly charged atoms and molecules that can change their orientation and movement when exposed to certain electromagnetic fields. This concept makes sense when it is said that an electromagnetic field will induce an electric field in the human body which will be polarized and will have a positive and negative end. Therefore in a cell any positive ions will be probably attracted to the negative pole of the field and the negative ions to the positive side. The causes of this would probably be determined by how strong the induced electric field is and how powerful the electromagnetic field itself is. If it is in fact strong enough the ions will be able to move in the direction of their opposing charge. When an ion is exposed to a steady magnetic field, it causes it to move in a circular orbit at a right angle to the field, this is probably caused by the electric field which is being produce by the magnetic field. This occurrence is called cyclotron resonance. The speed of the orbit is determined by the charge and mass of the ion and the strength of the magnetic field. If an electric field is added that oscillates at exactly the same frequency and it is also at a right angle to the magnetic field, energy will be transferred from the electric field to the ion, causing it to move faster. The same effect can be created by applying an additional magnetic field parallel to the constant magnetic field. This is important because the earth already provides a steady-state magnetic field of between 0.2 and 0.6 gauss. The frequency, which is then required to produce cyclotron resonance in some important ions in the human body, falls within the ELF (extremely low frequency) regions, between 1 and 100 hertz. This is the frequency range of all our electric appliances in the 50-60 hertz range. It is also important to mention that this kind of resonance is frequency dependent, and not based on power. Also these effects would only be temporary and would disappear after the electromagnetic field is gone.
All of the effects which were described above are non-thermal effects which electromagnetic fields are thought to cause. These are in fact the consequences that are being discussed on whether they exist. Electromagnetic fields, though, are known to cause thermal effects. In fact, since they are a form of energy, any object which will absorb one of these fields, it will absorb this energy as thermal energy, therefore as heat which will raise its temperature. This increase in temperature will probably depend on the strength of the field. Thermal effects though aren’t a large threat to organisms, first because they are temporary, in fact, when the object’s exposure to the EMF is terminated the temperature falls back down. Secondly the increase is only of few degrees and also any exposure limits passed by governments are based on these thermal effects, so there is no danger they could be harmful to humans.
Because this research paper will focus on the effects of EMF on enzymes, in the next few paragraphs they will be introduced so that a more educated prediction on the outcomes of the experiment will be made. Enzymes are known to be the human body’s catalysts, in fact, they are protein-like molecules whose function is to speed up chemical processes which go on in organisms. A cell itself contains hundreds of different enzymes, each of them has a specific function and each one has a specific reaction to catalyze. A cell will produce two kind of enzymes: one type which will be used inside of the cell in its vital reactions (protein synthesis, cell respiration, etc…), also it will produce other enzymes which will act on reactions taking place outside the cell. Usually all cells produce the same type one enzymes, but they will not all produce the same type two enzymes, this will depend on the function and the specialization of the cell. Enzymes are genetically controlled and therefore each cell has a certain gene which codes for a specific enzyme. To produce the enzyme the cell uses the same process it uses to create proteins, protein synthesis, after all enzymes are protein with a tertiary structure, which go on to specify and become catalysts. Enzymes, just as proteins, are composed of amino acids which are smaller molecules whose basic structure is as following:
R
|
H2N C COOH
|
H
The amino group consists of the H2N, while the acid group is the COOH.
R is the variable group, the side chain that will specialize the amino acid. For example the amino acid alanine has an R group of CH3. Even though there are thousands of enzymes and proteins in the human body, there are only 20 kinds of amino acids and therefore 20 different R groups. These side chains vary in size, shape, electrical charge, bonding capacity and chemical reactivity. They also hold an extreme importance because both the structure and the mechanism of catalysis will ultimately depend on the specific biochemical properties of the amino acid R group. Also what will distinguish a protein or enzyme from one another, is the sequence of amino acids and how they interact with each other to form different structures and give the molecules different properties. For example many proteins are used as channels found in a cell’s membrane, these are used for active transport of substances which are either too big to diffuse through the membrane and for ions which also need assistance in entering the cell because of their charge. A protein which is used in the transport of, for example, positive potassium ions, will be formed so that its negative charged amino acids will be facing the inner walls of the channel protein. This will stop any repulsion between the ions and the walls of the proteins through which the particles will move through, instead it will produce an attraction between the two which may facilitate the movement. The interaction between different amino acids will also create bonds which will be essential for an enzyme and or a protein. Two amino acids containing a sulfur atom in their R groups will be able to create a sulfur bridge, a quite strong bond which will ensure the enzyme’s strength. While two amino acids with a hydroxyl group will be able to form a hydrogen bond, which, even though it is more weak, it contributes to the strength but also give flexibility to the molecule. Then other interactions will produce ionic and covalent bonds which are also very important to the enzyme.
Most reactions in our body naturally take place even without the help of catalysts. Yet they would normally require an enormous amount of time which we don’t have, to speed up these reactions the body would have to raise its temperature to values which would not support life. This is why enzymes play a key role in our body, they allow these reactions to take place in a small amount of time and do not need any other input of energy such as heat. The key to their function as catalysts holds in their structure, in fact even the slightest change of it will jeopardize the ability of functioning of the molecule. This property, given to enzymes, comes from the fact that they can lower the activation energy of the reaction they are catalyzing. In fact any enzyme contains an active site, that part on the molecule at which the chemical reaction usually takes place. Usually the molecule itself, being made up of an extremely long and complex amino acid chain, is usually larger than the substrates, therefore the active sit, we can imagine, is confined to a small area. Also only few amino acids will be in direct physical contact with the actual reaction, these, though, will play a crucial role. They will hold the substrates in a lock and key configuration with the enzyme, and, ultimately, promote the chemical changes that occur in the substrates. The activation energy of a reaction is the amount of energy needed to start a certain reaction, for example in some reactions it may be heat energy, any kind of energy which can be transferred to the substrates’ particles as kinetic energy, or movement energy. In fact an increase in kinetic energy would mean that the particles, of say two different substrates, are moving at a faster speed this will cause them to have a greater chance of collision with each other and therefore of reacting together. While an enzyme is able to reduce this quantity of energy needed to begin the process by bringing the two substrates into contact with each other. By doing this the particles do not need to increase their kinetic energy to start up the reaction but since they are physically in contact with each other the reaction will spontaneously take place immediately without any additional energy. In most reactions, in fact, the body’s own constant temperature, 37C, will give the particles enough kinetic energy to begin reacting when brought in the active site. The effectiveness of the site can be understood by taking a look at the way it works. In fact the substrates physically fit perfectly in their enzyme’s active site, creating an enzyme-substrate complex, the reaction then takes place, and the resulting substances are released. This is the famous lock and key method which works just like a key which perfectly fits in its lock. And this brings up the second importance of an enzyme having an active site. This site also helps the enzyme to be specific and unique to the body. Each enzyme catalyzes a different reaction with different substrates and will have a different active site which has a specific shape complementary to the substrates’ form. An enzyme will be restricted to act on certain molecules, any other substance will not fit in the active site and wouldn’t be able to react. This gives the body more control over which reactions will take place. In fact by reducing the production of a certain enzyme, the body is also reducing the speed of a certain reaction, while by producing more catalysts the process will obviously speed up. Enzyme-controlled reactions usually occur in steps which make up a metabolic pathway, this makes them easier to be controlled. To resume, the ways an enzyme lowers the activation energy and therefore allows reactions to take place in a reasonable amount of time with no need of an extra energy input, are by:
1 Bringing substrate molecules closer together to aid reaction
2 Stresses bonds which need to be broken in order to form the new products
3 Active site of enzyme increases surface area for reaction to take place
4 Orientates substrate molecules in more efficient ways for reaction to occur.
It is also important to note that the lock and key model has been replaced with a newer more accurate one called the induced fit model. The lock and key model is a very stiff one where the molecules are rigid structures with complementary shapes. The new theory gives the molecules a bit more flexibility. The enzyme’s active site, in fact, has been proven to be able to slightly mold or shape itself around the substrate. Of course the site is still specific to one specific reaction, and will not be able to mold itself around another substrate on which the enzyme isn’t supposed to act. Like any other catalyst, a very important property of these molecules is the fact that they are not destroyed by the reaction on which it is acting, the enzyme will remain intact after the process is over and the body will be able to reuse the molecule to catalyze that reaction another time. Because they depend so much on their shape, enzymes are very fragile molecules, even the slightest change in their structure may interfere with their efficiency, they are very sensible to factors which could alter the bonds which keeps the molecule’s shape such as temperature and pH. In terms of temperature we would assume that an increase of it would only aid the reaction and so the enzyme’s function because it would increase the substrates’ kinetic energy making the reaction faster. This statement is partially true, in fact, this does happen the reaction rate does increase with a raise in temperature until a peak called the optimum temperature, at this point the reaction rate is at its greatest speed. We can imagine that this optimum value changes for each reaction and enzyme. As any experimental results would show, after the optimum temperature the reaction rate sharply decreases. In fact the high temperature will denature the enzyme molecule, this means that the hydrogen bonds, one of the links which hold the molecule together, are broken. This will cause the structure and the shape of the enzyme to change, the active site where the reaction occurs will also change shape and ultimately the substrates will not be able to fit in the site and the reaction will slow down. A similar thing happens with pH, there is an optimum pH value at which the reaction will be at its greatest speed and then after that the enzyme denatures and the reaction rate decreases. Most enzymes will function their best at a pH of 7 but some, such as those which are situated in the stomach and work in a more acidic environment, will have an optimum pH value of 2 or 3.
This experiment will study four enzymes: catalase, bromalain, papain, actinidin. Catalase is a molecule found in a number of human organs and tissues, including the liver, where its job is to speed up the decomposition of hydrogen peroxide ( H2O2) into oxygen and water: 2H2O2 2H2O + O2
Hydrogen peroxide is a toxic by-product of metabolism, and its rapid conversion to water removes its toxicity. Bromalain, is found in the pineapple fruit, its function in the actual fruit is not known, but it has been discovered that this enzyme is able to brake the protein found in gelatin collagen which is a fibrous protein found also in bones, cartilage, tendons, ligaments, connective tissue, and skin. The other two enzymes, papain and actinidin are also found in fruits, the first one in papaya and the other in the kiwi fruit. Both of them have also been found to break up collagen. All of these enzymes were chosen because of their easy availability, in fact all of the fruits can be bought and liver can be also found in any grocery store. To create an electromagnetic field a CB radio was used. This is very much like a walkie-talkie which is able to work over longer distances, and is therefore more powerful. Most CB radios have more than one channel over which they can transmit or receive, the one used had in fact 12 channel, or frequencies. They use radio frequencies in the medium to high range. For this experiment the most powerful EMF transmitter was chosen, the most powerful would have been marine radios which can transmit over 25 W, but these are illegal to use on land, therefore the next most powerful transmitter would have been citizen band radios which use 5W. To make a prediction for this experiment may be complicated since no other results have ever been published on this topic. What is the most probable thing which will happen is that the reactions will not be effected by the electromagnetic field to which they will be exposed. What exactly is going to happen and what the exact results are going to be is not known, but an educated guess can be made. Any factor which would disrupt enzyme activity would probably have to change it’s structure so that its shape would also be altered and its active site would loose the complementary shape which it had to the substrates which wont be able to fit, the reaction will so slow down. An electromagnetic field will probably induce a magnetic and electric field on the enzyme. The effects of this on the molecule will probably depend on the strength of the fields. If the electric field is strong enough, as said before, it will be able to attract to itself amino acids contained in the enzymes which have different charges. This may result in a drastic shift of the amino acid chain and ultimately a breakage of the peptide bonds which hold them together, this will lead to a change of in the structure. What it is most probable to happen is that the induced electric field will not be strong enough to cause such a movement of the amino acids, but the amino acids, and therefore the enzyme itself, will orientate so that the different charges are facing toward their opposite pole. This will probably not cause any alterations in the enzyme’s shape or active site and the reaction will still be able to take place. If the EMF is able to orientate the enzyme, it will also be able to change the substrate molecules’ orientation. If the two molecules end up facing opposite ways they may not be able to form an enzyme-substrate complex and the reaction may not take place.
VARIABLES:
The independent variable, in this experiment will be the presence of an electromagnetic field which would act on the enzyme. The dependent variable would therefore be the speed of the reaction rate with and without an EMF, this will be measured by the amount of product produced over the amount of time taken. A few other factors need to be taken in consideration so that the two independent and dependent variables can be controlled. One of these factors would be temperature. To make a fair comparison we are going to have to keep all of the experiments with the gelatin and the fruit enzymes in the same temperature throughout the whole reactions. The two experiments with catalase should also be carried out at the same temperature. This will make sure that the molecules in the experiments regarding the same enzyme will have the same kinetic energy, and therefore temperature wont be a factor influencing the reaction rates. Another factor which needs to be controlled would be the quantities used for the reactions. To produce accurate results it is important to use the same amount of enzyme and substrate for both experiments with and without the presence of an electromagnetic field. By doing this we will be sure that none of the two experiments will be advantaged by the fact that they have more enzyme molecules and their reaction rate will be faster. If the quantities used are controlled, the surface area should be too. If the two experiments use the same amount of enzyme, but in one of them, for example, the bromalain is found on only one piece of pineapple, while in the other four pieces of pineapple are reacted with gelatin, common sense will tell us that the second experiment will have a faster rate of reaction since there is a greater surface area over which the reaction can take place. This will therefore alter the results. Also all of the experiments should be carried out as far as possible from any possible electromagnetic interference, especially the reactions which should not be exposed to an EMF should be far from any electric appliance or large electric cables or anything which carries electricity. Finally for all experiments the same channel on the CB radio should be used, so that all enzymes will be exposed to the same frequency.
APPARATUS:
Pineapple, kiwi, papaya fruits; graduated cylinders; test tubes; test tube stopper; frozen calve liver; Hydrogen peroxide; electronic scale; water; plastic container; 6 gelatin snacks; CB radio; plastic tube; knife.
METHOD:
For fruit enzymes: Record at what time the experiment started. Cut a slice of the fruit, weight the slice on the scale, and record the weight. Cut the slice in several pieces, record how many were cut. Record the weight of a gelatin snack, this value should be found on the package itself. Label the container of the gelatin snack by indicating which fruit or enzyme is being added. Place the pieces of fruit, which should be of equal size, in the gelatin, some of them should be put in holes made in the gelatin with a knife, others can just be placed on the surface of the gelatin. The whole should be covered with cellophane film and placed in a refrigerator, this will make sure the temperature will remain constant for all the experiments. After three days the gelatin and the fruit can be taken out of the fridge. The film and the fruit can be removed. By now most of the gelatin should have turned into liquid. Pour all of the liquid into a graduated cylinder, then record the value which the liquid reaches. When taking the fruit out it should be made sure that any access gelatin liquid should be also included in the measurement.
After the first experiment is over, the second can be started. This requires the exact same steps as the first one. Be sure to use the same amount of fruit, the same number of pieces and also the same amount of gelatin snack, and also to record all of the quantities used. Once the fruit has been added to the gelatin, they should be placed in an open top box and then put in a fridge. A CB radio should be turned on and an elastic rubber band should be secured over the talk/transmit button so that it remains pressed. The CB should then be placed in the fridge so that its antenna rests on one of the edges of the box (see diagram). After three days the gelatin should be removed from the fridge and the same method to measure the liquid gelatin as the one used in the first experiment should be used. The new results should also be recorded.
For catalase enzyme: Cut, with a knife, a small piece of frozen calf liver. Weight it on a scale and record the value obtained. If the liver is 2 grams heavy, it should be reacted with 5 ml of hydrogen peroxide. Therefore 5 ml, or more depending on how much liver is being used, should be measured with a graduated cylinder, the value should be recorded, and then the liquid should be poured in a test tube. At the same time a container, of about the size of a plate, should be filled with water. A graduated cylinder of 60 ml or larger should also be filled with water and then it should be placed upside down in the container containing water. If properly done, the water in the cylinder should remain there without moving. This process should be done trying not to produce any air bubbles in the upside down cylinder, if this were to happen the results would not be accurate. One of the plastic tube’s ends should be passed through the water into the cylinder while the other end should be passed through the hole in the rubber stopper. The apparatus is now ready for the reaction to occur. The piece of liver should be added to the hydrogen peroxide and the test tube should be quickly covered with the stopper. When the liver starts reacting with the hydrogen peroxide lots of bubbles and a gas will be given off this is when a stopwatch should be started and after one minute the amount of water in the cylinder which has been displaced by the gas, should be measured by reading the water level in the cylinder, this value, which would equal the amount of gas produced by the reaction, should also be recorded.
For the second experiment the same method should be used as the first one. But when the liver is about to be dropped in the test tube the CB radio should be turned on and the transmission/ talk button should be kept pressed throughout the one minute. Be sure to use the same quantities used in the first process, and also to use a piece of liver similar in shape to the one used previously. Also all of the same values as the ones from the first experiment should be recorded.
METHOD CORRECTIONS:
Only one important change was made to the method. The CB radio required 10 AA alkaline batteries which lasted for about three hours. Therefore the electromagnetic field had to be suspended every three hours for about 2 to three minutes to change the empty batteries. Also during the night, for 12 hours, the CB radio was also turned off for convenience reasons and re-turned on during the morning. This time schedule was followed for all gelatin/ fruit experiments.
DATA COLLECTION:
Frequency used: 26.965 MHz
Maximum transmit power of CB radio: 5 watt
Amount of Amount of liquid
fruit used Amount of gelatin collected Fruit Enzyme W/out EMF With EMF gelatin used W/out EMF With EMF
Kiwi Actinidin 40g 8pc. 40g 8pc. 99g 6ml 23ml
Papaya Papain 30g 8pc. 30g 8pc. 99g 6ml 8ml
Pineapple Bromalain 25g 8pc. 25g 8pc. 99g 27ml 24ml
Catalase Enzyme:
Amount of liver used Amount of H2O2 used Amount of O2 produced
With EMF 2 g 5ml 54m
Without EMF 2 g 5ml 55ml
UNCERTANTIES:
Many uncertainties rose up as the experiments were carried out. First of all, even though one of the control variables was to keep all the reactions far from any potential electromagnetic fields, all of the experiments involving the gelatin had to be carried out in a refrigerator, this is because the gelatin had to be stored in cooler temperatures or else if it had been in room temperature (the experiment was done during summer where the temperature could reach 90F) it would have melted. The fridge probably emitted an electromagnetic field since it runs by electricity. It was also hard to make sure that the same fruit surface area had been exposed to the gelatin because mainly, while doing the second experiment, how many pieces had been packed in the gelatin and how many were just left on the surface during the first experiment was forgotten. It is very probable that the fruit’s surface areas were quite different in the two experiments. Many other errors many have happened in the measurements. The scale which was used, in fact, was not an electrical one but a normal analogical one which wasn’t as accurate and had 5 grams intervals. Therefore all of the weights measured with that scale aren’t very precise. It was very hard to determine the amount of gelatin broken by the enzyme into liquid, in fact it was difficult to judge whether the gelatin was liquid or still solid, the line is very fine in fact many parts were just about to turn into liquid and it was not clear whether they were meant to be included in the measuring. Another incertitude came up when the excess liquid gelatin was shaken off the pieces of fruit. When doing this some of the fruit’s juice may have been also squeezed in with the rest of the liquid. Also while the slices of fruit were acting on the gelatin, some of their juice may have been released and then it may have mixed with the liquid gelatin produced. The gelatin plastic containers also caused a problem, in fact it wasn’t sure whether they would obstacle the electromagnetic field created by the CB radio’s antenna. Lastly the CB radio as it ran out of battery would not transmit electromagnetic fields at the strength it did when the batteries were fully charged. In the catalase experiment some more uncertainties were encountered. One of them was caused by the graduated cylinder which was used to measure the amount of O2 produced in the reaction. In fact it was hard to read accurate values since it wasn’t a very specific cylinder, but it was a quite big one which only had intervals of 1 ml. While filling up the cylinder with water and when turning it upside down into the water filled container, some air bubbles were formed in the top of the cylinder. This happened in both experiments, and the air bubbles created in the cylinders were about the same size in both trials.
DATA ANALYSIS:
As we can see from the tables of results obtained, the outcomes of these experiments are quite contrasting. In fact in the first two experiments regarding kiwi and papaya fruit, we see an increase in the amount of gelatin broken down into liquid. This means that the enzymes actinidin and papain were able to break down more collagen proteins when the electromagnetic field was present then when it wasn’t. Therefore the reaction rate for these two enzymes was faster under the influence of an EMF. The reason for which the field may have improved the efficiency of the enzyme is not clearly known. It could have, in fact, orientated both the enzyme and the substrate molecules in a more efficient way which may have speeded up the reaction. Also it is known that electromagnetic fields have thermal properties. In fact one of the most dangerous characteristics is that the energy which they transmit is absorbed by objects, organisms and molecules as thermal energy, raising the substance’s temperature. If the electromagnetic energy was absorbed by the reactions as heat, it could have increased the molecules’ kinetic energy, increasing their movement and their chance of collision causing the reaction rate to increase. But in the experiments involving the pineapple fruit and the liver, the amount of products produced in the reactions were less under the effects of the electromagnetic field than without them. These results are very contrasting to the ones described earlier where the opposite happened. It could have happened that the effects it had on the previous enzymes and reactions would have had different consequences on catalase, bromalain and the reactions they catalyzed. For example the electromagnetic field may have also altered the orientation of the molecules in these two reactions, but in a way which did not encourage the reaction and therefore slowed it down. This could have happened because the molecules in question are different from papain and actinidin, they have a different amino acid sequence which will cause the enzymes to have different charges on different parts of their molecule. This means that the enzymes will react and orientate themselves differently from the other two enzymes. Since three of these experiments involved the protein collagen, we know that their substrate all were impacted the same by the EMF, and therefore they were all orientated in one manner. What could have happened is that, thanks to their specific distribution of charges on their structure, papain and actinidin were able to match the collagen’s orientation and therefore carry out their function of increasing the reaction rate. While bromalain orientated itself in a way which its active site was probably facing away from the collagen proteins and was not able to efficiently carry out the reaction, the reaction rate was obviously slowed down. For these reactions it can be ruled out the possibility of the electromagnetic field being able of actually altering the enzyme or the substrate’s structures by attracting to itself amino acids with a certain charge which would be able to break all bonds around themselves to follow their attraction to the opposite charge of one of the electrical poles created by the field. If this were to happen the results which would have been collected would show either no difference between the reaction rate of the one under the influence of an electromagnetic field and the one under no influence, or the reaction exposed to the field would come up to be slower than the control reaction. Also this could not have happened or else every enzyme should have been, in some part, negatively affected by the EMF. But as the results state, two of the reactions were actually facilitated by the radio’s emissions, and therefore their structure couldn’t have been affected by the field. The reaction catalyzed by the catalase enzyme, as it can be seen from the results, was slowed down by the presence of an electromagnetic field. This could also be due to a disturbance, caused by the field, in the orientation of the molecules which wont be able to complete the reaction anymore. Both the catalase and the bromalain enzyme could have though been affected by the energy given out by the electromagnetic field and which was absorbed by the molecules as heat. These two enzymes could have, in fact, been more sensible to heat than papain and actinidin, their optimum temperature may have been surpassed with the added heat the field supplied. This means that the enzyme could have been denatured by the increase in temperature provided by the CB radio, this would, as said in the theory, alter the enzyme and its active site’s structure and the substrate molecule wont be able to fit in the site, the reaction will therefore slow down. All of these explanations of what could have caused these results are, of course, meaningless if the uncertainties encountered produced inaccurate outcomes. Most differences in the amount of product produced are quite small, most of them, except for the actinidin reaction, are just of a couple milliliters difference. It could well be that an uncertainty caused these results. It can be seen, in fact, that some problems which rose during the experiments could have caused an alteration of the final outcomes. For example, in uncertainties in was explained that the reactions of the breaking down of collagen with the three fruit enzymes had to be carried out in a refrigerator which produced a field of a low intensity. It is possible that this may have influenced the process. In fact the control experiments had to be carried without any exposition to an electromagnetic field. This obviously did not happen since they were placed in the path of the fridge’s electromagnetic field. Whether this would have had any effects is very questionable since most electrical appliances produce very weak fields which aren’t very harmful. But if it did have influence the reaction than the control results would have been tainted, the values, in depending on what kind of effects the field would have on the enzyme, would have been higher or lower creating a larger or smaller gap in between the outcomes of the two experiments. The additional field could have also affected the results of the experiment which utilized the CB radio. In fact, on depending whether the additional EMF strengthens or weakens the original field, the values would either increase or decrease. The next problem was whether the surface area of the fruit pieces used for both experiments, one using an EMF and one without, was the same. As said before this was hard to manage both because the arrangement of the pieces of fruit was not the same for both experiments, also it was hard to repeat the same exact shape for the pieces. If in one of the two experiments the surface area of the fruit was larger than in the other one, that reaction would be advantaged because the enzyme molecules have more area over which they can break down the protein collagen. If the opposite was true than the reaction would obviously be slower. It can be seen, therefore, how surface area matters a lot to the final products of the reaction. It is also important to note that even though the two experiments did not have the same exact amount of surface area, the two values probably did not differ by much, and probably this small difference couldn’t have altered the results by much. Measurements were also a problem. In fact the apparatus used to determine the values needed was not very accurate. For example the scale and the cylinder both gave imprecise values. This could have caused two examples not to be using the same amounts of enzyme molecules, or, in the case of the cylinder, not to be able to indicate the exact quantities of substance produced. The fact that the exact amount of enzyme was not known and could have not been precisely replicated does not matter as much, because these differences are quite small and cannot effect the results that much. What matters, though is the fact that the exact quantity of products, especially for the catalase enzyme, could not be determined. This is quite important because electromagnetic fields would probably produce hardly noticeable effects. For example in the catalase/ hydrogen peroxide experiment, the field might have had an influence on the reaction by, for example, reducing the production of O2, yet this reduction would probably be such a small difference that very accurate material would be needed to measure it. Other uncertainties include the problem regarding the measurement of the liquid gelatin produced by the reaction. It was, in fact, hard to distinguish between liquid and solid gelatin. This though couldn’t have affected the results much since the same approach on how to choose what to measure was used for all experiments. Other problems encountered during the experiments surely did not alter in any way the results. For example the plastic containers used to hold the gelatin may have caused an obstacle for the electromagnetic field, but this will not change the outcome of this research since all of the experiments used the same containers and therefore the field had the same resistance for all enzymes. Also the air bubbles, which were formed in the cylinder during the preparation of the catalase reaction, did not make a different because both experiments with and without an EMF had a similar bubble which was added to the amount of O2 produced. Lastly it was questioned whether the decrease in strength of the field, due to a decrease in battery power, would also influence the results. Again all experiments were exposed to the same field at the same strengths therefore it would not matter. The last concern, which rose during the measurement of the liquid gelatin, was whether the pieces of fruit would have released any of their juice during the reaction, or if, when the excess liquid was shaken off the fruit, any of the fruit’s juice was also included with the gelatin. This actually may have had a large impact on the results. The problem is that for the two experiment no the same fruit was used, but, because they were done four days apart, they were different, so one could have contained more juice than another therefore releasing more juice during the reaction and when shaken. This fruit juice was therefore included in the liquid gelatin and was counted in the measurement of the products. This is most probable what happened to the products of the reaction catalyzed by actinidin, we can see, in fact, that the difference is too large and what probably happened was that for the experiment with the field a more juicy kiwi fruit was used which released all of its juice in the gelatin.
CONCLUSION:
From the results obtained a conclusion cannot be drawn. The outcomes of this research were too conflicting to come up with a yes or no answer to whether an enzyme molecule and an enzyme controlled reaction is affected by an electromagnetic field. In fact what can be said is that an electromagnetic field will have an effect on depending which molecule and reaction is being exposed.
EVALUATION:
Even though the results of this research may have not been very conclusive, they obviously gave an insight to the vast argument of electromagnetic field and their effects on the human body. An important point which should be brought up is the fact that all of the experiments were done in an environment which is not our human body, the human physiology can easily manipulate these fields and therefore an enzyme may have different reactions to an EMF inside the body. Yet this research focused more on the effects at the molecular level. This is why the method was quite appropriate in the way that it was able to support the approach which was chosen for this research. Of course there is always room for improvement, and in this case most of it should have been is the choice of apparatus used. In experiments like these the lack of precision in the experiments, limits the accuracy of the results, especially because an electromagnetic field will only produce very small differences, and also because enzymes are very delicate molecules and a small error could easily disrupt their activity. More accurate materials for measurements should have been used. Also the choice for enzymes made was not very good. In fact it was quite hard to observe the products of the reactions catalyzed by the actinidin, bromalain and papain enzymes. It would have been easier and much more accurate if an enzyme such as lactase, which breaks down lactose protein into sucrose and fructose, would have been and the amount of glucose produced would have been measured. Yet the use of the three fruit enzymes also had an advantage. Because they are very similar enzymes and they all acted on the same protein collagen, we were able to make comparisons in between them and the effects the electromagnetic field had on them. This would have been hard to do if the enzymes, or their reactions, had nothing in common. Also the use of a CB radio made the experiments more realistic since these sorts of radios are very used especially in between truck drivers. Also by placing the reactions very close to the antenna, and by using a field with the maximum amount of strength which could be found and used, we could simulate long term effects in a much shorter amount of time. The results obtained of course were not enough to fulfill this research question, it in fact would require much more detailed studied. It would be interesting, in fact, to pursue this subject, which still requires a lot of work, by investigating more enzymes molecules. By doing this it could be seen which ones are positively affected, which ones are negatively affected, and which ones are not affected at all by electromagnetic fields. This would lead to a pattern that could be created by finding a common trait or property which links all of the molecules that, for example, are not affected by an EMF. This would require, though, a very meticulous study of every enzyme molecule, which would include such things as their amino acid structure, their active site and the reaction they catalyze. Also to expand this research different frequencies and field strength should be considered. It is important to remember that this topic is very delicate in the fact that many factors need to be taken in consideration when experimenting on this subject. And also that a question of this size may need years to be resolved especially because of the high controversy around it, the controversy that our society runs on electromagnetism and the possibility that this may harm us in any way possible is always tried to be eliminated.
