Enzymes Catalysts In Biochemical Reactions Biology Essay

Enzymes Catalysts In Biochemical Reactions Biology Essay Introduction Enzymes are resourceful catalysts for biochemical reactions, like all catalysts enzymes tend to speed up reactions. Enzymes use alternative reaction pathway of lower activation energy. They take part in the reaction, and as a result their able to provide alternate pathways. Throughout the reaction enzymes remain unchanged because they cannot experience any permanent changes. Enzymes only have the ability to change the rate of the overall reaction; they cant affect the reactions position of the equilibrium (Rsc). In most cases a chemical catalyst will catalyze any sort of reaction, enzymes differ in this sort. Enzymes tend to be specific, and this is due to the shape of enzymes molecules (Rsc). Enzymes are made up of several proteins in a tertiary structure; these proteins tend to be globular. Many enzymes consist of a protein and a non-protein, called a cofactors and coenzymes. Cofactors are inorganic molecules that bind to enzymes to help them function examples maybe be zinc/magnesium ions (Zn2+, Mn2+), and coenzymes are organic molecules that bind to enzymes to help them function. An example of one of the most important coenzymes is nicotinamide adenine dinucleotide (NAD+), this substrate acts as an electron carrier in cellular respiration (Nelson Biology 12). Enzymes consist of active sites, which are parts of the enzyme molecule that have the ideal shape and functional groups to bind to one of the reacting molecules. The reacting molecule that binds to the enzyme is called the substrate. An enzyme-catalyzed reaction takes a different direction than a reaction without catalyst. When the substrate binds to the enzyme a reaction intermediate is produced. This intermediate has lower activation energy than the reaction without the enzyme catalyst (Rsc). There are two kinds of enzyme reactions, catabolic and anabolic. In a catabolic reaction the interactions between the substrate and enzyme causes stress and distorts the bonds in the substrate, allowing bonds to break. In an anabolic reaction the enzyme allows two substrates to have proper orientation to allow bonds to form between them. As a result the activation energy is lowered in both the catabolic and anabolic reaction (Nelson Biology 12). Catalase is a common enzyme found in most plant and animal cells that functions as an oxidative catalyst, it decomposes hydrogen peroxide into oxygen and water. Its structure is made of 4 main polypeptide chains, which can each be over 500 amino acids long. Catalase optimum temperature can vary depending on the species; similarly the optimum pH also varies from approximately 4-11. In humans however the optimum pH for catalase tends to be neutral. One molecule of Catalase can break down 40 million molecules of hydrogen peroxide each second (Catalase). The overall reaction is: 2 H2O2 à ¢Ã¢â‚¬  Ã¢â‚¬â„¢ 2 H2O + O2 Many factors such as temperature, pH, inhibition of enzyme activity, substrate and enzyme concentrations can influence the affect the enzyme has on the reaction. As the temperature rises, reacting molecules gain more kinetic energy, as a result the chances of a successful collision increase and thus the rate increases. There is a specific temperature when an enzymes catalytic activity is at its maximum. This optimal temperature is usually around human body temperature (37.5 oC) for the enzymes in human cells (Figure 1). When the temperature increases past the optimal temperature the enzyme becomes agitated, it begins to denature and ultimately lose its overall affect on the reaction (Nelson Biology 12). This occurs because the increase in temperature achieves higher kinetic energy and as a result the intra- and intermolecular bonds are broken in the enzyme molecule (Rsc). Each enzyme works within a fairly small range of pH levels. Similar to temperature there is a pH at which its activity is at its maximum, the optimal pH (Figure 2). This is because changes in pH can create and break intra- and intermolecular bonds, changing the shape of the enzyme and ultimately the rate at which it will react. The rate of an enzyme-catalyzed reaction depends on the concentrations of enzyme and substrate. As the concentration of either is increased the rate of reaction increases (Figure 3). When substrate concentrations are increased the overall reactions proceeds to increase up to a certain point, at this point the active sites have become saturated by the substrate and there are no further significant changes in the rate of reaction (Figure 4) (Rsc). Some substances reduce or even stop the activity of enzymes in biochemical reactions. They do this by blocking or distorting active sites of enzymes. These substances are referred to as inhibitors. Inhibitors that occupy the active site and prevent a substrate molecule from binding to the enzyme are said to be competitive, as they compete with the substrate for the active site. Inhibitors that attach to other parts of the enzyme molecule, perhaps distorting its shape, are said to be non competitive (Nelson Biology 12). Figure 1: Table 1Analysis Amount of H2O2 (mL) Amount of Distilled Water (mL) Amount of pH Buffer (mL) pH Level Vertical Distance Travelled by Filter Paper Towards Meniscus Time taken by filter paper disc to move to meniscus (s) Upward velocity of Filter Paper Disc (cm/s) 10 mL 5 mL 7 (Control) 8.15 6.6 1.23 10 mL 5 mL 4 8.15 7.05 1.16 10 mL 5 mL 9 8.1 10.4 0.78 10 mL 5 mL 12 7.85 8.14 0.96 Figure 2: Graph 1 Test Tube Temperature ( °C) Distance (cm) Time (s) Rate of Reaction (cm/s) A 10.0 8.00 5.85 1.38 B 21.0 8.00 4.83 1.66 C 35.0 8.00 2.99 2.68 D 50.0 8.00 4.21 1.90 E 80.0 8.00 5.52 1.45 Figure 3: Table 2As the pH increased from 2-7 so did the velocity of the reaction (refer to figure 1: table 1). The reaction had an optimal pH of 7, and as the pH increased after the velocity of the reaction rapidly decreased. Notice the velocity for pH 12 is higher then the velocity of pH 9 (refer to figure 2: graph 1). Figure 4: Graph 2 As the temperature increased from 10oC-30oC so did the rate of the reaction (refer to figure 3: table 2). The reaction had an optimal temperature of 35oC, and as the temperature increased after the rate of the reaction began to rapidly decrease (refer to figure 4: graph 2). Enzyme concentration Distance (cm) Time (s) Rate of Change (cm/s) Other observations 100 % concentration 8 cm 3.02 s 2.65 cm/s bubbles appeared 80 % concentration 8 cm 5.06 s 1.58 cm/s fewer bubbles than previous composition 60 % concentration 8 cm 6.28 s 1.27 cm/s fewer bubbles than previous composition 40% concentration 8 cm 7.5 s 1.07 cm/s fewer bubbles than previous composition Figure 5: Table 320% concentration 8 cm 19.65 s 0.41 cm/s no bubbles appeared Figure 6: Graph 3 Figure 7: Table 4 Figure 6: Graph 3Increasing the concentration of the enzyme catalase (potato juice) rapidly increased enzyme activity (refer to figure 6: graph 3). Concentration of H202 of Distilled Water Trial Time of catalase to travel from the bottom of the test tube to the top (s) Distance of bottom of test tube to substrate(cm) Rate of change of the catalyzed reaction (cm/s) 15 mL of H202 3% 1 5.89 8.0 1.36 2 6.86 8.0 1.17 Total 6.38 8.0 1.27 13 mL of H202 2.6% 1 8.13 8.0 0.98 2 7.11 8.0 1.13 Total 7.62 8.0 1.01 10 mL of H202 2% 1 8.65 8.0 0.87 2 12.8 8.0 0.63 Total 10.73 8.0 0.75 7.5 mL of H202 1.5% 1 9.43 8.0 0.84 2 12.53 8.0 0.64 Total 10.98 8.0 0.74 5 mL of H202 1% 1 10.37 8.0 0.77 2 12.88 8.0 0.62 Total 12.63 8.0 0.70 Figure 9: Table 5 Figure 8: Graph 4Increasing concentrations of the substrate slowly increased from 1% to 2% (refer to figure 8: table 4), then as substrate concentrations increased more the rate of change became more rapid (refer to figure 9: graph 4). Experiment Number Amount of Inhibitor (copper (II) sulphate) (drops) Time taken by enzyme disc to float to top of test tube (s) Distance travelled by enzyme disc to top of test tube(cm) Rate of Change of Enzyme Activity(cm/s) 1 0 4.13 8.0 1.94 2 1 4.68 8.0 1.71 3 5 5.57 8.0 1.44 4 10 6.66 8.0 1.20 5 15 8.57 8.0 0.93 Figure 10: Graph 5 As the amount of copper (II) sulphate increases the overall reactions begins to slow down, and the rate of reaction decreases (refer to figure 10: graph 5). Evaluation Part One: Affects of pH Enzymes are very sensitive to changes in pH, and significant changes in pH can affect enzymes in numerous ways. The effects of pH on enzyme activity are due to changes in the ionic state of the amino acid deposits of the enzyme and the substrate molecules. These variations in charge will affect the binding of the enzyme and as a result, enzyme activity will increase or decrease. Over a tapered pH range these effects will be reversible however high acid levels often cause permanent denaturation of the enzyme (Users.rcn). Before conducting this experiment one can anticipate that pH levels too high or too low would cause the enzyme to denature and thus it would no longer have an affect on the overall reaction. In this experiment 5 pH levels were used 2, 4, 7(control), 9, and 12. When the buffer solution affected the pH levels of the H2O2 from 2 to 4 there was a slight increase in enzyme activity (from 0.47 m/s to 1.16 m/s). There was one control test tube contain ing H2O2 with a neutral pH of 7. This test tube conducted the highest velocity of 1.23 m/s. As a result the optimal pH for the H2O2 was at a neutral pH of 7. When the pH level of the H2O2 increased to 9 the velocity seemed to decrease, which illustrated the loss of the effect of the enzyme. However this trend did not seem to remain consistent because when the pH level was increased to 12 the velocity of the enzyme also increased. As a result, it can be stated that enzymes work best in the region of neutral pH levels, and when pH levels become too high or to low enzyme activity decreases thus the hypothesis proved to be partly correct. Part Two: Affects of Temperature The temperature of the H2O2 can severely affect the overall outcome of a reaction. Like most chemical reactions, enzyme-catalyzed reactions also increase in speed with an increase in temperature. As the temperature of the enzyme increases past a critical point thermal agitation begins to disrupt the protein structure resulting in the denaturation and loss of enzyme function (Nelson Biology 12). The hypothesis for this experiment was similar to that of pH, temperatures too high or too low would cause denaturation of the enzyme and thus it would no longer have an affect on the overall reaction. In this experiment 5 different temperatures were used 10oC, 21oC, 35oC (control), 50oC, and 80oC. When the temperature was decreased to 10oC the rate of the reaction was at it lowest of 1.38 m/s. At 21oC the rate slightly increased to 1.66 m/s. Thus there is a trend of lower temperatures causing the enzyme to lose its overall affect. There was one control test tu be containing H2O2 that was at room temperature which was 35oC. This test tube conducted the highest rate of reactions of 2.68 m/s. As a result the control test tube achieved the optimal temperature. When the temperature of the H2O2 began to increase from 50oC to 80oC there was a trend of the enzyme losing its affect, and having an overall lower rate of reaction. As the temperature increased before the optimal temperature the rate of the reaction increased, and when the temperature continued to increase past the optimal point there was a rapid decrease in the rate of the reaction thus it is evident the hypothesis was correct. Part Three: Affects of Changes in Concentrations The rates of enzyme-catalyzed reactions severely depend on the concentrations of enzymes and substrates. If one person is pushing a car it likely that car will take longer to get to and end point, however if 10 people are pushing that same car it will obviously get to the end point a lot quicker. It is the same with enzyme and substrate concentrations, the higher the concentrations the faster the reaction works. As the enzyme concentration increases so does the number of enzyme molecules, thus more substrate molecules can be acted upon at the same time which means they breakdown a lot faster. As the substrate concentrations increase, the reaction also proceeds to increase however with high levels of substrate concentrations the active sites become saturated and the enzyme no longer has an effect of the reaction (Worthington-biochem). The hypothesis for this experiment was simple, as enzyme and substrate concentrations increase so will the speed of the reactions. When changing the substrate concentrations, the five H2O2 concentrations where 3% (control), 2.6%, 2%, 1.5%, and 1%. The main trend in this experiment was the higher the concentration of the substrate the higher the rate of change. There was a significant and rapid increase in the rate of change from concentrations of 2% to 3%. When changing the enzyme concentrations, the five potato juice concentrations where 20%, 40%, 60%, 80%, and 100%. Changing the concentration of the enzyme had a similar affect to when the substrate concentrations were changed. The more concentrated the enzyme was the higher the rate of the reaction. The rate of the reaction rapidly increased from 20% to 40%, however it became a bit constant from 40% to 80%, and from about 80% to 100% it began to promptly increase again. As a result, it is evident the hypothesis was correct as the concentrations increased so did the reactions. Part Four: Effect of the Inhibitors Inhibitors are used to block active sites of enzymes. They are substances used to slow down, or in some cases stop catalysis. Inhibitors either compete with a substance for the enzymes active site (competitive), or they bind to another site on the enzyme changing its shape (non-competitive) (Nelson Biology 12). Before conducting this experiment one can anticipate the more amount of inhibitor present the slower the reactions will proceed. In this experiment copper (II) sulphate was used as the inhibitor. In the five trials 0, 1, 5, 10, and 15 drops of the copper (II) sulphate were used. The obvious trend was the more inhibitor the lower the rate of reaction. Thus, the hypothesis was correct. Sources of Error Error #1: Consistency of Filter Paper When conducting each individual experiment for many groups it seemed the most difficult task was getting the filter paper to arrive at the bottom of the test tube. When the filter paper was placed in the test tube it would go about half way down the test tube, however because the reaction catalyzed quickly the filter paper would begin to rise and travel back up to the top of the hydrogen peroxide liquid. As a result you would have to perform the experiment again, with a new catalyzed filter paper. This became a source of error because it made it difficult to collect consistent data. For every test tube, and trial the filter paper did not reach the bottom of the test tube at the exact same time. In some cases it would reach the bottom without difficulty, and in other situations it became a constant struggle to push it down the test tube. During certain trials the experiment had to be performed again and the hydrogen peroxide had already lost its affect from the previous catalyzed reac tion. As a result, it is evident that the consistency and rate at which the filter paper travelled down the test tube is a significant source of error. To improve this source of error, heavier and more durable filter paper should be used. One can purchase wet strength filter paper which will make its way down the test tube on its own without any human force. Error # 2: Accuracy of Inhibitor During this experiment it became difficult to get exactly 15 mL of hydrogen peroxide after the inhibitor has been added. Copper (II) Sulphate is a severely small solvent so when added to the hydrogen peroxide one cannot control the amount of liquid present. This occurs because before adding the copper (II) sulphate it is uncertain how much hydrogen peroxide needs to be reduced in order to have exactly 15 mL. This creates a source of error because now the data collected is inconsistent because of the different volumes of hydrogen peroxide. To prevent this source of error one can use a different inhibitor that will dissolve in the hydrogen peroxide and not change its volume. Error # 3: Catalase in Potatoes During the experiment potato juice was constantly being pumped and used as the enzyme to catalyze the reactions. However it was not considered that each potato is harvested in a different way and one potato may have several nutrients, while the other may be completely dead. This results in the difference of concentrations of catalase that was taken from each specific potato. Once again this source of error causes a inconsistency in the collection of data because one cannot be certain they used the same potato, that pumped a constant concentration of catalase throughout the whole experiment. For the purpose of this experiment if only one potato was ground and made into potato juice then catalase concentrations would be consistent and it would eliminate this source of error. Next Steps A similar experiment that could be performed is Saturation Points of Substrate Concentrations. In the current lab saturation was not tested when changing around substrate concentrations. One can test the amount of substrate it would take to saturate the active site on the enzyme, and proceed to evaluate how much more of the enzyme concentration is needed to unsaturate and dissociate the substrates from the active site of the enzyme. Another experiment that could be performed is Affects on Various Enzymes. Instead of just observing the affects of change of pH, temperature, concentrations, and inhibitors on Catalase it can be tested on other enzymes. For example Cellulase, Lactase, and Pepsin.

Face Recognition Study: Inverted V Upright Faces. Essay

Face recognition study: Inverted V Upright faces. Introduction: Face recognition is a difficult visual representation task in large part because it requires differentiating among objects which vary only subtly from each other. This particular face recognition study was expected to suggest that people recognise inverted faces less accurately than upright faces. The study involved sixty different faces observed on a computer screen by a sample of first-year university students. Hypothesis: The hypothesis for this study stated that it is expected that people recognise inverted faces less accurately than upright faces. The null hypothesis stated that there would be no difference in the amount of faces recognised regardless of whether they were upright or inverted and that if there was to be any difference that it would be down to chance. Method: Participants: The sample used consisted of 15 first-year psychology students of mixed ages. Gender or race held no significance for this study. The psychology students used participated in the experiment in there seminar groups at allocated times throughout a timetabled week. Materials: The materials used for this study consisted of the e-pro computer programme which was used in order to display the faces required for the experiment. Furthermore, the results of the study were interpreted using the SPSS computer software. Procedure: For the first part of the experiment, sixty faces, thirty of which were upright and thirty of which were inverted were displayed on a computer creen for two seconds per face. After each participant had viewed the full sixty faces, a distracter task was then issued to them in order to remove any short-term memory effects on facial recognition. The distracter task consisted of a series of personal questions and lasted for roughly five minutes. Upon completion of the distracter task, the second part of the experiment took place. During the second phase of the experiment, sixty of the previous faces w ere shown alongside a set of sixty new faces. Participants were asked to say whether or not they recognised the faces from the earlier stage of the task. Results: The mean number of recognised inverted faces was 0. 67 with a standard deviation of 0. 07. The mean number of recognised upright faces was 0. 74 with a standard deviation of 0. 05 ? Figure 1 shows the mean value for facial recognition of upright faces to be significantly higher than that of inverted faces: t(14) = 3. 55, p= 0. 03 Figure 1: Mean values of facial recognition for inverted and upright faces. Discussion: The results recorded from this study suggest that our hypothesis that people recognise inverted faces less accurately than upright faces may be correct. However, to be more certain that our hypothesis is accurate, it should be ensured that the experiment is repeated and that in this instance is counter-balanced across the whole sample of first-year psychology students collectively and not just within their seminar groups.

Movie Review: Singin’ in the Rain

Movies such as Chicago, Moulin Rouge, and Singin’ in the Rain are part of a file genre that places emphasis on music, dance, and song.   This genre is known as the Musical.   The power of the songs in Musicals explains why many people who have not seen the movie are still familiar with its title song â€Å"Singin’ in the Rain.†Ã‚   Aside from the memorable scores and lyrics, Musicals showcase the singing and dancing skills of their stars.   The critical and commercial success or failure of a Musical hinges not only on the storyline, as is the case with films of other genres, but the talents of the actors who bring the movie’s songs and dances to life. Singin’ in the Rain contains a number of elements that make it stand out from other American Musicals such as Chicago and Moulin Rouge.   The atmosphere of Singin’ in the Rain is light and happy which is accomplished by the character’s brightly colored clothing and the inclusion of relatively few night scenes.   This is not the case in either Chicago or Moulin Rouge, both of which have darker elements within them.   Because the theme of Singin’ in the Rain is more playful than the serious theme depicted in Chicago, there is a greater degree of entertainment in Singin’ in the Rain.   This movie was designed to be viewed by an audience seeking pure entertainment—an audience that need only sit back, relax, and enjoy the film from beginning to end. Many modern musical productions are far more costly than was Singin’ in the Rain; however, even with the discrepancy in production costs, several clever and memorable musical numbers from Singin’ in the Rain remain popular today. Because scripting and storyline are superseded in Musicals by choreography and score, the scenes most often remembered in a Musical are specific numbers contained within the film.   One of my favorites from Singin’ in the Rain is Cosmo Brown’s (Donald O’Connor) performance of â€Å"Make ‘em Laugh.†Ã‚   The song’s lyrics and the number itself reveal that Cosmo is Don Lockwood’s (Gene Kelly) sidekick.   It’s clear that Cosmo’s job is to keep Lockwood laughing and to prevent him from concern over anything bad. Cosmo’s enthusiastic performance in this number is easily the most comedic of the film.   Singin’ in the Rain is filled with mise-en-scà ¨nes, and Cosmo’s â€Å"Make ‘em Laugh† number uses mise-en-scà ¨ne to its fullest.   Every bit of setting, including the props and the people in this number are used by Cosmo as show instruments. Given the movie’s title, it isn’t surprising that the most famous number is Gene Kelly’s (as Don Lockwood) performance of the song â€Å"Singin’ in the Rain.†Ã‚   Narrative Convention dictates that rain signify sorrow or loneliness much as tense music in a horror movie signifies danger; however, the gloom one might expect to infiltrate Kelly’s performance simply does not do so.   Instead, this beautifully choreographed athletic dance and song number stands as Lockwood’s proclamation that he has succeeded in his career and in his heart.   Each step Gene Kelly performs is deliberate—each movement designed to thrill the audience the way Kelly’s Lockwood is himself thrilled by his fantastic fortune. The use of mise-en-scà ¨ne in the number â€Å"Singin’ in the Rain† does not detract from Kelly’s performance: it augments it.   His wearing a felt hat allows his facial features to be seen without the rain’s moisture obscuring his emotions.   The umbrella he carries adds a gentleman-like quality to his movements.   The street on which he dances remains basically deserted and is perfectly illuminated by the well-placed snug lights.   Personally, I think it is the most enjoyable rainy scene I have ever viewed in a movie. My only critical comments are centered on a portion of the film’s latter half during which time Lockwood, Cosmo, and R. F. Simpson (Millard Mitchell) are planning to make the musical film Dancing Cavalier.   This is followed by the surreal performance â€Å"Broadway Melody† which I found unnecessary.   The woman in this scene seemed to have come from nowhere, did not have a clearly defined relationship with Lockwood or Kathy Selden (Debbie Reynolds), but the odd emotion that was present in the number might be representative of American ideals. Singin’ in the Rain falls within the expected boundaries of the Musical.   The ending is predictable (but not unsatisfyingly so) and relatively little tension exists: the lovers meet serendipitously, and there is really no threat to their relationship. Singin’ in the Rain is from the 1950’s, and because of this, some younger people might not find the movie’s content satisfying; however, anyone, regardless of age, who can appreciate the outstanding singing and dancing performances of the movie’s characters will come away from the film satisfied.   In addition, part of this film’s content reveals the early development of movies from the silent era forward, and much of this is not only interesting but humorous as well. I admit to having been initially skeptical about enjoying this movie due to its age, but I found myself entertained throughout the entire film, and honestly, I can say that Singin’ in the Rain is the best Musical I have ever seen. Reference Freed, A.   (Producer), & Donen, S. & Kelly G. (Directors).   (1952).   Singin’ in the rain.   [Motion picture].   United States: Metro-Goldwyn-Mayer.   

What I Learned About Food Marketing - 856 Words

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