During this experiment, enzyme activity of catecholase and its relationships with enzyme concentration, pH, temperature, and substrate concentration were tested. Enzymes are proteins that speed up biochemical reactions. By using a spectrophotometer, absorbance rates of the various samples were measured and the enzyme activity for each relationship was observed. While we were testing the effects of enzyme concentration, we found that as the concentration of enzymes in solution increased, the higher the absorbance rate. We tested the absorbance of four samples, all containing different enzyme concentrations. When the relationship between enzyme concentration and absorbance is graphed, it shows a rapid increase that eventually levels out. …show more content…
This is because the reaction reaches maximum velocity, where the addition of more substrate would no longer affect absorbance because all of the enzymes are involved in the enzyme-substrate complex. When testing the affects of varying temperature, an inverse relationship was observed where increasing temperature decreased the reaction rate and absorbance. Three samples were placed in three different temperatures, 10°C, 24°C, and 50°C. After sitting for ten minutes, the absorbance of each sample was measured. Our results showed that optimal temperature was at 24°C. However, the actual ideal temperature was determined to be 10°C, where the absorbance is the highest. If the reaction is above or below the optimal temperature for that particular enzyme, the point where rate is maximized, then the rate decreases. At higher temperatures, some enzymes become denatured and will no longer function properly. The final relationship tested was enzyme activity and pH. Five samples with varying pHs were tested. After graphing, our data formed a bell-curve, where the optimal pH was recorded at seven. At any pH other than seven, the reaction rate decreased. Enzymes are sensitive to pH and will become denatured in environments
In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or
Enzymes are biological catalysts, which means it decreases activation energy in reactions. The lower activation energy in a reaction, the faster the reaction rate. Many enzymes alter their shape when they bind to the activation site. This is called induced fit, meaning for the enzyme to work to its full potential it has to change shape to binding substrate. The location of enzyme’s activation site is on the surface of the enzyme, where the binding of substrates take place. Enzyme activity can be influenced by a variety of environmental factors. If the concentration of enzyme is low, and there is a great deal of substrate, then increasing enzyme concentration results in more molecules available to convert substrates to products. Thus, increasing enzyme concentration can increase reaction rate. If substrate concentrations are low, and many of the existing enzymes are idle because of a lack of substrate, then adding enzyme will have no effect on reaction rate. Enzyme concentration affects the enzyme activity, because the more enzyme concentration the faster the reaction rate, until it hits it’s limiting factor. When substrate concentration is increased, it also increases rate of reaction. Temperature plays an important
The Effects of Varied Temperatures, pH Values, Enzyme Concentrations, and Substrate Concentrations on the Enzymatic Activity of Catecholase
Enzyme catalysis is dependant upon factors such as concentration of enzyme and substrate, temperature and pH. These factors determine the rate of reaction, and an increase in temperature or pH above the optimum will
These results show how temperature of extreme high, or low affects enzyme activity. The highest rate of enzyme activity occurred at 37 Cº. Anything that was hotter or cold than 37 Cº slowed the reaction rate. As I thought, 100 degrees would denature the enzyme, and that was the case. The data provided shows exactly what temperatures enzymes work best, and worst. The objective was achieved as we discovered the different reaction rates under different temperatures. The results are reliable, as we know enzymes do not work well when under extreme heat or denaturation occurs. What I learned in this experiment was that enzymes don’t work well under cold temperatures because they tend to move slower. My hypothesis did not quite match, because I thought they work best at lower temperatures.
Five different temperatures of enzyme (spinach extract) (5°C, 20°C, 35°C, 45°C and 65°C) were added to individual measuring cylinders -each filled with 7ml of Hydrogen Peroxide (H202). The height of foam (oxygen + water) produced by the reaction was recorded for each temperature of the catalase after 30 seconds, to find at which degrees the enzyme activity had the fastest reaction rate. The data collected from this experiment suggested that the enzyme extract had the greatest efficiency at 20 °C, and the temperatures greater displayed a decline in rate of reaction.
This leads me to the argument that there is a relationship between concentration and absorbance that will enable me to determine the concentration of a solution through the measurement of the color change in a reaction tube (Bio 5LA- Lab # 5, pp.3). It is evident, that the relationship between concentration, reaction rate, color change, and absorbance plays an important role in demonstrating that the reaction rate, goes hand in hand with concentration. Ultimately, their relationship will directly affect the reaction rate of an enzyme-catalyzed reaction (Maslov, Dmitri).
The kinetic profile of tube 1 is represented by a horizontal line in graph 1. Tube 2 contained 0.01ml of enzyme and graph 2 represents the kinetic profile of tube 2. It shows that the absorbance of tube 2 increased over time at an exponential rate. The amount of enzyme added to tube 3 was 0.1ml. The absorbance of this tube increased at a steady rate over time. Graph 3 represents tube 3 and its enzyme kinetic profile is indicated by the positive linear line. About 0.5ml of enzyme was added to tube 4 and graph 4 represents its kinetic profile. The absorbance increased over time, but at the end it began to plateau. Comparing the kinetic profiles of 4 tubes, the appropriate enzyme concentration needed for the assay was determined to be
In the following experiments we will measure precise amounts of potato extract as well as Phenylthiourea, combined with or without deionized water and in some instances change the temperature and observe and record the reaction. We will also investigate the different levels of prepared pH on varying samples of the potato extract and the Phenylthiourea and record the results. We will answer question such as what is the best temperature for optimum temperature reaction as well as the best pH level for the same reaction.
This experiment is designed to analyze how the enzyme catalase activity is affected by the pH levels. The experiment has also been designed to outline all of the directions and the ways by which the observation can be made clearly and accurately. Yeast, will be used as the enzyme and hydrogen peroxide will be used as a substrate. This experiment will be used to determine the effects of the concentration of the hydrogen peroxide versus the rate of reaction of the enzyme catalase.
reaction rate increases. If the temperature of an enzyme gets to high the reaction rate will slow
This experiment is designed to test the role of temperature on enzyme activity. Enzymes are
Although there is also a maximum rate, it is not that the substrate will stop producing, it is that the enzyme will be completely saturated thus stopping the production of the reaction. The reaction is also the same with the enzyme concentration in that the production will increase as the saturation increases, but the substrate will also become saturated and will yield production. Enzymes are important in the biological world because it can help a scientist control the reaction of a substance based on the factors he or she wants to follow. This experiment will prove that temperature, pH, substrate concentration, and enzyme concentration can alter the reaction rate of a substance.
When examining the effect of pH or temperature on enzyme function it is important to consider the type of enzyme being examined. While there may be an apparent effect of pH and temperature on all enzymatic function, the extent of the effect is dependent on the type of enzyme being examined. The current study is focused on the effect of temperature and pH on catechol oxidase; an enzyme that oxidises catechol.
that changes in temperature, pH, enzyme concentration, and substrate concentration can affect the initial reaction rates of enzyme-catalyzed