State the optimum pH for sucrase activity and describe how sucrase activity changes at more acidic and more alkaline pH values. Table 2: Effect of Temperature on Sucrase Activity Optical Density 10 °CC (50 °F) 20 °C (68 °F) 30 °C (86 °F) 40 °C (104 °F) 50 °C (122 °F) 60 °C (140 °F) 70 °C (158 °F) 1 0.006 0.273 0.791 0.940 0.927 0.807 0.613 2 0.010 0.285 0.761 0.954 0.934 0.846 0.604 3 0.009 0.255 0.773 0.941 0.907 0.845 0.642 average 0.008 0.271 0.775 0.945 0.923 0.833 0.620 Effect of Temperature on Sucrase Activity 2. Was the rate of increase of sucrase activity higher at a pH of 8.5 or a pH of 5.5?…
The lowest one was hot temperature. This was because the enzyme was trying trying to move too fast and it was not able to react the right way because of the denatured…
INTRODUCTION: The objective of this lab is to measure the activity of an enzyme and the effects of environment conditions on enzyme activity. Enzymes are catalysts; agents that speed up chemical reactions by lowering the activation energy required. This means that a catalyst helps reactions occur at a greater speed and lower temperature.…
The difference between the two graphs is the speed of the reaction. The temperatures of the two tests were very similar throughout the experiment. when doing this experiment one should have a paper towel ready to wipe the side of the test tube to be able to read the temperature. Conclusion: This experiment tested the difference between a untreated and treated catalase enzyme.…
From 10oC to 20oC, the average rate of reaction of the class results is higher than the raw results rate of reaction by a maximum of 0.75mL/sec. However, from 30oC to 50oC, the raw results presented a slightly higher lot of rate of reaction than the average rate of reaction from the class results. The highest rate of reaction difference was for 50oC, with a difference of 0.3mL/sec between the raw and average results. This information supports the hypothesis, yet the result for 10oC and 20oC do not support the hypothesis, as due to the information known about enzymes, the lower the temperature, the slower the rate of reaction should be, therefore the average rate of reaction does not support the…
In this part of the experiment there was an experimental error as the reaction rate should have been lower when there was a lower…
ABSTRACT: Enzymes are catalysts, speeding up of chemical reactions, of biological systems by lowering the activation energy (Transitioned from the AP Biology Lab Manual). In addition, in order to determine the rate of an enzymatic reaction, one must measure a change in the amount of at least one specific substrate or product over time. We were curious about determining the effects of pH and heat on enzymatic activity because these are factors that usually affect the shape of an enzyme. We measured enzyme activity using an indicator for product at different pHs and temperatures.…
Temperature clearly alters the enzyme reaction rate and the results of our experiment greatly defends our first hypothesis. However, if you single out the data recorded from the solution placed in the 0 degree Celsius and compare it to the rest of the data from the solutions placed in the other heating bathes you will see a quiet interesting result. What we believe that seems to be happening here is a discrepancy in our data because it does not quiet seem to follow the pattern of our other three recordings. We came to the conclusion that the particles inside our solution that was placed in the 0 degree bathe caused the reading in the spectrophotometer to be inaccurate and misread. In future work of similar experiments or use with the spectrophotometer, one should make sure the solution inside the cuvette it is well agitated and shaken to decrease the error of misreading the concentrations.…
The purpose of conducting this experiment was to explore how different factors affect the reaction rate of enzymes reacting with their corresponding substrates in order to learn more about how enzymes function in different environments. The independent variables investigated in this experiment were the concentration of different substrates, the temperature of the environment, and the effect of a catalyst on the reaction rate. The dependent variable for all of the investigations was the time it took for the reaction to occur. To investigate the effect of the concentration of the substrate on the reaction time, four test tubes were used.…
Discussion In this study, the Catechol enzyme was studied under the conditions of varying pH, temperature, substrate concentration, and enzyme concentration. In Figure 1, the data suggested that the trend was neither directly nor inversely proportional, but the highest activity rate was at 24°C. Most enzymes denatured at higher temperatures of approximately 40°C, which led to the inability to see any color change (Helms et al., 1998). At lower temperatures, the enzyme was somewhat efficient because molecules move slower at lower temperatures, so enzymes lost productivity.…
A timer was placed for a minute and the data was collected every five seconds. (see pg. 36 lab manual) Results: Figure 1-The Rate of Reaction for optimal Temperature In this graph we can clearly see that Horseradish peroxidase reacted the most with the enzyme at 25 ℃ .…
In a similar experiment done by a student (UK Essays [B], 2015) they also discovered that the optimal temperature was between 30oC and 40oC and they also made the statement that 37oC would have been optimal but no results were gained from this temperature so claim can be made, many other experiments also claim that 37oC is the optimal temperature. The reason that the temperature has this effect on the reactions is because of particle collision theory. An increase in temperature causes the enzymes and the substrates to collide more frequently as they have more energy therefore increasing the reaction rate. When the temperature exceeds its optimum the active site denatures, slowing down or stopping substrate binding and hating the reaction (Kopaleishvili, 1995). At lower temperatures, the energy of particles is lower and there are less collisions.…
Amylase is an enzyme that breaks down starch. Among other factors, high temperatures denature enzymes. Through experimentation this was not observed. The results of the experiment resulted in flawed data. By human error, a mistake was made that affected how well the enzymes synthesized starch.…
To investigate the effects of concentration on the activity of salivary amylase Hypothesis: The lower the concentration of the salivary amylase, the less the enzyme activity and vice-versa is true provided that other factors such as temperature and the pH are kept constant. Variables: Independent variables: • the concentration of the salivary amylase Dependent variables: • the enzymatic activity • the colour change of the saliva solution Controlled variables: • the temperature…
In experiment 2.1, absorbance readings for both heated and unheated corn and tapioca starch were taken. For both starch’s the heated results came to be much higher then the un-heated as seen in Table 2.1. Iodine reacts with the amylose compound in starch where it gets trapped in the amylose coils and blue-ish colour is formed after the addition of Lugols reagent (Fennema and others 2008). The absorbance readings came out higher for heated corn starch because iodine had more amylose to react with. As corn-starch is heated gelatinization occurs where amylose is released since the starch granule is disrupted.…