More handpicked essays just for you.
Effect of temperature on enzyme activity
Impact of temperature on amylase
Effect of temperature on enzyme activity
Don’t take our word for it - see why 10 million students trust us with their essay needs.
Recommended: Effect of temperature on enzyme activity
The enzyme experiment was conducted to further comprehend the effect of temperature on amylase activity. The varying temperatures used in this experiment were 0°C, 25°C, 55°C, and 85°C. The two kinds of Amylases that were experimented with were fungal Amylase from Aspergillus Oryzae, and bacterial amylase from Bacillus licheniformis. The experiment was setup to determine the temperature at which these two different amylases function more properly, this is know as the optimum temperature of enzymes. Starch was added to a bacterial amylase to create a mixture and approximately after two minutes, the mixture of starch and bacterial amylase was added to three drops of Iodine that was in a well of a spot plate, The same steps were repeated with
After conducting this experiment and collecting the data I would have to say that the optimal temperature for enzyme activity would have to be room temperature which in my experiment was thirty-four degrees Celsius. I came to this answer because the glucose test strip showed that at room temperature there was more glucose concentration that at either of the other temperatures. Due to temperature extremes in the boiling water the enzymes could no longer function because the breakdown of lactose stopped. The cold water also hindered the breakdown of the lactose but as the water warmed the enzymes were more active which can be seen in the results for the cold water at 20 minutes B. Describe the relationship between pH and the enzymatic activity of lactase.
For example, incubating the samples at different temperatures would create more data points to establish an optimal temperature. From the results in the experiment in this study, it is known as temperature increases, enzymatic activity increase, and vise versa. However, what can not be observed is at what point does the increase in temperature begin to denature the enzyme, above 60°C. Furthermore, assays can be preformed to determine optimal pH, as well. From Dutta’s, and his partners, experiment it shows that there is a range where the Heliodiaptomus viduus’s lactase shows the most activity, which is between 5.0 and 6.0
called an active site. This active site is made by a few of the amino
The Effect of Temperature on an Enzyme's Ability to Break Down Fat Aim: To investigate the effect of temperature on an enzyme’s (lipase) ability to break down fat. Hypothesis: The graph below shows the rate increasing as the enzymes get closer to their optimum temperature (around 35 degrees Celsius) from room temperature. The enzyme particles are moving quicker because the temperature increases so more collisions and reactions occur between the enzymes and the substrate molecules. After this the graph shows the rate decreasing as the enzymes are past their optimum temperature (higher than). They are getting exposed to temperatures that are too hot and so the proteins are being destroyed.
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
The Effect of Temperature on the Activity of the Enzyme Catalase Introduction: The catalase is added to hydrogen peroxide (H²0²), a vigorous reaction occurs and oxygen gas is evolved. This experiment investigates the effect of temperature on the rate at which the enzyme works by measuring the amount of oxygen evolved over a period of time. The experiment was carried out varying the temperature and recording the results. It was then repeated but we removed the catalase (potato) and added Lead Nitrate in its place, we again tested this experiment at two different temperatures and recorded the results. Once all the experiments were calculated, comparisons against two other groups were recorded.
The temperature of amylase The temperature of starch Room temperature Concentration Ph values The variable I will be changing is the volume of amylase. Safety: The sand is To make sure I carry out this experiment safely I will make sure I wear a pair of goggles. I will ensure I keep my stool under the table and all
Investigating the Effect of Enzyme Concentration on the Hydrolysis of Starch with Amylase Aim: Investigate the effect of enzyme concentration on the rate of an enzyme-controlled reaction. Using amylase and starch as my example. Introduction: I am investigating the effect of the concentration of the enzyme, amylase on the time taken for the enzyme to fully breakdown the substrate, starch to a sugar solution. The varied variable will be the concentration and all other variables are going to be fixed. The different concentrations will be: 0.5% 0.75% 1.0% 1.5% 2% An enzyme is a class of protein, which acts as a biological catalyst to speed up the rate of reaction with its substrates.
The results of this experiment showed a specific pattern. As the temperature increased, the absorbance recorded by the spectrophotometer increased indicating that the activity of peroxidase enzyme has increased.At 4C the absorbance was low indicating a low peroxidase activity or reaction rate. At 23C the absorbance increased indicating an increase in peroxidase activity. At 32C the absorbance reached its maximum indicating that peroxidase activity reached its highest value and so 32 C could be considered as the optimum temperature of peroxidase enzyme. Yet as the temperature increased up to 60C, the absorbance decreased greatly indicating that peroxidase activity has decreased. This happened because at low temperature such as 4 C the kinetic energy of both enzyme and substrate molecules was low so they moved very slowly, collided less frequently and formed less enzyme-substrate complexes and so little or no products. Yet, at 23 C, as the temperature increased, enzyme and substrate molecules
Influence of Temperature on the Activity of Potato Catalase Hypothesis That the higher the temperature the higher the reaction rate of potato catalyse to a point were denaturing occurs in the enzyme and the reaction rate of the potato catalase drops off. Prediction The rate of Catalase activity will be faster at higher temperatures until a point, because at higher temperatures there are more chances of collisions between the enzyme's (Catalase) active site and the substrate (hydrogen peroxide). However the rate depends on the active site being able to join with the substrate, and at higher temperatures the enzyme can be denatured, which changes the shape of the active site which thus prevents the reaction from happening. At first, as the temperature increases the activity of the Potato catalase also increases this is because the collision rate of the enzyme with the hydrogen peroxide is increased.
Abstract: Enzymes are catalysts therefore we can state that they work to start a reaction or speed it up. The chemical transformed due to the enzyme (catalase) is known as the substrate. In this lab the chemical used was hydrogen peroxide because it can be broken down by catalase. The substrate in this lab would be hydrogen peroxide and the enzymes used will be catalase which is found in both potatoes and liver. This substrate will fill the active sites on the enzyme and the reaction will vary based on the concentration of both and the different factors in the experiment. Students placed either liver or potatoes in test tubes with the substrate and observed them at different temperatures as well as with different concentrations of the substrate. Upon reviewing observations, it can be concluded that liver contains the greater amount of catalase as its rates of reaction were greater than that of the potato.
However, the decrease varied depending on the temperature. The lowest temperature, 4 degrees Celsius, experienced a very low decrease of amylose percentage. Temperature at 22 degrees Celsius and 37 degrees Celsius, both had a drastic decrease in amylose percentage. While the highest temperature, 70 degrees Celsius, experienced an increase of amylose percentage. In conclusion, as the temperature increases the percentage of amylose decreases; however, if the temperature gets too high the percentage of amylose will begin to increase. The percentage of amylose increases at high temperatures because there is less enzyme activity at high temperatures. However, when the temperature is lower, more enzyme activity will be present, which results in the decrease of amylose percentage. This is why there is a decrease of amylose percentage in 4, 22, and 37 degrees Celsius. In this experiment the optimal temperature is 37 degrees Celsius, this is because this is the average human body temperature. Therefore, amylase works better at temperatures it is familiar
I blanked it with 2 cm³ water, 1 cm³ amylase and 3 drops of iodine.
The pH of the solution would alter the rate of the reaction if it was
Researchers then hypothesized that the results would indicate the greatest amount of potato enzyme activity level will take place at room temperature. In this experiment, researchers used potato extract and different temperature levels to test the hypothesis. Moreover, researchers wanted to test the color intensity scale and how specific catechol oxidase is for catechol. In this experiment, researchers used dH2O, catechol solution, hydroquinone, and potato extract. Lastly, researchers tested the substrate concentration and how it has an effect on enzyme activity.