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Lab Report on How Temperature Affects Enzymatic Activity
The effect of temperature on enzyme activity
Effect of temperature on the rate of enzyme activity
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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 shape of the molecules is changing and so the enzyme molecules can no longer fit into the gaps in the substrate that they need to and therefore the enzymes have de – natured and can no longer function as they are supposed to and cannot do their job correctly. Changing the temperature: Five different temperatures could be investigated. Water baths were used to maintain a constant temperature. Water baths were set up at 40 degrees, 60 degrees and 80 degrees (Celsius). Room temperature investigations were also carried out (20 degrees). Using a Bunsen burner, tripod and beaker of water 100 degrees could also be tested and 0 degrees was tested by using ice. (I didn’t investigate the 80 degrees temperature). Fair test: Below is a list of things that were kept the same throughout the investigation: Volumes of lipase and milk (by using syringes); volumes of phenolphthalein and sodium carbonate (using pipettes); (best volumes from the preliminary work were used). Each temperature was repeated three times to get a good average. The milk and lipase were equilibrated to the right temperatures before the lipase was added to the milk. Equipment list: Test tubes were used to hold the milk, the lipase and the milk and lipase solutions. Test tube racks were used to hold the test tubes
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.
2. A test tube was then filled with 35ml of yeast and placed in the
The procedure of the lab on day one was to get a ring stand and clamp, then put the substance in the test tube. Then put the test tube in the clamp and then get a Bunsen burner. After that put the Bunsen burner underneath the test tube to heat it. The procedure of the lab for day two was almost exactly the same, except the substances that were used were different. The
When this substrate fits into the active site, it forms an enzyme-substrate complex. This means that an enzyme is specific. The bonds that hold enzymes together are quite weak and so are easily broken by conditions that are very different when compared with their optimum conditions. When these bonds are broken the enzyme, along with the active site, is deformed, thus deactivating the enzyme. This is known as a denatured enzyme.
Animal metabolism consists of the utilization of nutrients absorbed from the digestive tract and their catabolism as fuel for energy or their conversion into substances of the body. Metabolism is a continuous process because the molecules and even most cells of the body have brief lifetimes and are constantly replaced, while tissue as a whole maintains its characteristic structure. This constant rebuilding process without a net change in the amount of a cell constituent is known as dynamic equilibrium (Grolier1996). In the combustion of food, oxygen is used and carbon dioxide is given off. The rate of oxygen consumption indicates the energy expenditure of an organism, or its metabolic rate (Grolier1996).
This happens when the temperature is too high; the process is called “denaturing”. When an enzyme reaches a certain temperature, it will have so much energy that it is de-shaped; it is “denatured”. This diagram shows how a denatured enzyme will not work: [IMAGE] The enzymes will hardly work at very low temperatures (they wont be
I then used the analysis function within data loggers to calculate the gradient of the steepest part of the graph, this was a much more accurate method and the results are given below. Results = == == == Rate of Fat Hydrolysis (pH per Sec) % Concentration of Lipase Repeat 1 Repeat 2 Repeat 3 Average 1 -0.01 -0.01 -0.0100 2 -0.01 -0.01 -0.01 -0.0100 3 -0.02 -0.02 -0.01 -0.0167 4 -0.05 -0.06 -0.06 -0.0567 5 -0.03 -0.06 -0.06 -0.0600 Due to insufficient time a repeat for the 1% lipase could not be carried out, the first repeat for the 5% lipase (highlighted) looks to be anomalous so I have not included it when calculating the averages.
placed in each tube. Each tube was then placed in a water bath of the
Measuring cylinder to measure small amounts of fluids. Pipette to gather small amounts of fluids. Test tube holder to hold test tubes. 2. Molar Salt solutions to submerge potato chips in.
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
Changes in pH lead to the breaking of the ionic bonds that hold the tertiary structure of the enzyme in place. The enzyme begins to lose. its functional shape, particularly the shape of the active site, such. that the substrate will no longer fit into it, the enzyme is said to. be denatured.
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
The Effects of Temperature on the Rate of Clotting Milk and Rennet Introduction ------------ The following experiment investigates the effects of different temperatures on a mixture of rennet and whole milk. On having the choice between testing the mixtures reactions at various temperatures, or testing the mixture with various amounts of concentration of rennet, my partner and I decided upon the first option. We made this decision as we felt it would be valuable to our scientific knowledge if we had a better understanding of how different temperatures can effect the behaviour of an enzyme, such as Rennin, which is also known as Chymosin. Our scientific knowledge tells us that enzymes work most efficiently at specific temperatures, and this experiment helps us to discover exactly which temperatures they are.
The pH of the solution would alter the rate of the reaction if it was
5 test tubes were prepared for dilution respectively to 5 spec tubes that had the inhibitor and water and ready for the enzyme addition. Recordings were done every 60 seconds for 3 minutes. Reaction rate was then calculated after time ended. After having used the inhibitor, the steps were repeated but replace the inhibitor with water as control and experimented for the rates without the inhibitor. Percentages were graphed by the percentage inhibition versus the substrate concentration for the inhibitor. Part 5 of the experiment was to determine the effect of temperature or pH on the reaction rate. In doing so, each group in the lab was designated a particular enzyme that was exposed in different temperatures (Schultz, 2006). The enzymes were exposed before the beginning of the experiment into these different temperatures: boiling, warm (heat), room temperature, cold (ice bath), and frozen. Each enzyme was allowed back to room temperature before adding the buffered catechol with the 1 ml of enzyme into the spec tube (Schultz, 2006). Reaction rate was then determined from the reading. Absorbance versus time was plotted with the determined initial rate of each