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Effects of pH on enzyme activity
Yeast fermentation lab report introduction
The effect of changing temperature on enzyme activity
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Enzyme Lab Report
Kyle Zalatar
Sach Dubey
Brandon Chen
Damon Che
Dougherty Valley High School
Abstract
The purpose of this experiment was to witness how enzymes act in different conditions for instance how enzymes would react in different temperatures or a different ph level.We found that any temperature which is not the standard for the enzyme will lower the productivity. For the first lab we represented our hands as catalysts and we were connecting pop beads blindley to record how effective we were, in the second trial we put on gloves to simulate how enzymes react in different temperatures, we found out enzymes are less productive in different temperatures. The second lab was more literal we used yeast as our enzyme and we put paper
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This experiment also needed 4 students, one being in charge of the yeast, another being in charge of the solutions and stirring rod, another one being the timer, and the last student writing down data. In order to make the filter paper float up to the top, there were twenty holes punched and the tweezers were used to pick up one piece at a time and soaked in the yeast for 5 seconds each time. After the paper was taken out of the yeast, it was transferred onto the stirring rod and pushed all the way to the bottom of the test tubes and used the timer to measure how long it took to float back up. This was done five times to all three different pH waters and calculated the average of each one to get better …show more content…
The claim stated that the reaction rate of an enzyme will decrease when the pH is changed. The data(see Table 1) supports this hypothesis. The reaction rate of the enzyme decreased when the pH was affected. After 180 seconds of testing, the number of Pop Beads metabolized dropped from 31 in normal conditions to 8 when affected by a change in pH. Secondly, in the yeast lab, the data taken displays the effects of temperature, pH, and concentration on the reaction rate of catalase. The claim stated that changing these variables will result in a decreased rate of reaction. The data refutes this claim. Over the course of five trials, the reaction rate of catalase did not decrease after manipulating variables of temperature, pH, and concentration(see Table 2). This is evident because the time it took for the paper to rise did not decrease at all when variables were
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
For example, substrate concentration, enzyme concentration, and temperature could all be factors that affected the chemical reactions in our experiment. The concentration of substrate, in this case, would not have an affect on how the bovine liver catalase and the yeast would react. The reason why is because in both instances, the substrate (hydrogen peroxide) concentration was 1.5%. Therefore, the hydrogen peroxide would saturate the enzyme and produce the maximum rate of the chemical reaction. The other factor that could affect the rate of reaction is enzyme concentration. Evidently, higher concentrations of catalase in the bovine liver produced faster reactions, and the opposite occurs for lower concentrations of catalase. More enzymes in the catalase solution would collide with the hydrogen peroxide substrate. However, the yeast would react slower than the 400 U/mL solution, but faster than the 40 U/mL. Based on this evidence, I would conclude that the yeast has a higher enzyme concentration than 40 U/mL, but lower than 400
Catalase is a common enzyme that is produced in all living organisms. All living organisms are made up of cells and within the cells, enzymes function to increase the rate of chemical reactions. Enzymes function to create the same reactions using a lower amount of energy. The reactions of catalase play an important role to life, for example, it breaks down hydrogen peroxide into oxygen and water. Our group developed an experiment to test the rate of reaction of catalase in whole carrots and pinto beans with various concentrations of hydrogen peroxide. Almost all enzymes are proteins and proteins are made up of amino acids. The areas within an enzyme speed up the chemical reactions which are known as the active sites, and are also where the
Input variables In this experiment there are two main factors that can affect the rate of the reaction. These key factors can change the rate of the reaction by either increasing it or decreasing it. These were considered and controlled so that they did not disrupt the success of the experiment. Temperature-
One of the most primitive actions known is the consumption of lactose, (milk), from the mother after birth. Mammals have an innate predisposition towards this consumption, as it is their main source of energy. Most mammals lose the ability to digest lactose shortly after their birth. The ability to digest lactose is determined by the presence of an enzyme called lactase, which is found in the lining of the small intestine. An enzyme is a small molecule or group of molecules that act as a catalyst (catalyst being defined as a molecule that binds to the original reactant and lowers the amount of energy needed to break apart the original molecule to obtain energy) in breaking apart the lactose molecule. In mammals, the lactase enzyme is present
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
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
Jim Clark. (2007). The effect of changing conditions in enzyme catalysis. Retrieved on March 6, 2001, from http://www.chemguide.co.uk/organicprops/aminoacids/enzymes2.html
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 blended on high to make the potatoes more liquid-like. I grabbed the cheesecloth and placed on the top of the blender. I poured the potato extract on the container and labeled it. I found out that I have to make 1% sugar solution so I grabbed the sugar and measured into 5 grams on the scale. I added 5 grams of sugar on 250 ml graduated cylinder and poured the water into the cylinder. I mixed the sugar with water and poured it into the saucepan. I refilled the water into the graduated cylinder and poured into the saucepan. I turned on the heat of the stove and saw the sugar dissolved. I poured into a container and labeled 1% sugar solution. I repeated the same thing with 1% salt solution by using 1 gram of salt and filled the water into graduated cylinder by 100 ml. I answered question three. In the first experiment, I grabbed four transfer pipets and used it to put solutions into the test tubes by 3ml. I labeled it and placed into the plastic cups so it can stand upright. I grabbed each test tube and poured 2 ml of catalase solution into it. I also tapped and swirled to measure the bubbles by using the ruler. I wrote the numbers into the lab report. In the second experiment, I labeled the room
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.
Introduction / Background Information. This is an experiment to examine how the concentration of the substrate Hydrogen Peroxide (H2O2) affects the rate of reaction of the enzyme Catalase. In this experiment I will be using yeast as a source of catalase. Enzymes are catalysts which speed up specific reactions. Enzymes such as catalase are protein molecules, which speed up a specific reaction within the cell.
Planning Firstly here is a list of equipment I used. Boiling tubes Weighing scales Knife Paper towels 100% solution 0% solution (distilled water) measuring beakers potato chips Cork borer. We planned to start our experiment by doing some preliminary work. We planned to set up our experiment in the following way.
more carefully and so I can get an idea of what's going to happen. I
Their table had 15 mL glucose, 10 mL RO water, and 10 mL of yeast which they then placed in an incubator at 37 degrees Celsius. In conclusion, I feel that the absence of RO water in the flask made the enzymes work a little harder than when the RO water was in the mixture of the flask. Comparison #4 is between the Controlled Table and Table #5. The mixture for that table’s flask was 15 mL Sucrose, 10 mL of RO water and 10 mL of yeast, which the flask was then placed in an incubator at 37 degrees Celsius.