This graph shows that as enzyme concentration increases absorption also increases. In this case absorbance can be used to measure the enzyme’s activity, the higher the absorption the higher the activity. Since absorption increases as enzyme concentration increases, enzyme activity is promoted by increased enzyme concentrations. After a certain point enzyme activity would fail to increase as a result of increased enzyme concentration since there wouldn’t be enough substrate for all of the enzymes to react with. My results did not completely support my hypothesis, while I was correct about pH, temperature, enzyme concentration and inhibitors I was incorrect about substrate concentration. I originally believed that increasing substrate concentration …show more content…
Test tube 2 was the control, in this tube the enzyme was absent, and the purpose of controls are to set a baseline to see if other factors impact the result. Another control that could have been added would be a test tube that has the substrate absent and is the enzyme alone. Tyrosinase does display substrate specificity since it was able to react with the substrate. The optimal temperature appears to be slightly above room temperature for this enzyme. The reaction occurred more slowly at lower temperatures because the particles in the solution are slowing down and aren’t colliding as frequently, in the higher temperatures it slows down because the enzyme is getting denatured, this effect becomes larger as temperature increases. Changing the concentration of enzymes has a direct impact on the enzyme activity. When enzyme concentration increases so does enzyme activity, and when enzyme concentration decreases so does enzyme activity. Enzyme activity and enzyme concentration are directly proportional up until a certain point where increased concentration will have no effect on enzyme …show more content…
These conditions aren’t the same for every enzyme, for example some enzymes may have a higher tolerance for heat and may not become denatured at the temperatures where tyrosinase became denatured. Since enzymes can only properly operate under certain environmental condition it is extremely important for organisms to provide those conditions in order to maintain their functions. Organisms as a result are limited to what they can ingest and where they can live, for example ingesting an extremely basic or acidic solution could cause enzymes in a stomach to not operate
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
Catecholase is an enzyme formed by catechol and oxygen used to interlock oxygen at relative settings, and it is present in plants and crustaceans (Sanyal et. al, 2014). For example, in most fruits and vegetables, the bruised or exposed area of the pant becomes brown due to the reaction of catechol becoming oxidized and oxygen becoming reduced by gaining hydrogen to form water, which then creates a chain that is is the structural backbone of dark melanoid pigments (Helms et al., 1998). However, not all fruits and plants darken at the same rate. This leads to question the enzymatic strength of catecholase and how nearby surroundings affect its activity. The catecholase enzyme has an optimal temperature of approximately 40°C (Helms et al., 1998). Anything above that level would denature the tertiary or primary structure of the protein and cause it to be inoperable. At low temperatures, enzymes have a slower catalyzing rate. Enzymes also function under optimal pH level or else they will also denature, so an average quantity of ions, not too high or low, present within a solution could determine the efficiency of an enzyme (Helms et al., 1998). Also, if more enzymes were added to the concentration, the solution would have a more active sites available for substrates and allow the reaction rate to increase if excess substrate is present (Helms et al., 1998). However, if more
There is an optimum temperature that enzymes have for maximum productivity and its rate of reaction. This temperature is usually not that far away from the temperature of the body or room temperature. But, when the temperature is substantially reduced, like being in the ice bucket for ten minutes, this usually reduces the productivity of the enzymes. Similar to the experiment, it takes more time for the same amount of work when the temperature is severely decreased. So, an increase in temperature increases the reaction rate of enzymes. But, there is also an upper limit to the factor of temperature. After a certain temperature, the extreme heat can be harmful for the enzymes and can cause denaturation, as bonds in the enzymes can break and can change the shape of the enzyme. So, extreme low and high temperatures has a decreasing effect on the activity and reaction rate of
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
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
Test-tube C had the best concentration according to the results. Three test-tubes were labelled A-C. Test-tube A had 1ml enzyme solution which was added to test-tube B which had 4ml buffer (pH 5 was used). 1ml of the solution from test-tube B was then added to the test-tube C which also had 4ml buffer (pH 5). Test-tube C was used as the enzyme in all the reactions. Nine test-tubes were taken out of them one was used as the the blank, labelled as test-tube 9. The blank had 5ml buffer (pH 5), 2ml hydrogen peroxide, 1ml guaiacol and no enzyme. Then, 3ml of buffer (pH 3) and 2ml of enzyme were added to test-tube 1. Test-tube 2 had 2ml hydrogen peroxide and 1ml guaiacol. Test-tube 1 and 2 were mixed. The same procedure was used for test-tube 3 as test-tube 1, but this time the buffer was pH 5. Test-tube 4 was prepared the same way as test-tube 2. Then, Test-tube 3 and 4 were mixed. Test-tube 5 was prepared as test-tube 1 but with buffer of pH 7 and test-tube 6 was prepared as test-tube 2. Next, test-tube 5 and 6 were mixed. Last but not the least, test-tube 7 was prepared as test-tube 1 but with buffer of pH 9 and test-tube 8 was prepared as test-tube 2. Then, test-tube 7 and 8 were mixed. The spectrophotometer was set to 470nm and using the blank it was set to zero. The four test-tubes with different pH’s (pH 3, pH 5, pH 7, pH 9) were read
In biology class, we were learning about enzymes. Enzymes are proteins that help catalyze chemical reactions in our bodies. In the lab, we were testing the relationship between the enzyme catalase and the rate of a chemical reaction. We predicted that if there was a higher percentage of enzyme concentration, then the rate of chemical reaction would increase or it would take less time. We placed 1 ml of hydrogen peroxide into four depressions. Underneath the first depression, we place 1 ml of 100% catalase and make 50% dilution with 0.5 ml of water. We take 50% of that solution and dilute with 0.5 ml of water and we repeat it two more times. there were four depressions filled with catalase: 100%, 50%, 25% , 12.5 % with the last three diluted
The Vmax values, as determined from the Lineweaver-Burk plot, for the uninhibited, half uninhibited, and inhibited enzymes were, 0.3647, 0.1262, and 0.3087 μmol/min respectively. The non-linear regression V¬max¬ values for the same enzyme were 0.3343 (9.09% error as compared to Lineweaver-Burk plot), 0.1264 (0.16% error), and 0.2694 μmol/min (14.6% error) respectively. The differences in the values are due to the presence of error introduced by a Lineweaver-Burk plot, where data points at higher and lower substrate concentrations are weighed differently (Tymoczko, p.115). This error is the reason why a Michaelis-Menten plot is preferred.
...e substances at 37.5̊C due to the fact that in the previous experiment, this was found to be the optimum temperature that catalase reacts at. It was because of this constant that I used the set of data of the catalase at 37.5̊C from the first experiment to provide a neutral environment for the experiment. The way in which the data was collected for the first experiment was identical to that needed to be done by the second. From this data, it was determined that the neutral environment for the catalase had the best results, which makes it clear that when the enzyme is in a pH of the opposite extremes such as basic or acidic, it is un able to function properly. When it is too basic then the enzyme will become inactive and when the enzyme is too acidic then the enzyme will denature, both rendering it unable to function at its optimum efficiency that all enzymes need.
This is evident as the average gradient for 0.5% catalase concentration is 0.067%/s and the average gradient of 4% catalase concentration is 0.315%/s. The rise of oxygen production has occurred because as the hydrogen peroxide is added to the varying levels of concentration of catalase. The solution with the highest enzyme concentration will yield the most activity, thus producing more oxygen gas ("Enzyme Investigation. How Does The Concentration Of Hydrogen Peroxide Affect The Amount Of Oxygen Produced By The Enzyme Catalase? - International Baccalaureate Biology - Marked By Teachers.Com"). This assumption is based on scientific theory, which states an increase in enzyme concentration will also increase the chances of substrate-enzyme binding.("General Principles - Chemwiki") An example of this is the average R2-value for 1% catalase solution was 0.090%/s and the average R2- value of the 2% catalase solution was 0.094%/s. This indicates a strong positive correlation, meaning that as x increases (catalase concentration), y also increases (rate of oxygen
The enzyme will drastically slow down activity due to cold temperatures of 24°C. Just like the energy stored in human and plant organisms. If cells are under a certain temperature within living things, the ability to function will not hit equilibrium but will slow down the rate of chemical reaction. It is clear that room temperature is where we will see most of the activity. This is part of the reason why homeostasis is important to living organisms – because homeostasis is the process to maintain internal temperatures so that the structure and function can work properly. The catalase enzyme vs. hydrogen peroxide delivered clear results that environmental factors can alter enzyme activity. That being said our hypothesis was accepted based on the prediction that heat will denature the enzyme while the activity of cold and room temperatures will still have a reaction. This hypothesis could have wrong if other factors were involved such as, if we let them sit for a long period of time or if there were more temperatures involved. In conclusion, later on we may want a larger form of data by including the class results but as of now this experiment went well and confirmed our
Mainly because different enzymes have different pH, and temperatures that they act on with. Adding more substrate can causes the enzyme to increase in activity. In the experiment you have ethanol who worked best with the changes of ph and temperature, whereas methanol was not so successful with the changes. The four alcohols each had the same reaction group but each had different chain length. Ethanol has a 2 chain length, Propanol 3, Methanol 1, and Butanol 4. As you can see in graph 2, the preferred alcohol was ethanol and the least preferred was methanol. You see this because ethanol has the highest absorbance and methanol has the least. The size of the substrate can determine how quickly the enzymes is able to recognize
Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is important that a specific enzyme is present during the process. For example, lactase must be able to collaborate with lactose in order to break it down (Madar & Windelspecht, 105).
In this lab, it was determined how the rate of an enzyme-catalyzed reaction is affected by physical factors such as enzyme concentration, temperature, and substrate concentration affect. The question of what factors influence enzyme activity can be answered by the results of peroxidase activity and its relation to temperature and whether or not hydroxylamine causes a reaction change with enzyme activity. An enzyme is a protein produced by a living organism that serves as a biological catalyst. A catalyst is a substance that speeds up the rate of a chemical reaction and does so by lowering the activation energy of a reaction. With that energy reactants are brought together so that products can be formed.
Enzymes are protein molecules that are made by organisms to catalyze reactions. Typically, enzymes speeds up the rate of the reaction within cells. Enzymes are primarily important to living organisms because it helps with metabolism and the digestive system. For example, enzymes can break larger molecules into smaller molecules to help the body absorb the smaller pieces faster. In addition, some enzyme molecules bind molecules together. However, the initial purpose of the enzyme is to speed up reactions for a certain reason because they are “highly selective catalysts” (Castro J. 2014). In other words, an enzyme is a catalyst, which is a substance that increases the rate of a reaction without undergoing changes. Moreover, enzymes work with