Enzyme Lab ReportNovember 3, 2017
In your own words, define objective qualitative and objective quantitative data. There are two different types of information that can be obtained from research. The types of Information that can be obtained are quantitative and qualitative data. Research results are considered qualitative when the results can be answered with a simple statement of yes or no. Qualitative data does not attempt to give a numerical value; instead it gives very little detail about data.
An example of qualitative data loud be a simple pH test and stating if a solution is acidic or basic without stating the pH numerical value. On the other hand, quantitative data assigns a value to the answer. Quantitative data is the type of information that provides more detail. Number values and units matter when giving a quantitative analysis. For example, If a pH=8. 44, the actual numerical value Is considered quantitative data. 2. Referring to the experiments on the effect of pH on enzyme activity, respond to the following Items pertaining to those experiments: (11) Write a 1 paragraph explanation that includes the following
Purpose and components of experiment How the Benedicts test measures the activity of reducing agents. How the Benedicts test was used to measure sucrose activity including qualitative and quantitative measures. Write a I-paragraph explanation of how PH affects ALL PROTEIN-BASED enzyme structure and function. The motivation to use the Benedicts test was to depict sucrose’s level of activity at various pH’s and explain how pH directly relates to the presence of the reducing agent of sucrose.
The amount of sucrose that Is detected Is directly related to the mount of sucrose converted to glucose and fructose. In order to adequately collect useful data; creating a numerical value scale as quantitative data directly relates to the color change results from the benedicts test. The building blocks of this pH experiment are having the enzyme at a specific indicted pH level and using the Benedicts test to reduce the sugar agents. The catalyst at a certain pH will impede the spontaneous reaction from occurring faster or slower depending on the pH of the that during the spontaneous reaction, there is a release of free energy.
The reaction approached equilibrium the fastest shown by qualitative data from the Benedicts test when the solution turned blue to red. The qualitative and quantitative data show that the transition state for the coercing reaction is the same point the sucrose was equal to the amount of sucrose converted. The rate of a particular reaction depends on the actual path through which the reactants are transformed to products. There are optimal conditions that are favored by enzymes where it becomes most active. At a certain pH level, the enzyme pushes the reaction to equilibrium without affecting the reactions change of G.
Accelerating the reactants to the unstable form in the transition state in effort to break bonds and form new bonds by releasing free energy to surroundings is the Job of an enzyme. The amount of reducing agents detected by the Benedicts test directly relates to the importance of pH for all protein enzymes. PH effects how fast a reaction with occur and increasing the likelihood that the reactants will interact productively. List of pH effects on enzymes: 1. Binding of substrate 2. Unionization state of amino acid group 3. Unionization of substrate 4.
Protein structure variation at certain pH’s . Enzymes require weak intra-molecular bonds (e. G. , hydrogen bonds, ionic bonds, and hydrophobic interactions) to stabilize their functional, three-dimensional structure. In addition, in any system, the ability of the Enzyme and Substrate to interact and therefore react is determined by the energy within that system. Based on these facts and your knowledge of protein structure, EXPLAIN, at the molecular level, the observed changes in enzyme activity at each of the temperatures used in lab exercise.
DO NOT INCLUDE SPECIFIC DATA POINTS OR A DESCRIPTION OF THE GRAPH. (10) When the environmental temperature is increased, the intermolecular atomic vibrations greaten, consequently breaking weak hydrogen and ionic bonds of the enzyme. More importantly, up to a certain point, the rate of an enzymatic reaction increases with higher temperatures because the substrates become more active and collide more often. Once the enzyme hits its peak of reaction rate, any temperature past that point will sustain a sudden drop in speed of the enzymatic reaction.
At low temperatures the rate of the reaction is low to no reaction at all. For example, if sucrose would take years to hydrolysis at room temperature. But when optimal temperature is reached, that means the reaction rate is at its peak. Higher temperatures agitate hydrogen bonds, ionic bonds that usually stabilize the shape of a protein enzyme such as sucrose, but when optimal temperature is reached, all protein molecules become denatured. At the reaction rate in which optimal temperature is found, all proteins are experiencing the same reaction.
The reaction that happening in simple explanation is the largest number of molecular collisions is occurring while at the same time being considered the fastest path to converting the reactants to product molecules. After the optimal temperature, temperatures higher reaction rate. 4. The amylase experiment used changes in transmittance to monitor enzyme activity. Write 1-3 sentence paragraph describing of the components and purpose of the experiment.
In a 1 sentence paragraph, state whether he rate of transmittance change is directly or inversely related to the amylase The main component at this part of the experiment is amylase. Amylase is a natural enzyme found in saliva that hydrolysis starch and glycogen into smaller pieces of polysaccharides. The overall purpose of this experiment is to measure the absence of amylase that indirectly relates to the enzyme activity with amylase. The use of spectrophotometer measures the amount of color loss in our solution and the color loss directly relates to how much amylase is present in our solution.
The spectrophotometer measures transmittance, which is how much light is transmitted in a sample. Since amylase is clear after conducting the Iodine test, the solution will have a higher transmittance amount. Some solutions have higher transmittance percentages because of being clearer such as amylase. The rate of transmittance change is indirectly measures the relationship of amylase and amylase, the substrate. 5. Referring to the graph on the Effect of Enzyme Concentration on Amylase Activity, direct relationship between Enzyme Concentration and Reaction Rate would be a straight line with a positive slope.
Explain why the observed and expected results differ for this experiment. Note: There are 2 possible reasons, both concern the limitations imposed by the design of the experiment. Include a brief explanation of the EXPECTED direct relationship between Enzyme Concentration and Reaction Rate FIRST before discussing your 2 reasons for the OBSERVED data. The expected direct relationship between the Enzyme concentration and reaction rate is a linear slope because that is predicted from calibrated substrate concentrations that are constant.
In a perfect situation, the rate of a reaction with enzymes involved will increase with increasing levels of substrate concentration levels. On the other hand, our observed data shows a steep slope followed by a gradual leveling off. In both the expected and observed graphs, both have an increase in reaction rate when more substrate concentration is added. But the reaction rate changes in the presence and absence of enzymes. So our expected slope is gradual with out enzymes while our observed data shows a steep slope until the enzymes are completely saturated in the solution, making the line on the graph level off.