Kmax For An Enzymatic Reaction Lab Report

axis at the terminal portion of the curve. The spirometry does show only a 61%

The optimum pH level would be pH 7. This is because this is where the highest amount of enzyme activity is taking place.

2. We measured 1 mL of turnip peroxidase (the enzyme) and 3 mL of neutral buffer (pH corresponding to the test tube number i.e. pH 5 in test tube 5) with a syringe and disposed it into tubes 3, 5, 6, 7, 8, and 10

7. The kinetic graph was correct as my hypothesis. My potential graph did not start in the same position as my data graph.

3) What do the rate of change values you just calculated represent? Why are some positive and some negative?

To improve the results from the experiment buffer solutions that were not whole pHs could have been used e.g. pH 4.5, 5.5 etc. This would have provided more reliable results as a wider range of results would have been produced. Using pHs with decimals would also help to more accurately determine the optimum pH as the optimum may have been above or below the pH stated in the hypothesis; 8. In this experiment however the optimum is taken at 8 because the graph does not rise again.

After getting the results of the 5 different concentrations using the formula c=A/εl (Lambert-Beer Law). So a new graph was created using the concentration plotted versus the time (s). The final rates of the reactions for the five different trial were first trial was 0.5 mM/s , second trial 0.3 mM/s , third trial 0.05 mM/s , fourth trial 0.03 mM/s , and for the fifth was 0.005 mM/s. the final result of the curve line was not that accurate because of the trial 4th that was a little off.

Enzymes are catalysts that function to speed up reactions; for example, the enzyme sucrose speeds up the hydrolysis of sucrose, which breaks down into glucose and fructose. They speed up reactions but are not consumed by the reaction that is taking place. The most important of the enzyme is the shape as it determines which type of reaction the enzyme speeds up. Enzymes work by passing/lowering and energy barrier and in doing so; they need to bind to substrates via the active. Once they do, the reaction speeds up so much more quickly than it would without the enzyme. Coenzymes and cofactors aid the enzyme when it comes to binding with the substrate. They change the shape of the active site so the substrate can bind properly and perform its function.

Purpose To determine the temperature at which the potatoes catabolic enzymes breakdown H2O2 (hydrogen peroxide) the fastest. Hypothesis If the temperature of the H2O2 is 35.7 degrees Celsius, then it will break down the fastest because that is the temperature enzymes work in the human body Materials -Ice Bath -Observation

Enzymes are molecules that accelerate the rate of a reaction through the lowering of the activation energy necessary to perform the reaction without their presence. Depending on the environment that the enzyme is in, determines how efficient the enzyme will be in accelerating the reaction. Factors such as pH and temperature play a role on the enzyme’s efficiency and overall success of the reaction. For example, having a high temperature can break apart non-covalent interactions within proteins—the most common form of an enzyme. The breaking down of these bonds would result in the enzyme having a conformational change that does not allow the substrate to fit into its active site. In our experiment, we used the enzyme cellobiase in order to study

An enzyme is a biological catalyst that speeds up the rate of reaction in certain biological functions. They play a vital role in many aspects of human physiology and are necessary for the functioning of a number of systems, for example in the digestive system to help to break down food. All enzymes have a unique active site that can fit on to a particular molecular arrangement on a target substrate; a substance e.g. carbohydrate, protein, or fat, that the enzyme is designed to breakdown. There are a number of different enzymes in the human body; each type produced specifically to perform a certain role. Enzymes are not themselves destroyed in the reaction to break down a

First, we can talk about error in the standard curve made which could be related to measurements of the absorbance leading to the equation of the straight line that could affect all of the calculations. Another source of error, as mentioned before, could be in the choice of the alkaline phosphatase concentration in B. Choosing a concentration that is not very accurate would have affected part C in the experiment. As of what concerns future improvements of this experiment, more standard dilutions could be used to generate the standard curve so that there is a wider range of values of concentrations of PNP for a more accurate conversion from absorbance values to PNP concentration values along the experiment. Furthermore, in part B and C more alkaline phosphatase dilutions and more PNPP dilutions could be prepared for the same reason: providing a wider range of values and therefore more accuracy in calculations. An addition area of improvement could also be related to the preparation of alkaline phosphatase in the first, trying to make a preparation that is as pure as possible for a higher value for the specific activity.

From Figure 4, the maximum velocity is the highest point on the curve and the constant (km) is ½ the maximum velocity. However, it is difficult to estimate Vmax using Michaelis-Menten curve with precision since the limits of the hyperbolic curve deviate at varying concentrations of the substrate. The data can be linearized using Lineweaver-Burk Plot to obtain Vmax and Km as follows: Slope=Km/V_max

Although we might not always acknowledge this small proteins, enzymes have come to be revolutionary when it comes to our survival. This is because enzymes are an example of catalysts, which affect the rate at which a chemical reaction occurs by speeding up. Moreover, this is imperative for our survival because chemical reactions provide the energy required by our bodies to perform several life processes that allow us to carry out many of the activities we perform as part of our everyday life. Thus, an enzyme's ability to function properly has become a major factor in our body's ability to function properly and maintain homeostasis. Unfavorably, however, there are some factors that can negatively affect an enzyme's ability to

THE EFFECT OF TEMPERATURE ON THE RATE OF ENZYME ACTIVITY DB-16-0081 Co-partner: TIMORE NURDINOV Introduction The aim from this experiment is to observe the effect of factors such as pH, temperature and inhibitor on enzyme activity and how it works.