Tube 2 Lab

Concentration values were greatly increased when the corresponding dilution factors were taken into account. Data for the concentrations determined using the standard curve and final concentrations are listed in Table 5

Figure 5. Effect of Cold Temperature (2 degrees C) of Vmax. This shows Tubes 3 and 4 as increasing, while the remaining tubes seemed to have been denatured.

This experiment supported the hypothesis that the stronger the concentration, the more efficient the enzyme catalysed chemical reactions. .As time continued, the amount of substrates that needed to be bind with an enzyme was reduced because most of the milk fats had been converted in to fatty acids, which then caused the rate of reaction to slow down as it was harder for the remaining substrates to collide with the enzyme. This means the moment where the reaction is the most effective is at the beginning, when the lipase solution was just added to the milk, which is known as the Initial Reaction Rate. This is reaction is displayed in graph 3, as all on the lines have a steep gradient at the begging of the test, which then begin to plateau towards the end of the reaction when the solution became colourless. It’s interesting that the 2% concentration had a higher initial reaction rate than the 4%

Enzymes quicken chemical reactions in a cell. This experiment was performed in order to determine if adding NaCl to an enzyme would have an effect on the rate of the reaction of the enzyme. It is said that salt inhibits the reaction the reaction rate of enzymes. It can inhibit reactions making the protein unstable or by also messing with the equilibrium constant of the substrate being catalyzed. In our experiment tube 1 consisted of 2.5% NaCl and was the only tube that reacted. This was due to the salt inhibiting all the other reactions. Though it does not effect the enzyme it effects the enzymes activity.

There was an increase in reaction rate as the substrate concentrations increased, for instance, at 2% substrate concentration the volume of oxygen obtained was 100ml in the duration of 2 minutes, whereas 6% was at an average of 200ml of oxygen obtained. This shows that as the different substrate concentrations were tested, the highest one which was 6% had the fastest reaction which was 90 ml per minutes compared to 2% which had a lower rate of reaction with 25 ml per minute. There is a hyperbolic relationship between the rate of reaction and the concentration of substrate, as shown in the graph. At low concentration of substrate, there is a steep increase in the rate of reaction with increasing substrate concentration, the catalytic site of the enzyme is empty, waiting for the substrate to bind. In addition, at the point of high substrate concentration, the enzyme activity is as high as it can be, this is known as the maximum velocity which is evident in the graph. This is the point in which all enzymes are bound to substrate and are turning them into products, most of the active sites are occupied so the rate of increase subsequently slows down. The rate of formation of product now depends on the activity of the enzyme, increasing the substrate concentration anymore has no effect on the rate of reaction as it has reached its maximum. As shown in the graph, it has reached its optimum at 190ml, with a reaction rate of 90 ml per minute. This shows that it has reached its optimum where enzyme activity does not increase any

The experiment was carried out to investigate the effects of the increase in the enzyme concentration on the rate of reaction. By using self investigative and experimental skills, the experiment was done in order to determine how the rate of reaction will be altered, whether it will increase, decrease or remain constant when the different concentration of enzymes added.

The purpose of this lab was to determine the affects of enzyme activity under specific temperature changes, pH values and substrate concentration. Since heat

If we viewed the slopes of the trials from figure 1 as the rates of enzyme activity, our results could be interpreted as the following: when in substrate concentration increased from a low concentration(for example, from test tube 1 to test tube 2), the rate of the enzyme activity increased with the increase in substrate concentration; but as the substrate concentration increased, the enzyme activity reached a constant rate where all the enzymes were saturated(slope=0), and increase in substrate concentration would have no effect on the activity rate. Also, the higher the initial substrate concentration is, the faster the activity rate reached the constant(for example, test tube 3 reached the constant rate 6

The purpose of this experiment is to measure the rate of catalase enzyme activity under different

The temperature, pH level, enzymes concentration, and substrate concentration can all affect the the enzymes. The spectrophotometer is an instrument used

For experiment two, the independent variable was changed to a pH buffer solution instead of salt concentration. The overall changes in absorbency are shown is figure 3. The solutions containing pH 4, pH 8, and pH 10 showed little to no change at the end of the 18 minute period; however the pH 6 solution absorbency changed drastically. It began with an absorbance of 2.5 at time zero and at 18 minutes it had an absorbance of 0.343. The stock tube with no enzyme, once again, showed no change. The enzyme could have become denatured at the other pH levels, which would have cause the lack of product being formed.

This experiment was carried out with many precautions to minimise error margins. These measures included using the same sample for all experiments, using the same apparatus for the repeated steps of the experiments, having the same person record the results, add substrate and enzyme. However there were still some results that were indicative of error which led to results that were substantially apart from the other

In additional, the observations of this experiment can be improved by adding 2-3 drops of detergent to each test tube, this would allow the foam suspension to be more prominent and therefore can be measured easier. Similar to the pH experiment if the observations were taken in equal time intervals the for example every minute it would be more accurate easier to deduce the rate of reaction of the enzyme. Other more minor sources of error experienced when measuring the effects of temperature on the pH of solution was systematic error in measuring the height of the foam suspension using a centimeter ruler, which like pH, introduced a (±0.5) degree of error. This can also be minimised through the use of a measuring cylinder, which would also minimise the chances of any solution being lost in transfer as it is all

As our experiment began, we crushed the lactase pill in a mortar and pestle and dissolved it in 4mL of phosphate buffer in a beaker. We let the solution sit for two minutes, then strained through a napkin that was slightly pushed into the new beaker so we could have our stock enzyme solution. Then, we took 1mL of the stock and added it to 9mL of phosphate buffer in a small flask to create 1/10 enzyme dilution. Again, we took 1mL of the 1/10 enzyme dilution and added to another flask filled with 9mL of phosphate buffer. We finally

The purpose of this experiment was to study the effects of enzyme concentration on catalase activity.