Rennin Lab Report

I put one test tube for each control, substrate, and enzyme in the 4° C (ice bath), 23° C (room temperature), 37° C (body temperature), and 60° C (water bath). Add the inhibitor that was used and what it was used for.

-VariablesoIndependent:The temperature of the milkoDependent:The time taken for the milk to solidifyoControlled:The same amount and type of milk usedThe same amount and concentration of enzyme mixture usedThe same test tube sizeResults:-TableAmount of enzyme mixture (mL)Amount of milk (mL)Temperature (oC)Time for milk to clot (min)Ex: 1 Ex: 2 Average2.551060+60+60+2.552034.2036.0035.12.55303.554.203.882.55402.102.252.182.55505.004.454.73Discussion:The experiment showed that changing the temperature did affect the rate at which the milk solidified. At low temperatures of 10oC and 20oC the milk took the longest to solidify and at 10oC did not even go lumpy after an hour. As the temperature increased the speed at which it reacted got faster until it reached around 40oC where the speed began to drop.

These results show how temperature of extreme high, or low affects enzyme activity. The highest rate of enzyme activity occurred at 37 Cº. Anything that was hotter or cold than 37 Cº slowed the reaction rate. As I thought, 100 degrees would denature the enzyme, and that was the case. The data provided shows exactly what temperatures enzymes work best, and worst. The objective was achieved as we discovered the different reaction rates under different temperatures. The results are reliable, as we know enzymes do not work well when under extreme heat or denaturation occurs. What I learned in this experiment was that enzymes don’t work well under cold temperatures because they tend to move slower. My hypothesis did not quite match, because I thought they work best at lower temperatures.

Enzymes will denature if they get too hot or cold or if the pH of the solution they are in is too high or too

This supports our hypothesis that the amplitude being adjusted doesn't effect the rate at which it swings. Now we move on to our question: Would mass be a factor? The first bob was replaced with something much smaller in weight. We returned the displacement back to 10 cms while keeping the length the same. We recorded the 10 periods and the average seems to be around the same approximate rate of 2.01. This debunks the theory of the pendulum being dependent on mass. Changing both the displacement and weight seems to not affect the rate in anyway.

The time in the water bath was also controlled to ensure that the enzymes were left to react for the same amount of time, making the experiment

However if the temperature exceeds the optimum temperature the enzyme becomes denatured. This is because there is too much energy causing the enzyme molecules to vibrate causing the bonds maintaining their tertiary structure to break. The enzyme unravels causing the shape of the active site to change so it can no longer fit with the substrate.

point at which the protein degrades and denatures – or falls apart into its lower levelstructures. Denatured proteins will often return to their original state, after the removal of the denaturing agent, except when they are degraded multiple levels (such as Quaternary to Secondary). Rate of reaction through catalysis can also be increased by increasing the concentration of either the enzyme or the reactants; enzyme if all the active sites are full or the substrate if the active sites are not all full.

2. (5 pts) List and explain the names and affiliations of the various characters/stakeholders in this story – I’m looking for us to use the story to map out the complexities that are generally associated with solving public health puzzles – the stakeholders you list and explain here should apply to many of the cases we consider going forward.

During these experimental procedures, the implication of multiple different temperatures on fungal and bacterial amylase was studied. In order to conduct this experiment, there were four different temperatures used. The four temperatures used were the following: 0 degrees Celsius, 25 degrees Celsius, 55 degrees Celsius, and 80 degrees Celsius - Each temperature for one fungal and one bacterial amylase. Drops of iodine were then placed in order to measure the effectiveness of the enzyme. This method is produced as the starch test. The enzyme was tested over the course of ten minutes to determine if starch hydrolysis stemmed. An effective enzyme would indicate a color variation between blue/black to a more yellowish color towards the end of the time intervals, whereas a not so effective enzyme would produce little to no change in color variation. According to the experiment, both the fungal amylase and bacterial amylase exhibited a optimal temperature. This was discovered by observing during which temperature and time period produced a yellow-like color the quickest. Amylase shared a similar optimal temperature of 55 degrees Celsius. Most of the amylases underwent changes at different points, but some enzymes displayed no effectiveness at all. Both amylases displayed this inactivity at 0 degrees Celsius. At 80 Celsius both the enzymes became denatured due to the high temperatures. In culmination, both fungal and bacterial amylase presented a array of change during it’s

We then tested the last set of test tubes containing milk and lactase, we did this to find which ones would present the most glucose concentration results, when placed in different temperatures, 4°C, boiling and room temperature. What we wanted to know was how far temperature could affect lactase to perform its enzymatic activity. We hypothesized that if the lactase is placed in a high or low temperature outside its active range, the temperatures would have a negative impact on the functions of the enzyme. If the temperature has an affect on lactose then we would see some temperatures in which lactase will be function able. We came to a conclusion that enzymes work at a temperature that is closest to body temperature (25°C); boiling water (100°C) denatures the enzyme, while the enzyme is not able to function properly if

To find the effect of temperature on the activity of an enzyme, the experiment deals with the steps as follows. First, 3 mL if pH 7 phosphate buffer was used to fill three different test tubes that were labeled 10, 24, and 50. These three test tubes were set in three different temperature settings. The first test tube was placed in an ice-water bath for ten minutes until it reached a temperature of 2° C or less. The second tube’s temperature setting was at room temperature until a temperature of 21°C was reached. The third tube was placed in a beaker of warm-water until the contents of the beaker reached a temperature setting of 60° C. There were four more test tubes that were included in the procedure. Two of the test tubes contained potato juice were one was put in ice and the other was placed in warm-water. The other two test tubes contained catechol. One test tube was put in ice and the other in warm water. After

After 30 minutes the test tubes were shook and then held against a white background in a well lit room. The colour of each solution was recorded.

Temperature alters the kinetic energy and there is fast collision between enzyme and the substrate (RSC 2004). At low temperature, there is low kinetic energy, means there is few collisions between substrate molecule and enzyme, while at high temperature there is high kinetic energy, more collisions, and the rate of reaction is high (Nygma science 2010). The rate of reaction doubles for every 10 oc. Thus, heating up an enzyme by 10OC, the rate of reaction is going to double reaches a point where the enzyme starts to denature and this process is irreversible (Nygma science 2010). Different enzymes have different temperature variations. As such, most enzymes have an optimum temperature of 30OC, while some of the enzymes has less than 30OC (Bio factsheet 2017). For example, a cold-water fish would die at 30OC, because their enzymes denature. Exceptionally some bacteria’s enzymes can withstand 100OC

The activity of an enzyme is affected by its environmental conditions. Increasing temperatures increases the kinetic energy that molecules possess. If enzymes are overheated, they start denaturing. Denaturing is a process in which the enzyme loses its primary structure due to overheating or by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent, radiation or heat. If proteins in a living cell are denatured, this results in possible death of the cell. Denatured proteins can exhibit many different characteristics from loss of physical form to communal aggregation. (www.worthington-biochem.com/introbiochem/factors.html‎ )