Introduction: So what is an enzyme? An enzyme is “any protein that acts as a catalyst, increasing the rate at which a chemical reaction occurs. The human body probably contains about 10,000 different enzymes.”(Farlex) The active site or sites of every enzyme are composed of a particular array of amino acids. The active site exhibits specificity for the substrate of the enzyme. The enzyme should bind and catalyze the reaction for its specific substrates better than with any other substrates. Therefore, the following experiment is testing the ability of lactase to specifically bind and interact with lactose compared to maltose. Materials and Methods: Enzyme Specificity To begin with the experiment, two microfuge tubes were labeled. …show more content…
The EDTA tube required 0.5 M EDTA to be added until the solution reached 1.25 mL of EDTA. To the Control tube, distilled water had to be added. Once done, this tube now contained 1.25 mL of water. After these steps were done, each tube called for three drops of milk. The tubes must then be inverted and allowed to sit for one minute. Once one minute had gone by, each tube needed three drops of lactase solution. For now, both tubes had to be placed in the 40 °C water bath and left alone for ten minutes. After the ten minute timer went off, the two tubes were taken out of the water bath. A glucose strip had to be placed in each tube for one second each. Once that had been done, both glucose strips had to be set out on the lab bench for thirty seconds. At the end of thirty seconds, the strips and their new coloration had to be compared to the chart provided, which helps to determine the amount of glucose in mg/dL. Results: 8.3 The results for enzyme specificity were determined by the amount of glucose present in the lactose and maltose microfuge tubes. Inside the lactose labeled tube, the average glucose measurement was 1,700 mg/dl. (Table 1) On the other hand, the tube labeled Maltose had an average glucose measurement of 20 mg/dl. (Table 1) Substrate Lactose Maltose Glucose (mg/dL) 1,700 mg/dl 20
Data from Table 1. confirms the theory that as the concentration of glucose increases so will the absorbance of the solution when examined with the glucose oxidase/horseradish peroxidase assay. Glucose within the context of this assay is determined by the amount of ferricyanide, determined by absornace, which is produced in a one to one ratio.1 Furthermore when examining the glucose standards, a linear calibration curve was able to be produced (shown as Figure 1). Noted the R2 value of the y = 1.808x - 0.0125 trend line is 0.9958, which is statistically considered linear. From this calibration curve the absorbance values of unknowns samples can be compared, and the correlated glucose concentration can then be approximated.
We then took 1ml of the 0.1% solution from test tube 2 using the glucose pipette and added it to test tube 3, we then used the H2O pipette and added 9ml of H2O into test tube 3 creating 10ml of 0.01% solution.
The control for both curves was the beaker with 0% concentration of substrate, which produced no enzyme activity, as there were no substrate molecules for...
These labels indicated the lactose solution that was be placed into the mini-microfuge tubes. The varying lactose ph solutions were obtained. The four miniature pipets were then used, (one per solution,) to add 1mL of the solution to the corresponding mini-microfuge tubes. When this step is completed there were two mini-microfuge tubes that matched the paper towel. Then, once all of the solutions contained their respective lactose solutions, 0.5mL of the lactase enzyme suspension was added to the first mini-microfuge tube labeled LPH4 on the paper towel, and 4 on the microfuge tube. As soon as the lactase enzyme suspension was added to the mini-microfuge tube, the timer was started in stopwatch mode (increasing.) When the timer reached 7 minutes and 30 seconds, the glucose test strip was dipped into the created solution in the mini-microfuge tube for 2 seconds (keep timer going, as the timer is also needed for the glucose strip. Once the two seconds had elapsed, the test strip was immediately removed, and the excess solution was wiped gently on the side of the mini-microfuge tube. The timer was continued for 30 addition seconds. Once the timer reached 7:32 (the extra two seconds accounting for the glucose dip), the test strip was then compared the glucose test strip color chart that is found on the side of the glucose test strip
Equipment list: Test tubes were used to hold the milk, the lipase and the milk and lipase solutions. Test tube racks were used to hold the test tubes
6. Place the test tube in the beaker. Secure the test tube and thermometer to the retort stand using clamps. Begin heating the water bath gently.
The three-dimensional contour limits the number of substrates that can possibly react to only those substrates that can specifically fit the enzyme surface. Enzymes have an active site, which is the specific indent caused by the amino acid on the surface that fold inwards. The active site only allows a substrate of the exact unique shape to fit; this is where the substance combines to form an enzyme- substrate complex. Forming an enzyme-substrate complex makes it possible for substrate molecules to combine to form a product. In this experiment, the product is maltose.
The mixture for that table’s flask was 15 mL Sucrose, 10 mL of RO water and 10 mL of Yeast, which the flask was then placed in an incubator at 37 degrees Celsius. In my hypothesis for comparison #4 the measurements would go up again with every 15 min. intervals because of the high tempeture and also be higher that then Controlled Table’s measurements. Hypothesis was right for the first part but was wrong for the second part of the comparison, the measurements did increase in the table’s personal flask but the measurements did not get higher than the Controlled Table’s measurements, see chart below. In conclusion, I feel that the substitution of glucose for sucrose made the enzymes work just as hard as the Controlled Table’s flask but just not as much because sucrose was too strong for the enzymes to
Introduction Most mammals are initially born with the ability to break down the polysaccharide, lactose into smaller monosaccharides but at an early age, usually as the child starts to rely less on their mother for direct nurturance, this ability ceases. This inability to break down lactose is known as lactase non-persistence. Lactase Non-persistence is the wild type in the population surprisingly even though a vast majority of the population is lactase non persistent. Individuals with the ability to digest the lactose found in milk are considered lactase persistent or lactose tolerant.
Place the dialysis tubing into the cup it corresponds with 11. Fill the first cup with the solution indicated on the outside of it until the solution completely covers the model cell placed inside. 12. After 24 hours remove the dialysis tubing bag from the cup. Once again gently roll it back and forth on a paper towel to remove excess liquid.
2.5 7.5 1 4 1.25 8.75 0.5 5 0.6 (0.625) 9.4 (9.375) -. 0.25 6 0.3 (0.3125) - 0.3125. 9.7 (9.6875) -. 0.125 Grapefruit Juice Test tube Glucose ml Distilled water ml Glucose % Colour Transmission Glucose Concentration 1 10 - 4 2 5 5 2 3 2.5 7.5 1 4 1.25 8.75 0.5 5 0.6 (0.625) 9.4 (9.375) -. 0.25 6 0.3 (0.3125) - 0.3125.
4. Put milk samples into the beaker for about five and a half minutes and take samples out after time is up. 5. With the warm samples, open the pouch containing the gel cassette and remove the cassette.
...remain the same at 4ºC and 25ºC. The final result of this experiment was that glucose was more present in environments of higher temperatures. Our hypothesis and predictions were wrong because lower temperatures do not break down the enzymes because they become denatured. The enzyme activity decreases once the temperature decreases, as well. Enzyme activity increases when there is a rise in temperature, which is why lactose is broken down in much higher temperatures, resulting in a high presence of glucose.
In this experiment, researchers used different measurements of catechol and 1cm of potato extract. Researchers hypothesized that the increase in substrate would level out the enzyme activity by
tube. Add 6 mL of 0.1M HCl to the first test tube, then 0.1M KMnO4 and