Background: The sugar molecule lactose is found in dairy products and people with Lactose Intolerance are unable to digest lactose because the enzyme lactase is unable to split the sugar molecule into glucose. Lactase is an enzyme that breaks lactose down into galactose and glucose. Lactase functions best between 21 and 48 degrees Celsius (or 70 and 120 degrees Fahrenheit). Cooler temperatures will slow down lactase’s function, whereas high temperatures can denature it or lactase will lose its shape. If lactase is rendered nonfunctional because of temperature or pH extremes, the breakdown of lactose stops. Lactose intolerance occurs when this breakdown fails due to insufficient or ineffective lactase. The experiment will stimulate the process …show more content…
Hypothesis: If the amount of lactase is higher in plain yogurt, than the amount of glucose will also increase because lactase is an enzyme that breaks up the milk sugar lactose to produce the sugar glucose. If more lactase is present in a substance, such as the plain yogurt, than it will be easier and more efficient to break down the lactose into glucose. Therefore, if higher levels of lactase are present, then there will be more glucose present. Variables: Independent: 20 mL of a substance (fat- free milk, fat- free lactose- free milk, vanilla ice cream, and plain yogurt) Dependent: Amount of glucose which will be measured using a glucose test strip Controls: • Amount of Lactaid original lactase drops (4) • Initial temperature of each substance (23 degrees …show more content…
The positive control solution is 2% glucose in water. This is necessary to make sure the glucose strips are able to detect glucose. The negative control solution is water. This is necessary in making sure the glucose test strips don’t react to plain water. 1. In a beaker, grind one glucose tablet (4 grams) with a spoon. 2. Add 200 mL of water and stir until the tablet is dissolved. 3. Fill a test tube with the 2% glucose water and label it with tape and a marker. This is the positive control solution. 4. Fill another test tube with 200 mL of plain water and label it Negative Control. 5. Test both the positive and negative control solutions with the glucose strips. 6. Dip separate strips into the glucose solution (positive control) and water (negative control). 7. Wait for the length of time specified by the test strip directions. 8. Record any color changes of the strip and determine the glucose concentration according to the key on the bottle. 9. Record any observations made. (A clear positive reaction for the 2% glucose control and a clear negative reaction for the water control should be seen). 10. Create the lactase solution. 11. Take 5 lactase caplets and grind them into a powder. 12. Measure out 200 mL of water in a beaker. 13. Add the lactase powder to the 200 mL of water and stir until completely
Briefly describe an alternative technique that could be used to measure the amount of glucose within sports drinks. (5 points)
We finally took 1ml of the 0.01% solution from test tube using the glucose pipette and adding it to test tube 4, we then used the H2O pipette and added 9ml of H2O to test tube 4 creating 10ml of 0.001% solution.
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
While the tube for specimen Cb turned a tannish white in the lower half of the tube while the top stayed the lavender inoculated tube color. Do to this evidence I determined that both specimens Ca and Cb cannot use the process Casein hydrolysis or Casein coagulation due to lack of soft or firm curds in both tubes. Since there was no casein curds formed, I concluded that specimens Ca and Cb also cannot perform the process of proteolysis. My conclusion is supported by the fact that there was no clearing of the medium. I have also determine that neither of my organisms can make the enzymes rennin, proteolytic or even proteases. I know my specimens cannot produce proteases due to the fact that there was no blue coloring in the tubes which means that the byproduct Ammonia was not produced to increase the pH. Since neither of my specimens can make these enzymes, I concluded that my specimens cannot break down lactose or casein. Although I did learn that specimen Cb can reduce litmus due to the evidence that the lower part of the tube turned a tannish white color with a purple ring at the top. This color change from a purple to a white means that the litmus was reduced turning it clear and leaving the white of the milk to show. Finally I know that specimen Ca cannot reduce litmus due to the fact that the tube had no change in
Lactase is an enzyme found in the digestive system. It is essential to the complete digestion of sugar in whole milk and milk products. Lactase specifically breaks down lactose, a complex sugar. Lactase cannot be absorbed by the body unless it is broken down by lactase into glucose and galactose. According to webMD, “Lacking lactase in their intestines, a person consuming dairy products may experience the symptoms of lactose intolerance…Abdominal cramping, flatulence (gas) and diarrhea can occur when a lactose intolerant person consumes milk products.” ("Lactase Enzyme oral : Uses, Side Effects, Interactions, Pictures, Warnings & Dosing - WebMD", n.d.) Lactase is not recommended for use in CHILDREN younger than 4 years of age. Safety and effectiveness in this age group have not been confirmed. (Kluwer, 2014)
The lac operon is a transcriptional control of lactose metabolism in bacteria. The operon contains three transcriptional genes, lac Z, lac Y and lac A, which encodes for β-galactosidase, permease and transacetylase respectively. Lac P and lac O copes for the lac promoter and the lac operator, essential to the functioning of this operon. β-galactosidase converts lactose to allolatose, while permease allow lactose to be transported into the cell. Transacetylase does not have a role in lactose usage. In the absence of lactose, there is no allolactose, converted from lactose by β-galactosidase, to the active regulatory repressor, and thus the repressor binds to the operator and transcription is inhibited, as the RNA polymerase bound to the promoter is blocked. In the presence of lactose, allolactose binds to the repressor, rendering it inactive and unable to bind to the operator, allowing the transcription of the three structural genes.
This would give us an extra measure of accuracy each time. Another way to improve the experiment and to produce consistent readings was to used distilled water. This is because the distilled water contains no impurities and therefore no hardness in water.
The second group of results was based on my biochemical test. The initial test was EMB agar, which appear light pink color that determine a negative result. The MacConkey agar appeared clear, indicating a negative result. The Durham fermentation tube for glucose appeared yellow and with bubbles on the
Because it’s very difficult to accurately measure lactose or glucose in solution, we use a false substrate (known as analog) for the enzyme known as ONPG (ortho-nitro-phenyl-galactoside). ONPG has a structure similar to lactose, so it can bind to the enzyme and be cleaved. The products are galactose and ortho-nitrophenolate. ortho-nitrophenolate is yellow in color and can be measured by spectrophotometry.
Kirk, Julienne., Stegner, Jane., 2010. Journal of Diabetes Science and Technology: Self-Monitoring of Blood Glucose: Practical Aspects. Retrieved from: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2864180/
American Diabetes Association (ADA) set a target of achieving blood glucose level in the range of 140-180 mg/dl for patients in critical conditions. Fasting glucose level should be below 140 mg/dl and random blood glucose level should be below 180 mg/dl (ADA, 2008; ADA, 2013). In hospitals it is necessity to maintain the blood glucose level in the narrow range and blood glucose monitoring should be done at the patient bedside. This maintaining blood glucose in the narrow range at the bedside, requires technically sound personnel and with high skills. Nurse or personnel, monitoring the blood glucose should be with the sound knowledge of physiology, pathology of abnormal glucose conditions, effects of abnormal glucose conditions, effect of age, gender, environmental conditions, fasting or feed conditions and temporal effect on glucose level. Along with this, nurse should have complete understanding of the different techniques used for the glucose monitoring, theoretical and practical know how of the instruments, troubleshooting of the instrument and maintenance of the instruments (Mraovic, 2012; Klonoff, 2010).
2. In the large beaker, put water and boil it completely. After that, remove the beaker from heat. 3. Sample tubes (A-D) should be labeled and capped tightly.
2018). It is recommended to perform at least three times a day including both pre-and postprandial measurements to achieve their goal for the glucose level management. In a large cohort study, the performance of more than 3 self-tests per day was associated with a statistically and clinically significant 1.0% absolute reduction in A1C (Berard et al. 2018). In situations where A1C does not accurately reflect glucose level, monitoring BG is necessary to adequately monitor glycaemia (Berard et al. 2018). The test involves pricking a finger with a lancet device to gain a small blood sample, applying a blood drop onto a testing strip, and determining the glucose concentration by inserting the strip into a reflectance photometer for an automated reading (Berman et al.
...he results of the yogurt production after 3 days are as follows: the yogurt has a semi-solid texture, acidic smell, and a sour taste indicating that Lactic acid production took place. The wine production results after the same amount of time was as follows: the wine smells slightly of alcohol, the amount of liquid decreased, and some bubbling is still present; the balloon is currently inflated and producing carbon dioxide. Based on these results the ethanol fermentation was also successful. During both of these experiments fermentation took place, in the case of the yogurt the Lactic acid gave the yogurt a tart taste and smell, and in the Ethanol fermentation the wine smelled of alcohol and produced carbon dioxide indicated by the air in the balloon. In conclusion, NADH was oxidized and Lactic acid and ethanol were produced in both experiments through fermentation.
Fehling’s solution to test the presence of glucose. The following figure (Figure 6) shows this experiment set up.