I. Introduction An enzyme is a protein that functions as a catalyst, to speed up the reaction by diminishing energy needed for the reaction (Ophardt, 2013). They also, “increase the rate of (a) reaction” without using as much energy as if it would when the reaction occurs on its own (Mader, pg.104). The beaded-like structure of an enzyme consists of a gap known as the “active site” which allows a substance to bind to the enzyme. Generally, an enzyme “acts specifically with only one reactant to produce a product” (Ophardt, 2013). The reactant that binds with an enzyme at the active site is known as a “substrate” and is engulfed by the enzyme creating an “induced fit model” where the reaction will occur. As a result of enzymes not being consumed by the reaction, it will not be part a product (Mader, pg.105). For mammals, lactase is an enzyme that allows the hydrolysis of lactose, a milk disaccharide, into glucose and galactose (Wiley, 2013). Lactase is a “membrane bound enzyme located in the brush border or microvilli of the small intestine” (Wiley, 2013). Given the definition of enzymes, lactase is only able to hydrolyze lactose, making it specific to lactose. The purpose of the following experiment is to test whether the enzyme lactase is specific to lactose, and to see how different environmental factors affect lactase function. The hypothesis we generated from this statement was that the lactose function is specific so it will only hydrolyze lactose. In order to test that, we first mixed different disaccharides to see if glucose was present in the solutions which proves that lactase has hydrolyzed lactose. In the first experiment, we had four test tubes containing a solution of Milk + Lactase, Milk + Water, Sucrose + Lac... ... middle of paper ... ...0 mg/dL of glucose was produced and that at a temperature of 25° C 300 mg/dL of glucose was produced. At a temperature of 100° C, there was no production of glucose, which indicates that the enzyme was possibly denatured. The data retrieved in this experiment illustrates that temperature can help or hinder the production of a product. References Appio, M. (n.d.). Lactase. MAP: Molecular Anatomy Project. Retrieved November 10, 2013, from http://maptest.rutgers.edu/drupal/?q=node/31 Mader, S. S. (2011). Inquiry into Life (13th ed., McGraw-Hill international ed.). New York, NY: McGraw-Hill. Ophardt, C. E. (n.d.). Enzymes. Virtual Chembook. Retrieved November 7, 2013, from http://www.elmhurst.edu/~chm/vchembook/570enzymes.html Wiley, J. (n.d.). Lactose Intolerance.Concepts in Biochemistry. Retrieved November 10, 2013, from http://www.wiley.com/college/boyer/04700
After conducting this experiment and collecting the data I would have to say that the optimal temperature for enzyme activity would have to be room temperature which in my experiment was thirty-four degrees Celsius. I came to this answer because the glucose test strip showed that at room temperature there was more glucose concentration that at either of the other temperatures. Due to temperature extremes in the boiling water the enzymes could no longer function because the breakdown of lactose stopped. The cold water also hindered the breakdown of the lactose but as the water warmed the enzymes were more active which can be seen in the results for the cold water at 20 minutes B. Describe the relationship between pH and the enzymatic activity of lactase.
For example, incubating the samples at different temperatures would create more data points to establish an optimal temperature. From the results in the experiment in this study, it is known as temperature increases, enzymatic activity increase, and vise versa. However, what can not be observed is at what point does the increase in temperature begin to denature the enzyme, above 60°C. Furthermore, assays can be preformed to determine optimal pH, as well. From Dutta’s, and his partners, experiment it shows that there is a range where the Heliodiaptomus viduus’s lactase shows the most activity, which is between 5.0 and 6.0
For example, if a person had been able to consume lactose products for their life with no problems, but in an unfortunate event had to have a portion of his or her small intestine removed, there would be a change in the number of present lactase enzymes in the stomach. Because the lactase enzyme is stored in the small intestine, the person may now experience lactose intolerance due to the decrease in the presence of lactase. Knowing where the lactase enzyme is stored can aid physicians in understanding what will happen after a procedure or the introduction of a new medication. The experiment was conducted to determine the optimal ph of lactose required to produce the maximum amount of glucose. It was predicted that the optimal ph of lactose would be most efficient at lactose ph 6, and that the lower the ph, the amount of glucose produced would increase
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
The expression of lac operon in each tube equals the amount of beta-galactosidase produced. Therefore, by looking at the amount of beta-galactosidase under different conditions collectively is a good way to understand the function of inducers and repressors in supervising the expression of lac operon and the control of gene expression generally.
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)
LI was first recognized in the 1960s when researchers found black children responding unfavorably to milk in their diets (Harrison 812). Research led to the discovery that lactose, the major sugar in milk and related dairy products, was undigestible in some people because they were missing the enzyme lactase. Lactase breaks down lactose into its component monosaccharide sugars, glucose and galactose. In people missing lactase, lactose passes undigested through the small intestine. In some people, the undigested lactose passes through the remainder of their systems with no ill effects. In others, however, the undigested lactose becomes viscous and ferments in the colon (Englert and Guillory 903). The thickness of the liquid and the fermentation cause painful cramping, gas and sometimes diarrhea. Besides not being able to digest lactose, these people suffer from malabsorption, which causes them to receive little or none of milk's nutrients (Houts 110).1
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
Background information:. Enzyme Enzymes are protein molecules that act as the biological catalysts. A Catalyst is a molecule which can speed up chemical reactions but remains unchanged at the end of the reaction. Enzymes catalyze most of the metabolic reactions that take place within a living organism. They speed up the metabolic reactions by lowering the amount of energy.
As a group the slope of the glucose line was recorded as 59.001 ppm/min. The class average for glucose was conducted from numbers that were varied in size. The lowest number being 3.0136 ppm/min and the highest being 1026.2 ppm/min. The class average was calculated as 471.201 ppm/min for the respiration rate of yeast when metabolizing glucose. Using class averages from multiple periods the result of 679.48 ppm /min was collected as the overall average. Moreover, the collection of data for sucrose was also compressed into averages. The slope of the line for sucrose was recorded as 280.3 ppm/min for a group collection. The data of sucrose included numbers starting at -873.51 ppm/min and ended with 1522.8 ppm/min being the highest. The class average recorded for the respiration rate of yeast when metabolizing sucrose was 649.246 ppm/min. The overall average of sucrose was 575.686 ppm/min. Also, the data for starch and lactose were also calculated into class averages and overall averages. As a group the slope of the lactose line was recorded 155.69 ppm/min, and the slope of the starch line was recorded as 367.34 ppm/min. The class average calculated for lactose was 214.183 ppm/min while the average for starch was 389.439 (units). Lastly, the overall averages were collected for lactose and starch. The overall average of lactose
Enzymes have the ability to act on a small group of chemically similar substances. Enzymes are very specific, in the sense that each enzyme is limited to interact with only one set of reactants; the reactants are referred to as substrates. Substrates of an enzyme are the chemicals altered by enzyme-catalysed reactions. The extreme specific nature of enzymes are because of the complicated three-dimensional shape, which is due to the particular way the amino acid chain of proteins folds.
According to Elmhurst, an enzyme is a protein molecule that is a biological catalyst with three characteristics. First, the basic function of an enzyme is to increase the rate of a reaction. Second, most enzymes act specifically with only one reactant called a substrate to produce products. The third and most remarkable characteristic is that enzymes are regulated from a state of low activity to high activity and vice versa (Elmhurst). According to Princeton, catalase is a common enzyme found in nearly all living organisms that are exposed to oxygen, where it functions to catalyze the decomposition of hydrogen peroxide to water and oxygen. Catalase has one of the highest turnover
The enzymes have active sites on their surfaces to allow the binding of a substrate through the help of coenzymes to form enzyme-substrate complex. The chemical reaction thus converts the substrate to a new product then released and the catalytic cycle proceeds.
Lactase, a type of enzyme usually found in the small intestine, breaks down lactose into sugars such as galactose and glucose. People that are lactose intolerant cannot consume anything containing dairy because they cannot break down lactose, a sugar found in milk. Those that are lactose intolerant lack the enzyme lactase. Without lactase, the body does not have the ability to break down lactose, which leads to a person having an upset stomach and diarrhea. Adults are more likely to be lactose intolerant than children because of the metabolic change in the body (Dritsas). The lack of lactase that people have can be compensated by taking pills to help break down lactose that is consumed; with the help of a lactase pill the body can now absorb galactase and glucose properly (McCracken, 481).
By taking a Carbon Dioxide, rich substance and mixing it with a yeast, solution fermentation will occur, and then it could be determined if it is a good energy-producer. In this study glacatose, sucrose, glycine, glucose, and water were used to indicate how fast fermentation occurred. The overall result shows that monosaccharides in particular galactose and glucose were the best energy source for a cell.