Dehydration Synthesis Lab Report

Secondary to the discussion post assignment for this week, I learned about lactose intolerance. When an individual drinks milk, an enzyme lactase, breaks down the lactose in the milk into two monosaccharides glucose and galactose which the individual then uses as energy for the body (Open Learning Initiative, 2015, pg.93). However, numerous individuals lack the necessary lactase needed to properly break down the lactose in their small intestine, resulting in bacteria in the colon breaking

The species of bacteria used to make yogurt both have a β-galactosidase system which hydrolyzes lactose into glucose and galactose. Because lactose is a disaccharide, it can be transported into the cell via the permease system. As aforementioned, glucose then enters the EMP pathway to yield pyruvate.

These results shown from this experiment led us to conclude that enzymes work best at certain pH rates. For this particular enzyme, pH 7 worked best. When compared to high levels of pH, the lower levels worked better. The wrong level of pH can denature enzymes; therefore finding the right level is essential. The independent variable was the amount of pH, and the dependent being the rate of oxygen. The results are reliable as they are reinforced by the fact that enzymes typically work best at neutral pH

Given the background, we hypothesized that for the first experiment, the lactase will break down lactose in milk and have a similar effect to sucrose. We also predicted that the Milk + Lactase reactant would have more glucose, the Milk + Water reactant would have a little bit of glucose broken down, the Sucrose + Lactase reactant would have less glucose than the Milk + Water reactant, and the Sucrose + Water reactant would have little to no glucose at all. As for the first procedure of the second experiment, we had hypothesized the more basic the solution would become, then the more glucose there would be. Our prediction for the first procedure of the second experiment was that there would be no glucose found in the solutions containing pH 4 and pH 7. For the second procedure of the second experiment, our hypothesis was that glucose would be present in the reactants at 4ºC and 25ºC while the reactant that had been in the hot water bath at 100ºC would have little to no glucose because it would have evaporated. We predicted that for this temperature experiment, the glucose would evaporate at 100ºC and would remain at 4ºC and 25ºC. For the first experiment we had found that a reactant of Milk + Lactase have high levels of glucose, while the other three reactants do not. As for the second experiment, for the first procedure, amounts of glucose were found in

In this lab experiment the action of the enzyme Amylase was observed on starch (the substrate). Amylase changed the starch into a simpler form, the sugar maltose, which is soluble in water. Maltose then breaks down the glucose chains of starch in the pancreas and intestines. Amylase is present in human saliva, and begins to act on the starch in the food while still in the mouth. Exposure to heat or extreme PH (acid or base) will denature proteins. Enzymes, including amylase, are proteins; if denatured enzymes can no longer act as a catalyst for the reaction. In the presence of potassium iodide, starch turns a dark purple color; however maltose does not react with I2KI. The rate of fading of starch allows a quantitative measurement of reaction rate.

They need to be broken down into simple sugars (monosaccharides) then digested/absorbed. In order to do this, the small intestine produces an enzyme called lactase. What lactase does is attaches itself to the lactose molecule and breaks it down into glucose and galactose. These molecules aren’t as big or complicated so they’re easily absorbed by the small intestine and into the bloodstream. Lactose Intolerance is when the body doesn’t actually produce the lactase enzyme, so the lactose can’t be broken down and absorbed. People with Lactose intolerance usually opt to take lactaid pills. The way these lactaid pills work is they contain the enzyme lactase that is responsible for the breakdown of lactose. You take these pills with the lactase in them and then now since your body now has the enzyme in needs to break down and absorb the lactose proceeds to do so. What people have recently found was that the pills don’t actually work due to the acidity levels in the stomach. So when you take the lactaid pills, they don’t make a difference because your stomach acids destroy the pills before they can take affect. What my results in Table 1 found that this was actually correct because, when the acid was introduced into this experiment it in essence rendered the pills completely useless. In Table 2 we found that, this issue was in fact due to the acidity because when you remove the acid, each test we did came back positive. Meaning that lactose was successfully metabolized/broken down into glucose. If we try and take account the sources of error that may have occurred during this lab, we have to take into account that these pills are recommended to be taken with food. So that while the pill is put into your system the stomach acids don’t destroy it because there is food in your system that it is already focused on. So maybe if we had mimicked the

HYPOTHESIS I hypothesize that the addition of lactase enzyme to the regular and the lactose free milk will change the concentration of glucose. RESEARCH • Lactose is one of the natural sugar that is present in the milk. • This sugar will give us glucose and galactose upon hydrolysis. • When lactose enters into the small intestine, an enzyme called lactase coverts it into glucose and galactose .

Lactase is an enzyme that breaks down lactose. Lactose is the sugar found in milk. It is made up of two monosaccharides: glucose and galactose. Therefore it is a disaccharide that needs to break down in order to be digested. However some people are “Lactose Intolerant” or lack lactase in their bodies. This means that they cannot consume lactose-contained food or drinks or they need help digesting it. People who are lactose intolerant must be very selective to make sure that they do not eat food or drinks with lactose. There are pills though, which are purchased by lactose intolerant people. This pill helps the people break down the sugar lactose into its smaller components.

“Lactase is an enzyme that breaks down lactose, the sugar in milk. It is produced by the cells lining of the small intestine. Most people are born producing it, but often make less of it as they age, which causes lactose intolerance the symptoms for this include nausea, bloating, and diarrhea to name a few. This enzyme is produced

Enzymes are proteins which can catalyse chemical reactions without changing themselves. The enzyme lipase breaks down the fat in dairy products such as full-cream milk for people who are lactose intolerant. Lipase acts on its specific substrate, lipids produces fatty acids. If enzyme concentration increases, random collisions between the substrates and active sites of enzyme increase due to the increasing amount of active sites which allow more collisions to happen, so the rate of breakdown of lipids to simpler substances will increase. During the experiment, sodium carbonate solution and pH indicator phenolphthalein will be added ahead of

Sucrose can be found in small amounts in fruit and vegetables but is more commonly consumed as table sugar (French, n.d.). Similarly to Lactose, Sucrose does not begin digesting until it reaches the small intestine (Jamerson, n.d.). There, the carbohydrate is broken down into absorbable monosaccharides through hydrolysis assisted by the enzyme Sucrase (Jamerson, n.d.). Also commonly ingested is the homopolysaccharide Starch (Decker, n.d.).

Whether it is for breaking down the sugar into monosaccharides or transporting the sugar into the cell. The ability for a sugar to undergo glycolysis is dependant on its ability to accept accept a phosphate group (adamcap.com, 2016). Sugar molecules that can more easily accept a phosphate group produce more CO2. Galactose must go through a three-step process in order to convert it into a type of glucose (adamcap.com, 2016). Galactose can be converted by yeast with the help of a group of special proteins made by the yeast. It does not usually do this however because galactose is not a good, high energy sugar (blogs.discovermagazine.com, 2016). Baker’s yeast cannot ferment with lactose because it lacks the enzyme, lactase, to break down lactose in the its two monosaccharides, glucose and galactose. The enzyme to break down fructose however is very common in living things and baker’s yeast (madsci.org, 2000). The reason stevia cannot be metabolized by yeast is because of its structure. It can’t be broken down in glycolysis into

The metabolism of E. coli can occur in the glucose first instead of the lactose. Since, E. coli cannot metabolize lactose at all time since lactose could not always be available in the environment sometimes. Moreover, the production of proteins o costs energy and materials. Glucose is metabolized first compared to some other sugars since it provides a better source of energy than lactose. Not only that glucose is an example monosaccharide while lactose is a example of disaccharide whereas the lactose is not able to be utilized first as the cells is not able to transport and cleaves the disaccharide lactose. In other words, after the metabolism of the glucose would b exhausted then only the lactose utilisation would be synthesized by using enzyme

Lactose Intolerance Lactose intolerance is the inability to digest significant amounts of lactose, the predominant sugar of milk. This inability results from a shortage of the enzyme lactase, which is normally produced by the cells that line the small intestine. Lactase breaks down milk sugar into simpler forms that can then be absorbed into the bloodstream. When there is not enough lactase to digest the amount of lactose consumed, the results, although not usually dangerous, may be very distressing. While not all persons deficient in lactase have symptoms, those who do are considered to be lactose intolerant.

The production of carbon dioxide in the yeast with lactose had a lower average than the average of yeast growing by it’s self. The lactose sugar effected the respiration the most. Its average growth was 3.896 and the plain yeast was 15.924; this makes the respiration rate 4 times smaller than the respiration rate of the plain yeast. The yeast highest point was 19.75, while the lactose only went up too 6.539; lactose is still 3 times smaller than yeast. Lactase was very harmful, while lactase and sucrose didn’t hurt as bad, but were not better than yeast. Lactase’s average respiration was about half of the yeast average respiration; while the average respiration of the sucrose in the almond milk was also about half of the average respiration in yeast. When looking at the smallest of the yeast and lactase you see the relationship of the lactase being half more clearly; the yeast smallest is 13.22, while the lactase’s is 6.07. Since 6 is half of 12, thirteen is