Lactase Lab Report

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

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.

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

In order to generate a bicyclic lactone in this experiment, a Diels-Alder adduct was produced. The bicyclic lactone to be generated was cis-1,3,3a,4,5,7a-Hexahydro-5-methyl-3-oxo-4-isobenzofuran-carboxylic Acid and was produced using a Diels-Alder reaction. The product was also analyzed quantitatively using percent yield. To prepare the Diels-Alder adduct 0.40 g of 2,4-hexadien-1-ol was added to a flask, then 5.00 mL of toluene and 0.40 g of maleic anhydride were added to the flask in that order. The mixture was warmed and stirred to induce a reaction. The reaction progress was monitored using a TLC plate with 30:70 hexane used as the mobile phase and silica gel as the stationary phase. The TLC plate revealed a new spot for the crude product, indicating the reaction had begun.

Lactose is a sugar that can be put into smaller molecules, glucose and galactose. Lactose is when you are not able to digest milk and dairy meaning that the enzyme lactase that breaks down lactose is not functioning properly. ONPG was used as a substitute for lactase because even though it is colorless it helps show enzyme activity by turning yellow. This experiment measured the absorbance ONPG when exposed to lactase within an environment of different salinity’s. The enzyme, lactase, was obtained by crushing a lactaid pill and then was added into four cuvettes. ONPG and salt solution of different concentrations were added and their levels of absorption was measured by a spectrophotometer. The results showed that higher salt concentrations have a lower level of absorption. There were 4 cuvettes and within those cuvettes that solutions within them were being tested and the results showed the more salt solution added with the lactase the lower the absorbance. The less salt solution there was a higher rate of absorbance. The data supported the hypothesis that with increasing NaCl concentration there would be a decrease in enzyme activity.

specific enzyme (Knowles, 1991). One part of the enzyme, salivary amylase, is that alpha amylase is in the saliva of most animals because this enzyme breaks down starch (Jacobsen, Melvaer, Hensten- Pettersen, 1972). In the presence of starch, this enzyme is present in saliva, but is not present when there is no starch present (Jacobsen, Melvaer, Hensten- Pettersen, 1972). The conditions for salivary amylase to have a reaction with starch would change in temperature and enzyme concentration, as well as, monitoring the pH levels (Jacobsen, Melvaer, Hensten- Pettersen, 1972). Salivary amylase is an enzyme is human saliva that helps in digestion of specific substrates, such as starch (Hudman, Friend, Hartman, Ashton, Catron, 1957). It breaks down starch molecules by splitting maltose from the non-reducing end of a gluten molecule (Jacobsen, Melvaer, Hensten-Pettersen, 1972).

-Lactase deficiency is a deficiency in the enzyme that breaks down lactose. The causes of lactase deficiency include congenital defects, secondary lactase deficiency, and primary (acquired).

When lactose becomes available the genes encoding β-galactosidase and lactose permease are upregulated in E. coli.

If someone is lactose intolerant, that means that they are lacking the enzyme lactase, so the lactose does not get broken down into galactose and glucose. If lactose goes undigested it creates many problems. It causes dehydrations because water and electrolytes get pulled into the intestines by the lactose, which acts like an osmotic agent. The result of the increased amount of lactose would be diarrhea, bloating, and gassiness. Although being lactose intolerant seems to be abnormal, it is actually natural. The production of the enzyme, lactase, is a mutation of the LTC gene, it allows us to produce lactase as adults. In all other mammals lactase is produced during infancy but not during adulthood.

The anaerobic threshold (AT), also called the “lactate threshold,” is the exertion level between aerobic and anaerobic training. The AT is the point during exercise where your body must switch from anaerobic to aerobic metabolism. Anaerobic exercise consists of weightlifting, sprinting, and jumping. Once an athlete reaches its anaerobic threshold, lactic acid builds up in the muscles faster than it can be cleared away resulting in muscle cramps. The AT is a useful measure for deciding exercise intensity for training and racing in endurance sports. On average untrained individuals have a low AT (approximately 55 % of VolumeO2max), and elite endurance athletes have a high AT (approx. 80 - 90% of VolumeO2max). lactate threshold.(1) Studies have been conducted on finding methods of improving anaerobic threshold. Lately High-intensity interval training (HIIT) has become a popular training modality in competitive athletes, recreationally-trained individuals, and clinical populations. HIIT consists of repeated bouts of short to moderate duration exercise

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

The opposition for consuming dairy products lies on the notion that the enzyme that is able to digest the lactose sugar, lactase, “grinds to a halt sometime soon after weaning.” This can be believed to be a biological reasoning why we should not consume dairy products after weaning. However, Zuk mentions that there are some humans who are able to break down lactose well after weaning. She also describes that the gene for lactase persistence is a dominant trait. Thus, like we learned in class an organism only needs one copy of the dominant gene for the lactase persistence to occur.

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

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.

Lactose intolerance occurs when the body has a hard time digesting dairy products. Lactose is a milk sugar and is broken down by enzymes in the intestinal track, allowing the enzymes to be used as an energy source. Lactase is an enzyme which breaks down lactose. Lactose intolerance occurs when the intestine does not contain lactase (Jackson). Low lactose activity in the small intestine, allows undigested lactose to pass into the colon, where the bacteria are able to convert the sugar into hydrogen gas and organic acids. This causes symptoms such as bloating and cramping (“Lactose Intolerance”). The two causes of lactose intolerance are primary lactase deficiency and secondary lactase deficiency. In primary lactase deficiency the level of lactase enzyme falls as a person gets older. This does not allow the person to tolerate the amount of lactose that they were used to. This affects around 70 percent of the population. Secondary lactase deficiency is a temporary condition in which the level of lactase drops due to a problem in a person’s digestive