Lipid metabolism is one source of energy for the human body. We eat food containing one form of lipids, triacylglycerols. Before starting lipid metyabolism, these fats get broken down into droplets by bile salts.Triacylglycerols can be broken into fatty acids plus glycerol via hydrolysis with the help of the pancreatic lipase enzymen and then get used by cells for energy by breaking down even further. Once the pancreas and cells have enough energy and don’t need to absorb anymore, fatty acids get synthesized back into triacylgleryols. The excess triacylglycerols get stored in adipose tissue. Excess storage leads to weight gain and obesity.
The enzyme being tested in this lab is the pancreatic lipase enzyme. It is secreted by the pancreas. In the intestinal tract, it is found breaking down lipids, or dietary
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fats, via hydrolysis, or the breaking of hydrogen bonds (WiseGeek.Org). This enzyme catalyzes the reaction of taking triglyceride substrates plus water and converting it into monoglycerides and 2 free fatty acids; so it take tri, or 3, glycerol and breaks it into mono, or 1, glycerol (Wikepedia). To stop this reaction from happening, or make the reaction rate happen slower, we need an inhibtor. There are two types of inhibitors being tested in this lab; competitive and non competitive. Competitive inhibitos will be similar to the substrate, which is coconut oil in this case, in the means of size, shape and functional groups around it. It still has to be a little different to react differently, if it were the exact same then it would react the same way which is not wanted.Since they are similar, they compete with the substrate for the enzymes active site. Once they bind to the active site, the original substate cannot bind and therefore it stops the reaction from happening because now the enzyme cannot catalyze the reaction. Uncompetitive inhibitors are just that, they do not compete for the active site of an enzyme. They also do not share many similarities to the substrate. It instead just binds somewhere else on the enzyme and therefore makes the reaction occur less efficiently. Inhibiting the above reaction catalyzed by the pancreatic lipase enzyme will help to find a treatment for obesity because once the reaction is stopped or slowed down, it will decrease the amount of fat being stored in adipose tissue. Since the fat isn’t being stored, it means it is being excreted from the body. This will lead to weight loss and thus, a treatment for obesity. The substrate that was used in this lab was coconutoil which has a carboxylic acid functional group.
The R group is a long carbon chain which is open. The two inhibiting drugs that are of interest are caffeine and alli, also known as orlistat. Caffeine has amine and amide functional groups. They are in two closed cyclic rings connecting each other. This drug may act as an uncompetitive inhibitor; it is not a competitive inhibitor because it does not look siilar to the substrate coconut oil and does not have any same functional groups. The cons of using caffeine is vomiting, digestive distubances, constipation and stomach cramps. The pros of this drug is that is prevents type 2 diabates, decreases fatigue and drowsiness. The other drug, alli, has an ester group. Ester groups and carboxyclic acids are derivatives of each other. Alli also has a long carbon chain attached to it similar to that of coconut oil. The similarities make Alli a competitive inhibitor. The pros of Alli are it helps with weight loss, it prevents type 2 diabeters and it it not addictive. The cons of Alli is it will cause kidney stones and has unpleasant gastrointestinal effects.
(Web.MD) The experimental question being tested in this experiment is: Which drug, caffeine or orlistat, best inhibits the pancreatic lipase enzyme to target lipid metabolism? A spectrophotometer will be used to measure the rate of the enzyme reaction, which is absorbance over time. The color of the solution will be observed. If it turns cloudy to clear, it means the enzyme is catalyzing the reaction. If it stays cloudy, it means the enzyme is being inhibited. The whole purpose of the experiment is to find the drug that best inhibits the enzyme which will minimize obesity by stopping it from breaking down fat and storing it in adipose tissue. Instead, the excess fat will be excreted from the body. The expected results were that Alli would inhibit the pancreatic lipase enzyme better than caffeine because it is a competitive enzyme. It will compete for the active site causing the reaction not to happen unlike caffeine, which is an umcompetitive enzyme, which will bind to another part of the active site on pancreatic lipase and only decrease the reaction rate.
The unknown bacterium that was handed out by the professor labeled “E19” was an irregular and raised shaped bacteria with a smooth texture and it had a white creamy color. The slant growth pattern was filiform and there was a turbid growth in the broth. After all the tests were complete and the results were compared the unknown bacterium was defined as Shigella sonnei. The results that narrowed it down the most were the gram stain, the lactose fermentation test, the citrate utilization test and the indole test. The results for each of the tests performed are listed in Table 1.1 below.
Data table 1 Well plate Contents Glucose concentration A 3 drops 5% sucrose + 3 drops distilled water Negative B 3 drops milk+3 drops distilled water Negative C 3 drops 5% sucrose +3 drops lactase Negative D 3 drops milk +3 drops lactase 15+ E 3 drops 20% glucose +3 drops distilled water 110 ++ Questions B. In this exercise, five reactions were performed. Of those reactions, two were negative controls and one was a positive control.
Living organisms undergo chemical reactions with the help of unique proteins known as enzymes. Enzymes significantly assist in these processes by accelerating the rate of reaction in order to maintain life in the organism. Without enzymes, an organism would not be able to survive as long, because its chemical reactions would be too slow to prolong life. The properties and functions of enzymes during chemical reactions can help analyze the activity of the specific enzyme catalase, which can be found in bovine liver and yeast. Our hypothesis regarding enzyme activity is that the aspects of biology and environmental factors contribute to the different enzyme activities between bovine liver and yeast.
The affects of pH, temperature, and salt concentration on the enzyme lactase were all expected to have an effect on enzymatic activity, compared to an untreated 25oC control. The reactions incubated at 37oC were hypothesized to increase the enzymatic activity, because it is normal human body temperature. This hypothesis was supported by the results. The reaction incubated to 60oC was expected to decrease the enzymatic activity, because it is much higher than normal body temperature, however this hypothesis was not supported. When incubated to 0oC, the reaction rate was hypothesized to decrease, and according to the results the hypothesis was supported. Both in low and high pH, the reaction rate was hypothesized to decrease, which was also supported by the results. Lastly, the reaction rate was hypothesized to decrease in a higher salt concentration, which was also supported by the results.
The purpose of this experiment was to discover the specificity of the enzyme lactase to a spec...
“Enzymes are proteins that have catalytic functions” [1], “that speed up or slow down reactions”[2], “indispensable to maintenance and activity of life”[1]. They are each very specific, and will only work when a particular substrate fits in their active site. An active site is “a region on the surface of an enzyme where the substrate binds, and where the reaction occurs”[2].
In biology class, we were learning about enzymes. Enzymes are proteins that help catalyze chemical reactions in our bodies. In the lab, we were testing the relationship between the enzyme catalase and the rate of a chemical reaction. We predicted that if there was a higher percentage of enzyme concentration, then the rate of chemical reaction would increase or it would take less time. We placed 1 ml of hydrogen peroxide into four depressions. Underneath the first depression, we place 1 ml of 100% catalase and make 50% dilution with 0.5 ml of water. We take 50% of that solution and dilute with 0.5 ml of water and we repeat it two more times. there were four depressions filled with catalase: 100%, 50%, 25% , 12.5 % with the last three diluted
Madar, Sylvia S., & Windelspecht, Michael. (2014). Inquiry into Life, Metabolism: Energy & Enzymes (pp. 104-107). New York: McGraw Hill.
Although many individuals are uncertain about the increasing statistics associated with obesity, more than seventy percent of men and virtually sixty-two percent of women within the United States adult population are overweight or obese (Wilmore, Costill, & Kenney). Obesity refers to the condition of having an excessive amount of body fat. If an individual’s amount of body fat becomes too excessive, he/she is at a much greater risk of developing life-altering diseases such as heart failure, hypertension, type II diabetes, cancer, gallbladder disease, osteoarthritis, etc. (Wilmore, et al., 2008).
When the enzyme amylase comes in contact with the starch molecules, it decreases the energy needed for the chemical reaction that breaks starch down into maltose, a simple sugar. The maltose molecules, or substrate. Fit perfectly into the enzyme’s active site, and thus the activation energy is reduced and the reaction can take place. This won’t work, however, if the enzyme is denatured. Denaturing occurs when either the temperature or pH of the enzyme is changed.
The carbohydrates you eat are converted to glucose. Glucose is the body’s primary source of energy. If your intake of carbohydrates is low, you reach a point where your body draws on another energy source - fat stores. The body burns fat and turns it into a
This is likely due to a variety of metabolic adaptations that increase the body’s ability to use fat as a substrate, including the following: “decreased muscle and liver glycogen storage and rate of breakdown, increased gluconeogenesis, increased triacylglycerol storage, and utilization, increased mitochondrial oxidative capacity, increased ketone production, and decrased use of glycolysis-dervied acetyl-CoA” (Fleming et al.,
Lipases are enzymes that break down the fats. Esters formed from glycerol and fatty acids are catalyzed and hydrolyzed by these enzymes. They are used in many biotechnological processes and have applications in food, cosmetics, detergents, pharmaceutical industries and industrial waste management. Numerous efforts have been done to isolate lipase producing microbes. Microbial lipases are commercially important, microbes like bacteria, yeast and fungi produce lipases.
Lipase is enzymes that speed up the reaction of breaking fat into fatty acids and glycerol. Lipase can be found in different kind of industry. It can be found in dairy industry, by lipase is used to break down the milk fats and give different flavour into the cheese. Those flavour came from when lipase turn fats into fatty acid. Lipase that are use to react is from the microbial that create bacteria. The bacteria that are created will create the lipase to react on product. Another object that are use to create the reaction to make cheese is the mild lipase power that included the lipase inside. The mild lipase will also help speed up the reaction of breaking down fats into fatty acids that can stronger the flavour of the products.
Other lipase enzymes, such as pancreatic lipases, are secreted into extra cellular spaces where they serve to process dietary lipids into more simple forms that can be more easily absorbed and transported throughout the body.