#9 - Digestion. Objectives: Prelab Activity. I Digestive System

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1 #9 - Objectives: Observe and understand the process of emulsification Understand the digestion of fats by pancreatic lipase and the purpose of bile Understand the digestion of protein by pepsin and the purpose of HCl Understand the digestion of starch (the substrate) by amylase (an enzyme) Understand what negative control is and why it is used Prelab Activity Fill in the table to correctly identify the reactants (substrates, enzymes), products, and reagents (also known as chemical indicators) used in each reaction described in Parts III, IV and V. Experiment Reactants Product(s) Reagent / Chemical Substrate Enzyme Indicators Part III Part IV Part V I Digestive System A. Introduction The digestive system functions to take ingested foods and break them down physically and chemically into small enough particles so that nutrients can be absorbed into the blood or lymphatic system. These nutrients can then be used for many functions including: releasing energy, creating more complex molecules such as proteins and nucleic acids, and maintaining fluid and electrolyte balance within the body. The organs of digestion include the gastrointestinal tract, the tube through which food travels, and the accessory organs which aid in the digestive process by mechanical or chemical means (Fig. 1). Page1

2 B. Digestive Reactions Like all enzymatic reactions, chemical digestive reactions must have a substrate and an enzyme as reactants. The substrate is the substance that the enzyme is acting on (it undergoes a chemical change) and the enzyme is the protein catalyzing this reaction (it can often be Figure 1. Organs of the Digestive system. reused and/or recycled). In this laboratory, in order to visualize that these digestive enzymatic reactions have occurred, we will utilize other chemical reactions using reagents (or chemical indicators) to detect the presence of fatty acids, proteins, and starch. A negative control is an experimental set up where you KNOW that nothing should happen. For an enzymatic reaction, a negative control would not include the substrate, enzyme, or both. This is included in experiments to validate when a reaction DOES OCCUR you can compare the results. II. Visualization of Lipid Emulsification with Bile salts A. Introduction: Bile Salts Bile is produced by the liver, stored and concentrated in the gallbladder, and then released into the small intestine when food is present in the duodenum. Bile is composed of bile salts, cholesterol, and bile pigments such as bilirubin. Specifically, it is the bile salts which function in digestion by acting as emulsifiers. The bile salts physically break up the lipids (mechanical digestion) into smaller droplets which provides more surface area for lipases to then break down the lipids chemically. Emulsifiers DO NOT chemically digest lipids but they aid in lipid digestion. B. Materials Figure 2. A. 2ml 2% Bile salt solution Vegetable oil lipid Distilled water 2, 2 ml microcentrifuge tubes (Fig. 2) Disposable droppers (transfer pipette) microcentrifuge tube. B. Transfer pipette (disposable dropper). A B Page2

3 C. Procedure 1. Label tubes 1 & 2 using a Sharpie Make sure to use separate droppers for each solution 2. Place 15 drops of oil in each tube. 3. To tube 1: add 15 drops of water. 4. To tube 2: add 10 drops of water and 5 drops of Bile salt solution. 5. Close both tubes tightly and shake to mix (30 seconds). 6. Observe directly after shaking. 7. Which tube has the larger lipid droplets 1 or 2? Put your observations in the lab report and answer the questions. 8. Dispose of the liquids in the appropriate container and dispose of the tubes in the trash. III. of Lipids with Bile and Pancreatic Lipase. A. Introduction Pancreatic lipase is an enzyme produced by the pancreatic acinar cells and chemically digests triglycerides (substrate) into fatty acids, glycerol, and some monoglycerides (products) within the small intestine. This catabolism makes the lipids small enough to be absorbed by the body into the blood or the lymph. Bile breaks up the lipid into smaller droplets so that lipase enzymes can have more access to the lipids for chemical digestion. A triglyceride is made of one glycerol molecule and 3 fatty acid chains (Fig. 3). As the lipase breaks apart the triglyceride, the fatty acids chains are released. These fatty ACIDs lower the ph of the solution. Therefore, we can visualize how much lipid catabolism occurs by using a chemical ph indicator like Bromothymol blue. The more the fatty acids accumulate, the more acidic the solution becomes. B. Materials 2% Lipase solution 35% Heavy whipping cream -contains fat and ph indicator (bromothymol blue) - ph 7 using NaOH (Fig. 4). 2% Bile salt solution 0.25M NaOH 3, 2ml microcentrifuge tubes Electronic water bath set at 40C (about body temperature) (Fig. 5). Figure 3. of a triglyceride by lipase. Figure 4. Showing cream with bromothymol blue: Left -greater than ph 7 (blue) ; Right less than ph 7 (yellow). Figure 5. Electronic water bath. Page3

4 Disposable droppers (transfer pipette) Microcentrifuge tube floater Distilled water C. Procedure 1. Label tubes A-C using a Sharpie on the TOP of the tubes, also put your initials. 2. Add the following solutions to the tubes in order from 1-4 as indicated in the table below. Make sure not to contaminate the solutions by mixing up the droppers or bottle tops. Table A: Lipid tube preparation. REACTANTS Tube A Tube B Tube C 1. Heavy cream 12 drops 12 drops 12 drops 2. Bile - 10 drops 10 drops 3. H2O 23 drops 13 drops - 4. Lipase drops Expected results? Or No digestion? Which are Negative controls for digestion? (indicate NEG.) 3. Close the caps tightly on all tubes and shake to mix (30 seconds). They should all appear a uniform blue color. If not, you may add one drop of NaOH to tubes that are yellowish. Record the initial color of all tubes in the lab report. 4. Place the tubes in the tube floater and place it in the 40C water bath for 30 minutes. While you are waiting start Experiment IV. 5. Observe the final color of the tubes after 30 minutes, recording the colors in the lab report and answer the questions. 6. Dispose of the liquids in the appropriate container before disposing of the tubes in the trash. IV. of Protein with Pepsin. A. Introduction Pepsin is a digestive enzyme produced by the chief cells of the stomach. Pepsin activity is greatest in an acidic environment such as the stomach, which secretes hydrochloric acid (HCl). Pepsin acts to break larger proteins (substrate) into shorter chain peptides. Thus, pepsin begins the digestion of proteins in the stomach, producing peptide chain fragments which will eventually be further digested in the small intestine. In this experiment we will be using pepsin to digest Figure 6. Biuret test for protein. Left - negative for protein (pale blue) Middle positive for protein (pale purple) Right shorter peptides present (pink). Page4

5 albumin (a protein) in the presence of acid, and then detecting the partially digested peptides using Biuret reagent. B. Materials 1% Pepsin solution 1M HCl solution 1% Albumin (a protein found in egg white and blood plasma) 3, 2ml microcentrifuge tubes Electronic water bath set at 40C (near body temperature) Disposable droppers (transfer pipette) Biuret reagent Protein indicator. Detects the present of peptide bonds. It is pale blue in the absence of protein and turns purple in the presence of protein; light pink / lavender in the presence of shorter peptides (Fig. 6). C. Procedure 1. Label tubes A-C using a Sharpie on the TOP of the tubes, also put your initials. 2. Add the following solutions to the tubes in order from 1-4 as indicated in the table below. Make sure not to contaminate the solutions by mixing up the droppers or bottle tops. Table B: Protein tube preparation. REACTANTS Tube A Tube B Tube C 1. Albumin 0 drops 12 drops 12 drops 2. Pepsin drops 3. HCl drops 4. H2O 24 drops 12 drops 0 drops Expected results? Or No digestion? Which are Negative controls for digestion? (indicate NEG.) 3. Close all tubes tightly and shake to mix (30 seconds). 4. Place the tubes in a microcentrifuge tube floater and place in the 40C water bath. 5. Wait 45 minutes and perform the Biuret s test on all tubes. While waiting, start Part V. 6. Biuret s Test: i) Invert the tubes to mix. ii) Add 3-5 drops of the Biuret s reagent to each tube, mix 30 seconds. Do not overfill. iii) Record the colors in the lab report and answer the questions. 7. Dispose of the liquids in the appropriate container and dispose of the tubes in the trash. Page5

6 V. of Starch with Amylase. A. Introduction Amylase is a digestive enzyme produced by salivary glands and the pancreas. It breaks dietary starches (polysaccharides) down into more simple sugars (disaccharides and monosaccharides). In this experiment we will be using bacterial amylase to digest a starch solution and using Lugol s solution (reagent) to detect the change in the starch level over time. B. Materials Amylase solution (2.5%)- on ice 5% Starch solution 6, 2ml microcentrifuge tubes Disposable pipettes (plastic dropper) Figure 7. Lugol s test for starch. Purple / black is positive for starch and progressively lighter as less starch is present. 3 drops Lugol s reagent Starch indicator. Detects the present of starches. It is pale yellow in the absence of starch and turns dark purple / black in the presence of starch. It will progressively get lighter purple / gray when less starch is present (Fig. 7). C. Procedure 1. Label tubes A-F using a Sharpie on the TOP of the tubes, also put your initials. 2. *Shake the reactants before pipetting. 3. Tubes A and B. Add the following solutions to the tubes in order from 1-3 as indicated in the table below. Make sure not to contaminate the solutions by mixing up the droppers or bottle tops. Table C: Starch tube preparation Tube A Tube B Tube C Tube D Tube E Tube F REACTANTS 0 min 0 min 10 min 20 min 30 min 40 min 1. Starch - 12 drops 12 drops 12 drops 12 drops 12 drops 2. H2O 15 drops 3 drops Amylase on ice drops 5 drops 5 drops 5 drops Expected results? Or No digestion? Which are Negative controls for digestion? (indicate NEG.) 3. Close tubes A and B tightly and shake to mix (30 seconds). 4. Perform the Lugol s test for starch on Tubes A and B - time 0 minutes. Lugol s Test for Starch: i) Add 3 drops of the Lugol s reagent to tubes A and B Page6

7 ii) Close the tubes tightly and invert (turn upside down and then right side up) to mix. iii) Immediately record the initial color after mixing, in the lab report 5. Tubes C-F -*Shake the reactants before pipetting. Add the following solutions to the tubes in order from 1-3 as indicated in the table below. Make sure not to contaminate the solutions by mixing up the droppers or bottle tops. 6. Incubate tubes C-F at room temperature, start timing. 7. Perform the Lugols test for starch on one tube every 10 minutes until all tubes are tested (ie. tube C at 10 minutes, tube D at 20 minutes, tube E at 30 minutes, and tube F at 40 minutes). Lugol s Test for Starch: i. Add 3 drops of Lugols reagent to the appropriate tube. ii. Close the tube tightly and invert to mix. iii. Immediately record the initial color after mixing in the lab report and answer the questions. 6. Dispose of the liquids in the appropriate container and dispose of the tubes in the trash. Page7

8 Lab Report #9 Name: II. Visualizing Bile Emulsification: 1. Which tube had the larger lipid droplets? Draw the final results as you see them How do the results show emulsification of fats? III. of Lipids with Bile and Pancreatic Lipase. 1. Record the initial color of all tubes by coloring the images labelled Time 0 minutes. Time 0 A B C 2. Record the final color of all tubes at Time 30 minutes. 3. In which tube was digestion most complete? (pick A-C) 4. How did you know that? Time 30 A B C 5. Is this what you expected? 6. Why was bile added to Tube C? Page8

9 IV. of Protein with Pepsin. 1. Color the final results as you see them in your tubes after 45 minutes of digestion and the Biuret s test. A B C 2. In which tube was protein digested? (pick A, B, or C) 3. How did you know that? 4. Were the results what you expected?. Explain: 5. Why was HCl included in the digestion of proteins with pepsin? V. of Starch with Amylase. 1. Color the results of the Lugol s test as you see them in your tubes at each time point. Time 0 10 min 20 min 30 min 40 min A B C D E F 2. In which tube was digestion most complete? (pick A-F) 3. How did you know that? 4. Were the results what you expected?. Explain: Page9

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