GENA PARTNERSHIP TEACHING PLAN LEARNING CYCLE: 5E Elizabeth Schaefer and Ambro Van Hoof

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1 GENA PARTNERSHIP TEACHING PLAN LEARNING CYCLE: 5E Elizabeth Schaefer and Ambro Van Hoof Note: Our teaching plan is not one lesson. It is a series of lessons throughout AP Biology connected by the unifying theme of lactose intolerance. Each category actually encompasses activities that will be presented over time. STAGE Engage Stimulates curiosity, addresses students prior knowledge ACTIVITY Posters from Got milk? campaign phrase replaced with Got lactase? PTC paper taste test review phenotype, genotype, dominance; then relate to lactose tolerance/intolerance (survey) Pre-Lab Demonstrations for Transformation Lab: X-gal, DNA quantities, Medical lab applications Explore Satisfies curiosity, builds upon prior knowledge DNA models to review nucleotide sequences, triplet codes Organic models to review polypeptide sequences and protein structure Relate genotypes/phenotypes to PTC tasters vs. non-tasters and to lactose tolerance/intolerance Organic model to review structure of lactose Explain Students gain understanding of the concept, new terms are introduced Discuss chemistry of lactose tolerant vs. intolerant individuals Power Point - Relate phenotype to its chemical (protein) component and DNA sequence LAB: Lactase Enzyme Lab Introduce topic of evolutionary influences on phenotypic changes. READ: GOT LACTASE? article ( ews/070401_lactose) Discovery Video clips Manipulating DNA

2 Elaborate Application of concepts recently learned, expansion of knowledge LAB: Curing Lactose Intolerant Bacteria (using Edvotek Kit #221 Transformation of E. coli with pgal blue colony) Attend Genetics Update Conference University of St. Thomas, Houston, TX: Students listen to 4 hour lecture on up-to-theminute topics in genetics Evaluate Reviews concepts recently learned, assesses student understanding Got Lactase? Assessment Questions Assessment questions Enzyme Lab Post-lab Group Discussion of Enzyme Lab objectives Analysis/assessment questions Bacterial Transformation Lab Post-lab Group Discussion and presentation of Transformation Lab Objectives AP Free Response question (Enzymes and enzyme specificity? use rubric to score AP Free Response question (DNA protein trait connection) use rubric to score

3 LAB TWO ENZYME CATALYSIS Lactase Enzyme Lab This lab will examine the specificity of the enzyme, lactase, to its specific substrate, lactose. Students will observe the actions of lactase and how shape is important to enzyme reactions. Objectives After completing this lab, the student will be able to: understand the specificity of an enzyme to a specific substrate; explain what will happen when an enzyme is denatured. Time required for lesson 30 minutes Introduction Lactose, the sugar found in milk, is a disaccharide composed of glucose and galactose (both six-sided sugars). Sucrose, ordinary table sugar, is also a disaccharide composed of fructose and glucose. Glucose is a six-sided sugar and fructose is a five-sided sugar. Lactase is an enzyme that breaks lactose down into galactose and glucose. Lactase can be purchased in pill form by people who are lactose intolerant. These people lack the enzyme, lactase, and cannot break down the sugar lactose into its component parts. Although lactose is similar to sucrose, lactase will break down only lactose because of the shape of the sugar. In this lab, you will see lactase break lactose down into galactose and glucose. You will also observe what happens if the shape of lactase is changed due to heating.

4 Materials/resources Lactase tablets 40 ml of regular milk 10 ml of lactose-free milk Distilled water sucrose (table sugar) Seven 50 or 100 ml beakers 10 ml syringe Marking pencil Timer Hot plate Glucose test strips (with color indicator chart) Procedures Solution preparation (prepared ahead of time) 1. Enzyme solution: Crush six lactase tablets; add to three hundred milliliters of distilled water. Stir until the tablets have completely dissolved. 2. Regular milk: this solution contains the lactose. 3. Sucrose solution: Add 10 grams of sugar to 200 ml of water. Stir until dissolved. 4. Denatured enzyme solution: (prepare one per class) o Place 50 ml of enzyme solution into a Pyrex test tube. o Add two hundred milliliters of water to a four hundred milliliters Pyrex beaker. o Place the test tube in the beaker (gently laying the test tube so it rests on the side of the beaker.) o Place the beaker with test tube on the hot plate. o Boil the water in the beaker for thirty minutes. o Let the solution cool to room temperature. Part A. Testing milks for glucose 1. Lab two of the beakers with the following labels: 2. Add 10 ml of the correct milk to each beaker. 1. Regular milk 2. Lactose-free milk 3. Test each for glucose with the glucose test tape. After 2 minutes, read the results. Record this data in Table A. If there was glucose present, mark a + in the table. If glucose was absent, mark a - in the table.

5 Table A: GLUCOSE TEST Type of Solution + or - Glucose Result Regular milk (with lactose) Lactose-free milk Analysis Questions 1. According to the glucose test, does regular milk contain glucose? Explain why or why not. 2. According to the glucose test, does lactose-free milk contain glucose? Explain why or why not. Part B. Enzyme activity 1. Label the remaining five beakers with the following labels: 1. Beaker A: regular milk and enzyme solution 2. Beaker B: regular milk and water 3. Beaker C: regular milk and denatured enzyme solution 4. Beaker D: sucrose solution and enzyme solution 5. Beaker E: sucrose solution and water 2. In Beaker A add 10 ml of regular milk and 5 ml of enzyme solution. 3. Swirl for 3 minutes. Test for glucose with the glucose test tape. After 2 minutes, read the results. Record this data in Table B. If there was glucose present mark a + in the table. If glucose was absent, mark a - in the table. 4. In test tube B add 10 ml of regular milk and 5 ml of distilled water. 5. Repeat Step In test tube C add 10 ml of regular milk and 5 ml of denatured enzyme solution. 7. Repeat Step In test tube D add 10 ml of the sucrose solution and 5 ml of enzyme solution. 9. Repeat Step In test tube E add 10 ml of the sucrose solution and 5 ml of distilled water. 11. Repeat Step 3.

6 Table B: GLUCOSE TEST Type of Solution + or - Glucose Result Beaker A: milk and enzyme solution Beaker B: milk and water Beaker C: milk and denatured enzyme solution Beaker D: sucrose solution and enzyme solution Beaker E: sucrose solution and water Conclusion and assessment 12. Why did the enzyme react to lactose but not to sucrose? 13. Diagram and describe the lactose and lactase reaction. 14. What happened when the enzyme was boiled? 15. Another way to affect the enzyme is by lowering the ph of the solution. However, lactase is supposed to be able to work in the stomach. Would lowering the ph of the enzyme solution affect the enzyme? Why or why not? 16. What type of reaction is this? Dehydration or hydrolysis?

7 GOT LACTASE? FORMATIVE ASSESSMENT QUESTIONS: (Use with Got Lactase? article 1. Are you lactose tolerant or lactose intolerant? Based on the information in this article, explain how your genes affect your ability (or lack of ability) to digest milk. 2. Describe the concepts of genotype and phenotype of a lactose tolerant individual. 3. Explain how a lactose tolerance mutation would spread through a human population that herds cattle. Make sure to include the concepts of variation, selection, and inheritance in your explanation.

8 Pre-Lab Demos: Bacterial Transformation Lab Some possible demos: 1. lactaid turns X-gal blue. goal: explain to the students what X-gal is, and what lactase does to it. Connects this lab with the enzyme catalysis lab. Bring: lactaid pill and 50ml sterile water to dissolve lactaid pill (or lactase drops) and solution of X-gal. Do: Add 25 µl of the X-gal to 250 µl of the dissolved lactase will develop a blue color over a few minutes time course. More detail: -dissolve one pill of Walgreens lactose fast acting relief in 50 ml water. Note: I assume other brands work too, but this is the one we used because there was a walgreens across the street from the lab. Note: I used distilled water out of habit, but tap water should work too. Note: it takes about minutes with intermittent shaking for the pill to fall apart. So start dissolving before the class starts Note: the pills contain filler that doesn t dissolve. I suspect the microcrystaliine cellulose is the culprit. Therefore, the pill never truly dissolves, and there always is a lot of white precipitate left. If this bothers you, you should be able to filter it out with a coffee filter. Note: I imagine that the lactase enzyme is not all that stable in water, so I dissolved a fresh pill just before each class period. -Add 250 µl of the dissolved pill to 25 µl of a 2% X-gal stock solution in front of the students. Note: I pointed out that I was only using 1/200 th of a pill -After a minute or two the mixture will turn blue. (I think the students really got why they used X-gal after this demo, because they could see it as it was passed around the classroom) -I also took a solutions of 40% glucose and galactose to show that the products of lactose digestion are not easily detectable by eye. 2 Lactase production is used in medical clinics to distinguish between E. coli and Salmonella. -Goal: relate the lab to something medically important, since all the students want to be doctors (or movie stars or athletes) when they grow up. Reinforce that normally E. coli is lac +, and we are using a mutant (or prevent the misconception that E. coli is lactase deficiency). -Bring: an LB plate, an LB-X-gal plate, and a MacConkey agar plate with E. coli and Salmonella streaked on it: the two species look exactly the same on LB, but very different on X-gal and on MacConkey. Note: most lab E. coli strains are lacz mutants, and won t work. Note: for most WT E. coli strains you do have to include IPTG to induce the lac genes. -Do: Pass plates around.

9 LAB6A: TRANSFORMATION OF E. coli with pgal INTRODUCTION E. coli. Escherichia coli (or E. coli for short) is a bacterium that is normally found in the lower intestines of warm blooded animals. They are part of the normal flora in the human gut. Some strains of E. coli are pathogenic and can cause food poisoning and other diseases in humans, but the strain of E. coli that you will be using in this lab is a non-pathogenic strain that does not cause disease in healthy individuals. Although this strain of E. coli is non-pathogenic, you should wear gloves, handle the strain with care, properly dispose of all waste, and wash your hands before leaving the lab. E. coli is also the work-horse of biotechnology, and transformation of E. coli is carried out daily in 1000 s of labs around the world. One example is that some strains of E. coli have been transformed with the human gene for insulin. These bacteria now make insulin, which is an important drug for the treatment of diabetes. Human insulin produced by E. coli is marketed under the name humulin. E. coli Lactase breaks down lactose and X-gal. Normal strains of E. coli have a gene, called LacZ that codes for a lactase enzyme (people studying E. coli usually call this enzyme β-galactosidase, but it catalyzes the same reaction as lactase). Lactase degrades lactose, a disaccharide that consists of two simple sugars galactose and glucose. Although lactase is very specific, and won t degrade other disaccharides such as sucrose, it will degrade some other compounds. One such compound is called X-gal by scientists. X-gal consists of galactose and 5-bromo-4-chloro-3-hydroxyindole (the official name for X-gal is 5-bromo-4-chloro-3- indolyl-beta-d-galactopyranoside, which even for scientists is hard to remember). Dilute solutions of lactose, glucose and galactose all are colorless to the human eye, which makes the lactose degradation reaction difficult to detect. However, when lactase breaks down X-gal, a blue compound is formed. Therefore scientist often use X-gal to detect the presence of lactase.

10 Medical labs tell E. coli apart from Salmonella by the production of lactase. Many different kinds of bacteria can cause food poisoning, and it is hard to distinguish one species from the other. Specifically, E. coli and Salmonella are very hard to tell apart. One difference is that E. coli makes lactase, and Salmonella does not. Doctor s offices use this to tell the two apart by plating bacteria on specialized media. They use MacConkey agar which is turned pink by lactase. Thus, if the media turns pink, the bacteria might be E. coli, and if the media stays white, the bacteria might be Salmonella. Although doctor s offices use MacConkey agar, they could also use X-gal plates. Food poisoning by E. coli is often caused by bad beef and does not require antibiotics, while Salmonella poisoning is often from bad chicken, and requires treatment with antibiotics. Thus, detecting lactase can help doctors decide whether to prescribe antibiotics and can help officials to focus on suspected foods. Water companies count lactase-producing bacteria to measure fecal contamination. The water company tests whether lactase-producing bacteria are present in your drinking water as a measure of water quality. Your family receives a yearly water quality report that lists how many coliform bacteria are present in the drinking water. Coliform bacteria are defined as rod-shaped, Gram-negative, non-spore forming organisms that ferment lactose. Coliform bacteria are abundant in the feces of most warm-blooded animals. The presence of coliform bacteria is therefore an indication of contamination with feces, and low water quality. Lactose intolerant E. coli. Although E. coli normally has a lactase gene, this lab will use a strain of E. coli that was developed by scientist and that has a mutation in the gene for lactase. This strain can not break down lactose. Essentially, the mutant bacteria suffer from lactose intolerance. Bacterial transformation. Bacterial transformation is a natural process whereby bacteria take up naked DNA from the environment, resulting in the stable addition of new genetic material to the bacterium and its descendants. Transformation of E. coli with plasmid DNA is very important in biotechnology. It allows scientist to rapidly produce large quantities of plasmid DNA, which then is used for many different applications. Transformation efficiency is defined by the number of transformed E. coli cells per microgram of DNA. Transformed E. coli cells are hard to count, but when they are plated on the right media, each transformed cell multiplies and forms a colony of billions of cells, which can be easily counted. For example, 10 ng of DNA were used to transform E. coli, and the cells were allowed to recover in 1 ml broth. One tenth of the broth (or 100 µl) was plated on agar plates that only allows transformants to grow, and 100 colonies formed. If 100 colonies grew out of the 100 transformed bacteria present in 100 µl, then 1000 bacteria were present in 1 ml. If 10 ng gives 1000 transformants, then1 µg would give 100,000 transformants, and the transformation efficiency is said to be 10 5 µg -1. For many applications transformation efficiencies of 10 5 to 10 7 µg -1 are sufficient.

11 Transformation is never 100% efficient. However, since a typical transformation experiment will use a billion cells, even if only 1 in every 10,000 cells gets transformed this will yield 100,000 transformants. The 1 in 10,000 cells might be hard to find, if it were not for the fact that only transformed colonies will grow on selective media. Scientists used bacterial transformation to prove that genes are made of DNA. Gregor Mendel discovered genes in 1865, but for about 80 years scientist did not know what genes were made of. Many had a hunch that they were made out of proteins, but that proved to be false. The first experiments to prove that genes are made of DNA were carried out by Oswald Avery, Colin MacLeod and Maclyn McCarty in 1944 (see also page of your text book). They worked on a species of bacteria called Streptococcus pneumoniae that either formed smooth colonies or rough colonies. They showed that they could extract the rough gene out of bacteria that formed rough colonies, and when they added the gene to bacteria that usually formed smooth colonies, these bacteria were transformed into bacteria that formed rough colonies. They then took the gene extract, and treated it with an enzyme that degrades proteins (protease). This had no effect: the genes could still transform, and they concluded that the genes were still intact when proteins were degraded. They also treated the gene extract with an enzyme that degrades DNA (DNase), and noticed that this destroyed the rough gene. This indicated that the rough gene was made of DNA. Many experiments since then have shown that other genes in bacteria and eukaryotes are also made of DNA. The pgal plasmid. Plasmids are circular molecules of DNA. Many different plasmids can be used in transformation experiments. The plasmid in this lab is called pgal and contains two genes Amp R and LacZ. The LacZ gene codes for lactase, and turns the media blue if X-gal is present. β-lactamase production makes E. coli ampicillin resistant. The Amp R gene codes for an enzyme called β-lactamase. β-lactamase breaks down a class of antibiotics called β-lactams. Penicillin, amoxicillin and ampicillin are all β-lactam antibiotics. While β- lactams antibiotics will kill bacteria, the breakdown products are harmless to bacteria. β-lactamase is an extracellular enzyme that is secreted from E. coli. Once outside the cell, the enzyme diffuses and inactivates ampicillin. Normal E. coli is killed by ampicillin, but E.coli that make β-lactamase can grow on plates that contain ampicillin. Small white satellite colonies may appear around a large blue colony of transformed cells. Cells in the satellite colony are not transformed, but can grow because the nearby transformed cell has secreted enough beta-lactamase to break down all the ampicillin in the media nearby.

12 Brief description of the experiment: (Experiment instructions can be found at: In this experiment, the student will transform host bacteria with plasmid DNA. The transformants acquire antibiotic resistance and form blue colonies on plates containing X-gal. The number of bacteria will be counted and the transformation efficiency determined. Before you start the experiment: 1. Read all instructions before starting the experiment and make sure you understand them. 2. Write a hypothesis that reflects the experiment and predict experimental outcomes: Objective of today s lab: The objective of this experiment module is to develop an understanding of the biological process of bacterial transformation by plasmid DNA. The student should be able to: 1. Explain that the LacZ gene codes for lactase, which allows bacteria to breakdown lactose and X- gal; 2. Explain that the Amp R gene codes for beta-lactamase, which allows bacteria to grow on media containing ampicillin; 3. Explain that LacZ and Amp R are linked genes because they are in the same DNA molecule; 4. Determine whether the LacZ gene on the plasmid is dominant or recessive relative to the LacZ gene on the chromosome, and to explain why; 5. Explain the roles of lactase in E. coli and humans. Observations/Data Analysis: Draw your observations in the circles below. Be sure to use correct colors. Record the number of colonies below each drawing. (A convenient method to keep track of counted colonies is to mark the colony with a lab marking pen on the outside of the plate.) X-GAL/Control 1 AMP/X-GAL/Control 2 AMP/X-GAL/pGAL # colonies # colonies # colonies DETERMINATION OF TRANSFORMATION EFFICIENCY Transformation efficiency is a quantitative determination of how many cells were transformed per 1 µg of plasmid DNA. In essence, it is an indicator of how well the transformation experiment worked. You will calculate the transformation efficiency from the data you collect from your experiment. 1. Count the number of colonies on the plate with ampicillin that is labeled: AMP/X-GAL/pGAL 2. Determine the transformation efficiency using the formula:

13 Number of final vol at Number of transformants X recovery (ml) = transformants µg of DNA vol plated (ml) per µg Quick Reference for this experiment: 25 ng (0.025 µg) of DNA used final volume at recovery 1.0 ml volume plated 0.25 ml Your Calculated Transformation Efficiency: transformants per µg Results/Conclusions: After conducting the lab and analyzing the results, answer the following questions in the space provided: 1. Why did you only count blue colonies? 2. Did you observe any satellite colonies? Why are they white? 3. What would happen if cells from a transformed colony were put on a new AMP/X-gal plate? 4. What would happen if cells from a satellite colony were put on a new AMP/X-gal plate? 5. Why did the control transformation not give any colonies on the AMP/X-gal plate? 6. Why are there so many colonies on the X-gal plate? 7. Were all the bacteria in the pgal transformation transformed? How can you tell? 8. Did transformation occur? What is the evidence?

14 9. What are some of the reasons why transformation may be unsuccessful? 10. Does this experiment show that the lactase gene and the Amp R gene are made of DNA? Why, or why not? 11. Is the LacZ gene on the plasmid dominant over or recessive to the mutant LacZ gene on the chromosome? 12. Why do you think E. coli normally has a lactase gene? Why do you have a lactase gene? 13. Do you think it is possible to cure human lactose intolerance by introducing a lactase gene into the body? What technical considerations should you keep in mind if you want to develop this treatment? What ethical considerations should you keep in mind if you want to develop this treatment?

15 FORMATIVE ASSESSMENT Bacterial Transformation Lab Assign each lab group one of the following topics (based on the lab s stated objectives). Each group will brain-storm then a spokesperson for each group will report to the entire class. 1. Explain the genotypic and phenotypic implications of the LacZ gene for E. coli. 2. Explain the genotypic and phenotypic implications of the Amp R gene for E. coli. 3. Explain the connection between the LacZ and Amp R in this experiment. 4. Determine whether the LacZ gene on the plasmid is dominant or recessive relative to the LacZ gene on the chromosome, and explain why. 5. Explain the specific roles of lactase in E. coli and humans.

16 Commentary on Lactase Enzyme Lab: The lactase lab is based on the required AP Biology catalase enzyme lab. In the present format, this lactase lab is simply a qualitative look at the lactase enzyme, in keeping with the lactose intolerance theme. Dr. van Hoof is in the process of adding the AP Biology-required quantitative aspect to the lab (enzymatic activity over time). The qualitative portion of the lab is fairly inexpensive, less than $20, and all components can be purchased locally. The only preparation involves dissolving the lactase tablets. The lab takes approximately 30 minutes. Commentary on Got Lactase? article: This article is an excellent discussion tool for bringing together several concepts. It emphasizes the concept of gene protein trait. In addition, it brings in evolutionary significance of mutations and natural selection and convergent evolution. Because the students understand the genetics of lactose tolerance/intolerance, the idea of natural selection makes sense to them. Commentary on Bacterial Transformation Lab: This lab is also an AP Biology requirement. I have tried several versions of Transformation Labs, but this one really was significance to the students because of the lactose intolerance theme. Last year, my students performed the Glowing Bacteria version. While it was cool to see the glowing colonies, there was no ownership/relevance to the students. The Edvotec kit price is $99 for 10 lab groups. This is basically the same price as some of the other kits that I have used. As with all transformations labs, there is a great deal of time-sensitive preparation over a period of several days. The Edvotec kit utilizes E. coli cells that have been made competent already, so you simply reconstitute and incubate 24 hours before the lab. The actual lab spans two days. The first day requires approximately 75 minutes. This includes about 15 minutes of a pre-lab discussion and demonstrations, which can be done the day before, if needed. (Although the demos are not required, they added so much to this lab. This was where Dr. van Hoof was vital, as I do not have access to all of the items that he brought.) The second day, observations and analysis, requires approximately 30 minutes. The formative assessment based on the lab s objectives was a excellent way to assess understanding of concepts. This will be used to determine if a concept must be reviewed or if any other adjustments must be made leading up to the lab or with the lab itself.

17 SUMMATIVE ASSESSMENT AP BIOLOGY EXAM FREE RESPONSE QUESTIONS (23 minutes each) Answers must be handwritten and in essay form. Outline form is NOT acceptable. Labeled diagrams may be used to supplement discussion, but in no case will a diagram alone suffice. Use this page for outline/rough draft; final answer must be on second page. Protein Structure and Function The physical structure of a protein often reflects and affects its function. a. Describe three types of chemical bonds/interactions found in proteins. For each type, describe its role in determining protein structure. b. Discuss how the structure of a protein affects the functions of (1) regulation of enzyme activity and (2) cell signaling. c. Abnormal hemoglobin is the identifying characteristic of sickle cell anemia. Explain the genetic basis of the abnormal hemoglobin. Explain why the sickle cell allele is selected for in certain areas of the world. Enzyme Structure and Function Enzymes are biological catalysts. d. Relate the chemical structure of an enzyme to its specificity and catalytic activity. e. Design a quantitative experiment to investigate the influence of ph or- temperature on the activity of an enzyme. f. Describe what information concerning the structure of an enzyme could be inferred from your experiment. Molecular Biology Scientists seeking to determine which molecule is responsible for the transmission of characteristics from one generation to the next knew that the molecule must (1) copy itself precisely, (2) be stable but able to be changed, and (3) be complex enough to determine the organism s phenotype. a. Explain how DNA meets each of the three criteria stated above. b. For each of the criteria stated above, describe experimental evidence used to determine that DNA is the hereditary material.

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