Sample w/ water w/ pancreatin Observation Exploratory questions: 3. What type of hydrolysis is used in this part of experiment? Explain. What other enzyme/s is/are responsible for lipid hydrolysis? How does triglyceride hydrolysis offers from cholesterol ester hydrolysis?
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Enzymatic Hydrolysis of Cooking Oil.
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- topic: ISOLATION AND CHARACTERIZATION OF CARBOHYDRATES 1. Erythrose is an aldoterose. Describe the result when it is subjected to each of the following tests:a. Molisch’s Testb. Barfoed’s Testc. Benedict’s Testd. Seliwanoff’s Test2. Illustrate the reaction and identify the principle involved in the Nelson test.Answer the ff. questions: 1. To which class does each enzyme belong? Explain your answers. a.) pyruvate decarboxylase b.) alanine aminotransferase c.) alcohol dehydrogenase d.) hexokinase 2. Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis? 3. Some plants contain compounds that inhibit serine proteases. It has been hypothesized that these compounds protect the plant from proteolytic enzymes of insects and microorganisms that would damage the plant. Tofu, or bean curd, possesses these compounds. Manufacturers of tofu treat it to eliminate serine protease inhibitors. Why is this treatment necessary?What are the corresponding answers, respond briefly, site sources Enzyme; Triacylglycerol Lipase Enzyme Official Name (write N/A if not applicable) Enzyme Official Number (4 digits) Simple or Conjugated Enzyme (specify cofactor if applicable) Type of Reaction Catalyzed Substrate Optimum pH Optimum Temperature Function/s Disease (give 1 and describe briefly) Enzyme: Urease Enzyme Official Name (write N/A if not applicable) Enzyme Official Number (4 digits) Simple or Conjugated Enzyme (specify cofactor if applicable) Type of Reaction Catalyzed Substrate Optimum pH Optimum Temperature Function/s Disease (give 1 and describe briefly)
- Case Study: Case Study: Catalase Activity Catalase H,O, 0 + O2 (2) Catalase is an enzyme that converts hydrogen peroxide (H,O) to oxygen and water. An experiment investigated the effect of temperature on the rate of the catalase reaction Small (10 cm) test tubes were used for the reactions, each containing 0.5 cm of enzyme and 4 cm of hydrogen peroxide. Reaction rates were assessed at four temperatures (10°C, 20°C, 30'C. and 60 C). For each temperature, there were two reaction tubes (e.g. tubes 1 and 2 were both kept at 10°C). The height of oxygen bubbles present after one minute of 10°C 20°C 30°C 60°C Height of охудen bubbles 4 cm H,02+ 0.5 cm erzyme reaction was used as a measure of the reaction rate: a laster reaction rate produced more bubbles. The entire experiment, involving eight tubes, was repeated on two separate days. Tubes Tubes Tubes 1 & 2 Tubes 3 & 4 5 & 6 7 & 8 1. What is the purpose of this experiment? inrestrgatee effect of demperalure on the rate ot he 2. Write a…Result nad Discussion Lead Acetate Reaction: Samples: lysine, cysteine, methionine Reagents: 10% Sodium Hydroxide (NaOH) and Lead Acetate Pb(CH3COO)2 -To 1 ml of the amino acid solution taken in a test tube, add few drops of sodium hydroxide (40%) and boil the contents for 5-10 mins over a bunsen burner. Cool the contents and add few drops of 10% Lead acetate solution and observe.Please help me answer these questions. Thanks. 6. Summarize your results with a data table with the different carbohydrates and the resulting reaction with the different tests. (link below) 7. What are the structural differences between glucose, sucrose and starch? https://docs.google.com/document/d/1ew0oZRcy3JWP0YWcRdgjJ906u0rf75QpLpHvLIGv05I/edit?usp=sharing
- Question:- Based on the figure below, predict what peptide bond could be the substrate of each protease(The bond marked in blue is where hydrolysis occurs, choose 2 peptides per protease type) Chymotrypsin:_________ Trypsin:_________ Elastase:_________ 1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SGAnswer the following questions summarizing the information in the lab: 1. Give two SPECIFIC examples of when, where, and why temperature and pH are important to the activity of enzymes in your body. Explain in your own words. 2. Briefly summarize your conclusions on the effects of temperature and pH on the action of the enzymes we used. What are the optimal conditions for peak catalase activity? 3. Design an experiment to test the effect of SUBSTRATE concentration on enzyme activity. Identify the independent and dependent variable. State your hypothesis and prediction. Briefly explain the protocol. What effect do you think changing the concentration of a substrate will have on the rate of activity?BSC1010C Enzymes & Cellular Regulation Dr. Harris 4. Compare the rate of the pepsin-catalyzed reaction at pH = 1.5 with the rate of the lipase- catalyzed reaction at pH = 1.5. 5. Compare the rate of the pepsin-catalyzed reaction at pH = 8.0 with the rate of the lipase- catalyzed reaction at pH = 8.0. 6. Based on your understanding of protein structure, explain in detail the effect of exposing an enzyme to a pH outside its optimal range. Include a discussion of the effect on both the structure and function of the enzyme. 7. At what pH values is lipase likely to be denatured? Explain your answer.
- Topic: Co-Enzyme Q10 Question: What does it mean when asked to explain the evidence behind medicinal chemistry of the CAM agent, and if the chemical structures relate to it's effects.BIOMOLECULES Please answer the questions properly. - Multiple choice Qyestion 1: If a cell has an adequate supply of adenine nucleotides but requires more guanine nucleotides for protein synthesis: 1. Glutamine-PRPP amidotransferase will not be fully inhibited. 2. AMP will be a feedback inhibitor of the condensation of IMP with aspartate. 3. ATP will stimulate the production of GMP from IMP. 4. ATP will inhibit nucleoside diphosphate reductase. А. 1, 2, and 3 В. 2 and 4 С. 1, 2, 3, and 4 D. 1 and 3Course : BiochemistryChapter : Amino acid metabolism In the catabolic reaction of amino acids, ammonia is produced as a side compound.Ammonia is so poisonous that it must be removed from the body in the form of urea.Please explaina. the reaction of amino acids with ketoglutarate to produce ammoniab. the urea cyclec. where do reactions a and b occur? Please write the answer on paper ( Handwriting )And provide pict with detail explanation because i want to learn every steps of the processThank you