Table of contents

1. Matter and Measurements4h 31m
2. Atoms and the Periodic Table5h 23m
3. Ionic Compounds2h 18m
4. Molecular Compounds2h 18m
5. Classification & Balancing of Chemical Reactions3h 17m
6. Chemical Reactions & Quantities2h 27m
7. Energy, Rate and Equilibrium3h 46m
8. Gases, Liquids and Solids3h 25m
9. Solutions4h 10m
10. Acids and Bases3h 29m
11. Nuclear Chemistry56m
BONUS: Lab Techniques and Procedures1h 38m
BONUS: Mathematical Operations and Functions47m
12. Introduction to Organic Chemistry1h 34m
13. Alkenes, Alkynes, and Aromatic Compounds2h 12m
14. Compounds with Oxygen or Sulfur1h 6m
15. Aldehydes and Ketones1h 1m
16. Carboxylic Acids and Their Derivatives1h 11m
17. Amines39m
18. Amino Acids and Proteins1h 51m
19. Enzymes1h 37m
20. Carbohydrates1h 41m
21. The Generation of Biochemical Energy2h 8m
22. Carbohydrate Metabolism2h 22m
23. Lipids2h 26m
24. Lipid Metabolism1h 45m
25. Protein and Amino Acid Metabolism1h 37m
26. Nucleic Acids and Protein Synthesis2h 54m

19. Enzymes

Factors Affecting Enzyme Activity

GOB Chemistry

19. Enzymes

Factors Affecting Enzyme Activity

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4:34 minutes

Problem 43a

Textbook Question

Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
a. changing the pH to 3.0

Verified step by step guidance

Understand the role of trypsin: Trypsin is an enzyme that catalyzes the hydrolysis of polypeptides in the small intestine. Enzymes have an optimum pH range where they function most effectively, and for trypsin, this range is 7.7 to 8.0.

Recall the effect of pH on enzyme activity: Enzymes are sensitive to pH changes because pH affects the ionization of amino acid side chains in the active site. Significant deviations from the optimum pH can lead to denaturation or reduced activity.

Analyze the given condition: The problem states that the pH is changed to 3.0, which is highly acidic compared to trypsin's optimum pH range. This drastic change in pH can disrupt the enzyme's structure and active site functionality.

Predict the impact on the reaction rate: At pH 3.0, trypsin is likely to lose its catalytic efficiency due to denaturation or altered active site geometry, leading to a significant decrease in the rate of the trypsin-catalyzed reaction.

Conclude the reasoning: The rate of the trypsin-catalyzed reaction will be negatively affected because the enzyme is no longer operating within its optimal pH range, and its ability to bind substrates and catalyze reactions is compromised.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Enzyme Activity and pH

Enzymes, including trypsin, have an optimal pH range in which they function most effectively. Deviations from this range can lead to denaturation or reduced activity, as the enzyme's structure and active site may be altered. For trypsin, which operates best at a pH of 7.7 to 8.0, a drop to pH 3.0 would significantly impair its catalytic ability.

Trypsin Function

Trypsin is a serine protease that specifically cleaves peptide bonds in proteins, facilitating digestion in the small intestine. It is secreted as an inactive precursor, trypsinogen, and activated by other enzymes. Understanding its role in protein digestion is crucial for analyzing how changes in conditions affect its activity.

Reaction Rate and Environmental Conditions

The rate of enzyme-catalyzed reactions is influenced by various environmental factors, including pH, temperature, and substrate concentration. Changes in these conditions can either enhance or inhibit the reaction rate. In the case of trypsin, lowering the pH to 3.0 would likely decrease the reaction rate due to unfavorable conditions for enzyme activity.

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Adults who are lactose intolerant cannot break down the disaccharide in milk products. To help digest dairy food, a product known as Lactaid can be added to milk and the milk then refrigerated for 24 hours.

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b. What might happen to the enzyme if the Lactaid were stored at 55 °C?

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Textbook Question

Fresh pineapple contains the enzyme bromelain that hydrolyzes peptide bonds in proteins.

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a. The directions for a gelatin (protein) dessert say not to add fresh pineapple. However, canned pineapple where pineapple is heated to high temperatures can be added. Why?

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Fresh pineapple contains the enzyme bromelain that hydrolyzes peptide bonds in proteins.

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b. Fresh pineapple is used in a marinade to tenderize tough meat. Why?

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Why do enzymes function only under mild conditions?

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Textbook Question

How would the following changes affect enzyme activity for an enzyme whose optimal conditions are normal body temperature and physiological pH?

a. raising the temperature from 37 °C to 60 °C

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Textbook Question

The enzyme urease functions in the body to catalyze the formation of ammonia and carbon dioxide from urea as shown:

Describe what effect the following changes would have on the rate of this reaction assuming a steady state has been reached:

a. adding excess urea

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Textbook Question

Pepsin, an enzyme that hydrolyzes peptide bonds in proteins, functions in the stomach at a pH optimum of 1.5 to 2.0. How is the rate of a pepsin-catalyzed reaction affected by each of the following conditions?

a. increasing the concentration of proteins

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Textbook Question

c. running the reaction at 0 °C

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