Textbook Question
One mechanism by which lead exerts its poisonous effect on enzymes can be stopped by chelation therapy with EDTA. Describe this type of lead poisoning and explain why it is reversible.
Ch.19 Enzymes and Vitamins
McMurry8th EditionFundamentals of General, Organic, and Biological ChemistryISBN: 9780134015187
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Table of contents
- Ch.1 Matter and Measurements27
- Ch.2 Atoms and the Periodic Table20
- Ch.3 Ionic Compounds8
- Ch.4 Molecular Compounds23
- Ch.5 Classification & Balancing of Chemical Reactions12
- Ch.6 Chemical Reactions: Mole and Mass Relationships28
- Ch.7 Chemical Reactions: Energy, Rate and Equilibrium64
- Ch.8 Gases, Liquids and Solids24
- Ch.9 Solutions52
- Ch.10 Acids and Bases25
- Ch.11 Nuclear Chemistry22
- Ch.12 Introduction to Organic Chemistry: Alkanes57
- Ch.13 Alkenes, Alkynes, and Aromatic Compounds47
- Ch.14 Some Compounds with Oxygen, Sulfur, or a Halogen50
- Ch.15 Aldehydes and Ketones45
- Ch.16 Amines42
- Ch.17 Carboxylic Acids and Their Derivatives57
- Ch.18 Amino Acids and Proteins82
- Ch.19 Enzymes and Vitamins63
- Ch.20 Carbohydrates44
- Ch.21 The Generation of Biochemical Energy65
- Ch.22 Carbohydrate Metabolism45
- Ch.23 Lipids42
- Ch.24 Lipid Metabolism33
- Ch.25 Protein and Amino Acid Metabolism24
- Ch.26 Nucleic Acids and Protein Synthesis45
McMurry8th EditionFundamentals of General, Organic, and Biological ChemistryISBN: 9780134015187Not the one you use?Change textbook
Chapter 19, Problem 64
The meat tenderizer used in cooking is primarily papain, a protease enzyme isolated from the fruit of the papaya tree. Why do you suppose papain is so effective at tenderizing meat?
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Understand that papain is a protease enzyme, which means it catalyzes the breakdown of proteins into smaller peptides or amino acids by hydrolyzing peptide bonds.
Recognize that meat is primarily composed of muscle proteins, such as collagen and myosin, which contribute to its toughness and structure.
Consider that when papain is applied to meat, it interacts with these proteins and breaks them down into smaller fragments, reducing the structural integrity of the meat and making it more tender.
Acknowledge that the enzymatic activity of papain is most effective under specific conditions, such as optimal temperature and pH, which are often achieved during cooking or marination.
Conclude that papain's ability to hydrolyze protein bonds is the key reason it is effective at tenderizing meat, as it softens the texture by breaking down the protein structure.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Protease Enzymes
Protease enzymes are biological catalysts that break down proteins into smaller peptides or amino acids. They play a crucial role in various biological processes, including digestion and metabolism. In the context of meat tenderization, proteases like papain cleave the peptide bonds in muscle fibers, making the meat softer and easier to chew.
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Intro to Enzymes Concept 1
Papain
Papain is a specific type of protease enzyme derived from the papaya fruit. It is known for its ability to hydrolyze proteins effectively, which is why it is commonly used in cooking as a meat tenderizer. Papain's effectiveness is attributed to its broad substrate specificity, allowing it to act on various types of proteins found in meat.
Meat Structure
Meat is composed of muscle fibers, connective tissues, and fat, all of which contribute to its texture. The toughness of meat is largely determined by the amount and type of connective tissue present. By breaking down these proteins, enzymes like papain can alter the meat's structure, resulting in a more tender and palatable product.
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Related Practice
Textbook Question
Activation of a zymogen is by covalent modification. How might phosphorylation or dephosphorylation (also covalent modification) modify an enzyme to make it more active (or more inactive)?
Textbook Question
What kind of inhibition (uncompetitive, competitive, or irreversible) is present in each of the following:
c. The antibiotic deoxycycline inhibits the bacterial enzyme collagenase, slowing bacterial growth. Deoxycycline does not fit into the active site of collagenase and binds elsewhere on the enzyme.
Textbook Question
What kind of inhibition (uncompetitive, competitive, or irreversible) is present in each of the following:
a. Penicillin is used to treat certain bacterial infections. Penicillin is effective because it binds to the enzyme glycopeptide transpeptidase and does not dissociate.
Textbook Question
What are the cellular advantages to feedback inhibition?
Textbook Question
Why do allosteric enzymes have two types of binding sites?