Chapter 11: Proteins: Amino Acids and Peptides Part 2
This flashcard set explores the role of proteins and amino acids in food science and nutrition. Topics include PKU and essential amino acid needs, plant-based protein sources like soy, limiting amino acids in cereals and legumes, protein combinations for complete nutrition, and amino acid properties related to structure and function. Great for students studying nutrition, dietetics, or biochemistry.
Name the 3 characteristics of denaturation.
Loosening or unfolding of the tertiary and sometimes secondary structure
Sometimes reversible
Involves only H-bonds
Key Terms
Name the 3 characteristics of denaturation.
Loosening or unfolding of the tertiary and sometimes secondary structure
Sometimes reversible
Involves only H...
The breaking of which reaction is irreversible?
Breaking disulfide cross-links
Define coagulation. What does it result from?
Permanent denaturation, which results when liquid or semiliquid proteins form solid or semisoft clots
Name 3 effects of coagulation a protein.
Changes its physical characteristics
Alters the ability to bind with water
Interferes with biological interac...
Name a denatured protein that can return to its original state?
Beaten egg whites
What kind of protein holds their new shape?
Coagulated proteins, ex: cooked eggs
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| Term | Definition |
|---|---|
Name the 3 characteristics of denaturation. |
|
The breaking of which reaction is irreversible? | Breaking disulfide cross-links |
Define coagulation. What does it result from? | Permanent denaturation, which results when liquid or semiliquid proteins form solid or semisoft clots |
Name 3 effects of coagulation a protein. |
|
Name a denatured protein that can return to its original state? | Beaten egg whites |
What kind of protein holds their new shape? | Coagulated proteins, ex: cooked eggs |
Name the 3 methods to physically denature proteins | 1) Temperature changes |
How do heat and cold affect proteins? | Heat: speeds up denaturation |
What mechanical actions disrupt protein structures? What strengthens gluten? | Disrupt: beating, rolling, kneading | Strengthens gluten: kneading |
How do sound waves/irradiation disrupt protein structures? | Prolonged exposure at high levels is needed |
Name the 2 methods to chemically denature proteins. | 1) Change in pH | 2) Exposure to mineral salts or metals |
Name examples of products in which acids have denatured milk proteins. | Sour cream, buttermilk, yogurt |
What kind of salts can denature proteins? | Sodium and potassium salts |
What are the 4 factors food scientists examine to determine how effective proteins work in a product? |
|
Name the 5 functions of protein in food. | 1) Proteins form gels |
Define a protein gel | Mixture of fluids locked in a tangled mesh of denatured and coagulated protein |
What are the 2 parts of protein gels? | 1) 3D molecular structure | 2) Liquid attracted to the protein |
What do acids do to gelatin? What can develp? | Acids soften gelatin, which may develop syneresis if stored or cooked for too long |
What increases gel stability? | Mineral salts, hard water, more gelatin, slow coolin rates |
What decreases gel stability? | Acids, sugars, food pieces, rapid cooling |
How is protein gel formed from muscle tissue? | When salt is added to destabilize proteins |
How can globular proteins change texture? | Spun into fibers under the right conditions |
Name 2 examples of texturizing. |
|
What kind of protein can act as an emulsifier? | Denatured protein |
How do proteins act as emulsifiers? | Polar side chain attracts water-based liquid and nonpolar side attracts oil |
How can casein act as an emulsifier? | Pressure used in homogenization of milk ENABLES casein to act as an emulsifier |
What makes extraction of oils from seeds more difficult? | Protein's ability to form an emulsion |
Define a foam. | Gas suspended in liquid or semi-solid |
How are foams formed? | By bubbling gas through a mixture, beating or whipping, and depressurization |
Give examples of foams. | Meringue, foam cakes, marshmallows, soufflés, bread |
Give examples of good foaming agents. | Albumin in egg whites and milk |
What is gluten? | Strongly cohesive and elastic protein |
How is gluten formed? | When a high protein flour is combined with moisture and stirred or kneaded |
What does gluten's strength result from? | Disulfide cross-links formed during kneading |
What happens to gluten when baked? | Gluten coagulates when baked |
What damages high protein foods? | High temperature and prolonged cooking |
What happens when high protein foods are damaged? | Protein molecules shrink and squeeze out H2O, resulting in a dry, rubbery, tough product |
Name 6 functions of protein as a nutrient. | 1) Support growth and repair |
How do proteins function as buffers? | Pick up and release acids and bases (side chain) |
How do proteins control bodily functions? | Proteins are apart of hormones that maintain body functions and enzymes (chem reactions) |
How do proteins provide energy? What is a byproduct? How does it affect health? | AA -> Energy (produces ketones and ammonia - strains kidneys) |
Name 2 ways food scientists are developing affordable proteins. | 1) Developed grains (triticale) | 2) Using biotechnology |
What is a health concern of protein? | Allergies |