Foodchem Lecture 11 Pics

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Morgan.liberatore
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Foodchem Lecture 11 Pics
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2012-03-18 22:23:50
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Foodchem Lecture 11 Pics
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Foodchem Lecture 11 Pics
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  1. Beta sheets regions can form when alpha helices fold in upon themselves in order to reduce their molecular free energy state
  2. Globular protein with random, helix and b-sheet forms
    • Additional hydrogen bonding can take place any time a hydrogen and electronegative oxygen/nitrogen are in proximity
    • Can form electrostatic bonds or can be solvated
  3. Additional hydrogen bonding can take place any time a hydrogen and electronegative oxygen or nitrogen are in proximity
  4. Net result of all the different kinds of bonds result in a protein macromolecule will try to find an equilibrium structure dictated by its environment and tends to be structurally locked into a specific conformation by a range of forces
    • Tetramer
    • Four tertiary globular proteins associating
    • Lipoprotein
    • Proteins complexed with lipids, generally triglycerides and phospholipids
    • Abundant in nature and have good emulsifying properties
    • Examples: Egg yolk, and some milk proteins
    • Glycoprotein
    • Proteins complexed with carbohydrate
    • Can range from simple sugars to heterosaccharides to polysaccharides
    • The carbohydrate is generally attached to the OH group of serine or threonine by an O-glycosidic bond or the amide group of asparagine, by an N-glycosidic linkage
    • Examples: Ovomucoid in eggs and soybean glycoproteins
    • Metalloprotein
    • Complex proteins which are complexed with a metal ion which is generally loosely chelated
    • Examples: Fe++ in myoglobin and hemoglobin where Fe++ is chelated by a porphyrin ring structure
    • Numerous enzymes have metal ions as prosthetic groups
    • Unfolding of the protein as it is denatured
    • Tertiary structure unfolds, secondary structure unravels
    • Leaves the peptide bonds more accessible to proteolytic enzymes
    • Denaturation results in reduction in solubility
    • Hydrophobic domains become exposed
    • Exposed hydrophobic domains bind together
    • They aggregate together
    • Precipitate out of solution
    • TD = Temperature of denaturation
    • Shows how with increasing temperature, degree of order is decreased
  5. Shows the effect of pH on protein denaturation
    • Urea
    • Can hydrogen bond competitively with the peptide linkage induced hydrogen bonds and disrupt both tertiary and secondary structure hydrogen bonds
  6. Urea can hydrogen bond competitively with the peptide linkage induced hydrogen bonds and disrupt both tertiary and secondary structure hydrogen bonds
  7. Water hydrogen bonding is integral to, and helps stabilize the structure of proteins, especially around charged groups
    • Detergents have both hydrophilic and hydrophobic groups
    • They are able to bridge the hydrophobic and hydrophilic regions of the protein and result in the opening of the internal structure of a protein
    • Bubble within a foam
    • Air is trapped within a protein/water matrix (bubble)
    • Each bubble has thin membrane (interface) which separates the two
  8. Foam can cause denaturation at the interface between the hydrophobic and hydrophilic groups
  9. The easy way to tenderize meat, by using papain, an enzyme to speed it up
  10. The hard way to tenderize meat, using this tool and physical force

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