protein 3 Flashcards

1
Q

Proteins in wheat flour are extracted using H2O, NaCl and
ethanol as solvent. What is the mode of action of these
solvents?

A
  • H2O: protein with a polar surface are extracted
  • NaCl: salting in –> at low ionic strength ions increase the
    solvation of charged groups at the protein surface
  • Ethanol: organic solvent –> more apolar solvent, increased
    solubility of hydophobic groups
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2
Q

how do globular proteins occur?

A

as soluable, monomeric or multimeric proteins
combination of alpha&beta- sheet

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3
Q

what are fibrous proteins?

A

muscle protein –> are tipically associated into larges complexes

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4
Q

what are random coil protein

A

these are neither globular or fibrillar
and do not have a fixed secondairy or tertiary structure

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5
Q

what does the solubility of protein influence?

A
  • appearance
  • teture
  • digestibility
  • foam/ emulsion properties
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6
Q

what happens to the solubility if you add salt ions around the pI?

A

normally the proteins wil aggregate; so not solubule

but by adding salt, they neutralize; increased solubility

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7
Q

what are chemical reactions that can happend?

A
  • hydrolysis of peptide bonds
  • formation of lysino-alanyl derivatives
  • formation or reshuffling of S-S bridges
  • deamidation of decarboxylation
  • maillard reaction
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8
Q

what is the sweetening power of aspartame?

A
  • 180 times that of sucrose
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9
Q

peptides are often bitter; what is the rule of thumb:

A
  1. Amino acids in a peptide are more bitter than free amino acids
  2. Non-terminal amino acids are more bitter than terminal amino acids
  3. A peptide is bitter when the average hydrophobicity >1400 Cal/mole
  4. Peptides > 6000 Da are not bitte
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10
Q

what is the advantage and disadvantage of total N content of protein?

A
  • fast
  • also insoluble materials
  • measures all nitrogen, also non protein
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11
Q

that is the advantage and disadvantage of spectrophotometric?

A
  • fast
  • cheap
  • only for soluble protein
  • influenced by other compounds
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12
Q

how does SDS work?

A
  1. Unfolding of protein and dissociate
    complexes
  2. Separation of proteins on a gel under
    influence of an electric field
  3. Separation distance on gel relates with
    molecular weight
  4. Calculate molecular weight by
    comparison with marker (contains
    protein of known Mw)
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13
Q

what is strecker degration ?

A
  • Combination of decarboxylation and deamination
  • Removal of alpha-carboxylic acid and alpha-amino group:
    Results in:
  • Formation of aldehydes (aroma compounds)
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14
Q

In big apolar group is L or D bitter or sweet?

A

L: bitter; D: sweet

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15
Q

in polar/ small apolar group is L or D bitter or sweet?

A

L: sweet natural, D: neutral

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