9 protein intro Flashcards

(59 cards)

1
Q

what are proteins?

A

macromolecules comprised of amino acids bound by peptide bonds

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2
Q

what’s the term for: providing a specific useful property or function in a food product

A

[protein] functionality

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3
Q

what are some useful properties targeted in protein functionality?

A
  • water binding capacity
  • emulsification capactiy
  • gel forming ability
  • coagulating properties
  • dough forming abilities
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4
Q

soybeans form a curd called

A

tofu

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5
Q

______ activity can be both beneficial and detrimental

A

enzymatic

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6
Q

name some examples of enzyme

A
  • protease - meat tenderizer
  • lipase - flavor developer
  • amylase - syrup/sugar manufacturing
  • glucose oxidase - remove headspace of packaging
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7
Q

what’s MSG?

A

monosodium glutamate - a flavor potentiator.

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8
Q

what are some currently uncommon sources of protein in our culture?

A
  • rapeseed
  • beans
  • peas
  • leaves
  • microorganisms
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9
Q

pros and cons of using plant proteins?

A

pros: more abundant, cheaper
cons: lesser protein quality

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10
Q

what is surimi?

A

imitation crab/scallop meat made from pollock

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11
Q

what are the components of an amino acid?

A

amine (NH2), carboxylic acid (COOH), and side chain (R) groups attached to an alpha carbon

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12
Q

at a low pH, an amino acid is

A

protonated (COOH/NH3+)

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13
Q

at neutral pH, an amino acid is

A

zwitterion (COO-/NH3+); net neutral charge

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14
Q

at a high pH, an amino acid is

A

unprotonated; net negative (COO-/NH2)

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15
Q

what does the pKa tell you?

A

when a H will pop on or off

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16
Q

a substance that can act as both an acid and a base is considered:

A

amphoteric

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17
Q

1) a protein in its neutral form have the attributes of a:

2) some of these attributes include

A

1) salt

2) crystalline structure, water soluble, decomposition at high temps

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18
Q

what is the only amino acid that is achiral?

A

glycine (R=H)

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19
Q

what are optical isomers?

A

mirror images of a compound that can’t be superimposed

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20
Q

asymmetry give a molecule the ability to rotate _____ ______ ______ in opposite directions

A

plane polarized light

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21
Q

what compound is used as a reference for determining configuration?

A

glyceraldehyde

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22
Q

it glyceraldehyde has its OH group on the right, what form does it have? what about left?

A

D or dextro; L or levo

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23
Q

what group do we look at when determining an amino acid’s form?

A

NH3 (amine) group; if it’s on the left it’s L, if it’s on the right it’s D

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24
Q

naturally, our amino acids come in what form?

25
what are the 7 categories of amino acids?
1) aliphatic side chain 2) hydroxy side chain 3) carboxylic side chain 4) basic side chain 5) aromatic side chain 6) sulfur-containing 7) imino acids
26
what are the aliphatic amino acids?
glycine, alanine, valine, isoleucine, leucine
27
what are some attributes of the aliphatic amino acids?
- relatively unreactive | - as chain length increases so does hydrophobicity
28
is glycine hydrophobic?
hell naw
29
what are the hydroxy side chain amino acids?
Serine (Ser), Threonine (Thr), Tyrosine (Tyr)
30
what are some attributes of the hydroxy side chain amino acids?
- OH can form ester linkage with a phosphate group - OH enables hydrogen bonding - OH is a very reactive moiety
31
true or false: casein is heat stable
true
32
O-glycosidic linkages are associated with what functional group?
OH
33
what are the carboxylic amino acids?
aspartic acid, glutamic acid and their amides, asparagine and glutamine
34
what are some attributes of the carboxyl amino acids?
- COOH is a very reactive group - at pH 7 they are negatively charged (polar) - tend to have LOW isoelectric points - play a role in non-enzymatic browning reactions - water soluble
35
what serves as an attacking point for reducing sugars?
amide group
36
N-glycosidic linkages are associated with what functional group?
amide
37
what are the basic side chain amino acids?
lysine, histidine, arginine
38
what are some attributes of amino acids with basic side chains?
- high isoelectric points
39
how many amide groups does lysine have?
2
40
arginine has a _____ group
guanadino
41
histidine has a _____ group
imidazole group
42
when a protein reaches its isoelectric point, this is its point of (highest/lowest) solubility in water
lowest
43
what are the aromatic amino acids?
phenylalanine, tyrosine, tryptophan
44
what are some attributes of the aromatic amino acids?
- can absorb UV light | - quite hydrophobic
45
what are the sulfur containing amino acids?
cysteine, cystine (cysteine's dimer), and methionine
46
a _____ _____ holds together two cysteine residues
disulfide crosslink
47
1) cystein has a: | 2) this group is (acidic/basic)
1) sulfhydryl group (SH) | 2) basic
48
what are the imino acids?
proline, hydroxyproline
49
what makes imino acids different?
they lack an NH2 group. they have NH instead
50
what are some attributes of imino acids?
- interrupt natural tendency to form alpha helix - found in collagen - can't form intramolecular hydrogen bonds
51
what are the essential amino acids?
HPVL2IT2 - histidine - phenylalanine - valine - leucine - lysine - isoleucine - threonine - tryptophan
52
what are the conditionally essential amino acids?
A2G2PST - arginine - asparagine - glutamine - glycine - proline - serine - tyrosine
53
what are the nonessential amino acids?
- Alanine - Asparate - Glutamate - Cysteine (we don't need cancer)
54
what are used extensively as flavoring agents to provide a meaty/brothy flavor?
hydrolysates
55
what is an example of a hydrolysate that's made from fermented soybeans
soy sauce
56
what do sulfur containing amino acids release to provide flavor due to their breakdown while being cooked?
H2S - hydrogen sulfide
57
what is responsible for flavors?
- peptides
58
the process of decay or rotting in a body or other organic matter is known as
putrefaction
59
what causes odors and off flavors association with putrefaction?
- enzymatic deamination | - decarboxylation of free amino acids by microbial enzymes