U6 Flashcards

(84 cards)

1
Q

proteins as structural components

A

skin, bones, tendons, muscles

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2
Q

catalytic agents

A

enzymes

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3
Q

regulating agents

A

hormones

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4
Q

immune agents

A

antigens and antibodeis

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5
Q

carriers

A

myoglobin and hemoglobin - O2 and CO2

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6
Q

nutritional role of proteins

A

provide AA and N

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7
Q

functions of protiens in food

A
water binding - texture 
emulsifiers 
gel forming
coagulating 
dough forming
palatability
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8
Q

what is palatablity

A

taste, texture, food quality

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9
Q

what protein in bread makes it palatable

A

gluten

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10
Q

what forms when milk coagulates. what products does this make

A

a curd. cheese, yogurt, sour cream

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11
Q

what forms when soy proteins coagulates. what product does this make

A

curd. tofu

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12
Q

what product is protein emulsification important for

A

sausages

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13
Q

endogenous enzymes

A

detrimental catalytic behavior in proteins - autolytic

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14
Q

exogenous enzymes

A

supplied by microbes in food

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15
Q

examples of beneficial catalytic behavior

A

proteases - tenderize meat
lipases - flavor development
amylases - form corn syrup.sugar products

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16
Q

example of a flavor potentiator

A

MSG - monosodium glutamate

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17
Q

examples of protein sources other than milk, eggs, and meat

A

rapeseed, beans, peas, leaves, microbes

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18
Q

what methods make meat analogs from soybean protein

A

texturization using extrusion

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19
Q

how many amino acids

A

20

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20
Q

what is the alpha carbon

A

connected to both NH2 and COOH groups

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21
Q

when is the AA protonated

A

low pH

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22
Q

when is the AA deprotonated

A

high pH

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23
Q

what is a zwitterion

A

COO- and NH3+. net charge zero

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24
Q

when does the zwitterion occur

A

isoelectric point

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25
formula for isoelectric point
pI = (pk1 + pk2)/2
26
amino acids have attributes of a ... (since the neutral form is still charged
salt
27
what properties do AA have that are similar to a salt
1. crystalline strucutre 2. wate soluble 3. decompose at high temperatuers 4. amphoteric - acid and bases
28
what occurs due to AA having 4 different substituents
optical isomerism and ability to rotate plant-polarized light. not superimposable
29
D or L?
both occur - racemic mixtures. but only L can form proteins
30
what is on the right for D and on the left for L
hyrgogen of alpha carbon
31
7 categories of amino acids
1. aliphatic 2. hydroxyl 3. carboxyl 4. base 5. aromatic 6. sulfur-containing 7. imino
32
5 types of aliphatic AAs
glycine, alanine, valine, leucine, isoleucine
33
defining feature of aliphatic AA
hydrophobic
34
3 types of hydroxyl AA
serine, threonine, tryosine
35
defining feature of hydroxyl AA
presence of OH group
36
bonds that hydroxyl AAs make
h bonds diester links o-glycosidic links
37
2 types of carboxyl AA
aspartic acid and glutamic acid
38
defining feature of carboxyl AA
acidic. negative at pH7 | isoelectric point is
39
bond that carboxyl AA can make
N-glycosidic link
40
what form do carboxyl AAs show in their natural form
amide - NH2. aspargie and glutamine
41
3 types of basic AA
histidine, lysine, arginine
42
defining feature of basic AA
basic - positive at pH7. isoelectric point is >ph7
43
what R group does histdine have
imidazole
44
what reaction does lysine do
maillard
45
what R group does arginine have
guanidine
46
3 types of aromatic AA
phenylalanine tyrosine tryptophan
47
which amino acid is in 2 groups
tyrosine
48
defining feature of aromatic AA
presence of aromatic group - absorbs UV light
49
what bonds can aromatic AA form
hydrophobic interactions
50
3 sulfur contianing AA
cysteine and methionine. cystine - which is the cysteine dimer
51
defining feature of sulfur AA
presence of a sulfur compound
52
what bonds can sulfur AA undego
disulfide crosslinks
53
what is a disulfide crosslink
RSSR - dimer of cysteine molecules, cystine, between peptides or within a peptide
54
2 types of imino aicds
proline and hydroxyproline
55
are iminoacids amino acids?
no - NH instead of NH2
56
what structure does proline interfere with and why
alpha helix because its incapable of forming hydrogen bonds
57
what increases as aliphatic AA chain lengthens
hydrophobicity
58
what is a diester link
one phosphate group linked to 2 hydroxyl AA via ester linkages
59
which is more acidic - aspartic or glutamic acid
aspartic
60
what does MSG stand for
monosodium glutamate
61
what reaction do carboxylic AA undergo
non-enzymatic browning - serve as reduction points for reducing sugars
62
what is more polar - amide or acid form of carboxyl AA
amide. makes it more watersoluble
63
is the sulfhydryl group acidic or basic
basic
64
what type of proteins contain iminoAA
structural
65
true or false - pH has no effect on charges of the side chains
false. high ph - convert NH3 to NH2. supress + charge low pH - convert COO to COOH. supress -
66
when is a protein least soluble
when it's neutral at its isoelectric point
67
how many essential AA
9
68
what causes flavor from proteins
free AA and peptides
69
what do protein hydrolases do in food
make meaty/broth flavor
70
how do sulfur containing AA contribute to flavor
breaking down when heated releases H2S
71
what is responsible for bitter flavors
peptides
72
what is putrefaction
decay of proteins by enzymatic denaturation or decarboxylation by microbes. causes bad flavors and odors
73
True or false: cysteine is a peptide because it is formed of 2 AA
false
74
True or false: the isoelectric point of proteins is controlled by COOH and NH2 groups attached to the alpha carbon
false
75
A longer aliphatic chain in an AA will increase its…
hydrophobicity
76
Amino acids are optically active compounds because they have … alpha carbon atom
asymetric, chiral
77
The amphoteric properties of proteins help regulate the … of the human body
ph
78
The first carbon atom that attaches to a functional group is called…
alpha carbon
79
Coagulating milk casein is the main mechanism to produce
cheese
80
True or false: proline is considered an alpha amino acid
false
81
When the AA has its alpha amine group to the left, it rotates light
counterclockwise
82
AA can act as acids or bases, hence they are…
amphoteric
83
Disulfide crosslinks result from the presence of … in amino acids
sulfhydryl (methionine doesn't form them)
84
The ability of AA to rotate plane-polarized light is…
optical isomerism