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Food Chemistry > amino acids > Flashcards

amino acids Flashcards

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1
Q

what are the 7 categories for the common amino acids

A

aliphalitic, hydroxylic, carboxylic, basic side chains, aromatic side chains, sulfur containing amino acids and imino

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2
Q

what are the 5 aliphatic amino acids

A

glycine, alanine, valine, leucine, isoleucine

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3
Q

what are the 3 hydroxyl amino acids

A

serine, threonine, tyrosine

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4
Q

what ability does the hydroxyl amino acid has

A

to form an ester linakge

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5
Q

what are the 2 carboxylic amino acids

A

aspartic acid and glutamic acid

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6
Q

complete this sentence

proteins that contain significant amounts of aspartic and glutamic acid tend to have… isolectric points

A

low

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7
Q

what are the 3 basic amino acids

A

lysine, histidine and aginine

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8
Q

lysine undergoes rapid reaction with reducing sugars which reduces what

A

the availability of this essential amino acids

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9
Q

arginine has a what group

A

guanidino

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10
Q

what is the R group for hstine

A

imidazole

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11
Q

what are the 3 aromatic amino acids

A

phenylalanine, tyrosine, tryptophan

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12
Q

what are the 3 amino acids of sulfur containing

A

cysteine, systine and methionine

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13
Q

what are the 2 types of imino acids

A

proline and hydroxyproline

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14
Q

proline and hydroxyproline are found where

A

collagen

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15
Q

free aminos acids and peptides gives flavor to foods what is the most common F.A.A

A

monosodium glutamate

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16
Q

what is used as flavorin agnets for meat or brothy flavour to soups

A

protein hydrolysate

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17
Q

the smell of a rotten eggs comes from what

A

hydrogen sulfide

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18
Q

what is putrefaction

A

a.a precursors of putrefactive odors and flavors in emat and fish

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19
Q

what happens to he free fatty acid to have bad odors and flavors

A

deamination or decarboxylation

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20
Q

what are the 2 amino acids that does not help to make helix formation?

A

proline and hydroxyproline

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21
Q

what are the 2 sub forms of beta sheet

A

parallel and antiparallel

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22
Q

suprahelix is found where

A

collagen

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23
Q

how do you form a suprahelix

A

3 supahelix

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24
Q

what is the classification of single proteins

A

albumins, globulins, glutelins, prolamines, scleroproteins, histones

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25
Q

what is albumins

A

protein that are soluble in neutral distilled water

26
Q

what is globulins

A

protein that are soluble in neutral, dilute salt solutions, but not in distilled water

27
Q

what is glutelins

A

are proteins that are solule in dilute acid or base, but not in neutral solution

28
Q

what is prolamines

A

proteins that are soluble 50-90% ethanol and insoluble in water

29
Q

what is scleroproteins

A

insoluble in water and neutral salts - resistant to enzymatic hydrolysis (generally structural proteins )

30
Q

what is histones

A

basic proteins

31
Q

what are the protein that food science has more interest

A

albumins and globulins

32
Q

what is lipoproteins

A

proteins complexed with lipids (normally triglycerides). Abundant in nature and good emulsifiers

33
Q

what is glycoproteins

A

proteins complexed with carbohydrate, which can range from simple sugars to heterosaccharide to polysaccharides. The carbohydrate is gnerally attached to the OH group of serine or theonine by an O-glycosidic bond. The carbohydrate is generally attached to the amide group of asparagine by an N-glycosidic linkage

34
Q

what is metalloproteins

A

proteins complexed with a metal ion, which is generally loosely chelated

35
Q

what is phophoproteins

A

proteins conjugate to ionarganic phosphates

36
Q

this is the definition of what?

change in structure or conformation of a protein that does not involve breaking of peptide bonds

A

denaturation

37
Q

continue the sentence

when the conformation of a protein is changed, many of its …. properties are also changed

A

physical

38
Q

what are the common changes observed when denaturation takes place

A
  1. unfolding of the tertiary structure of the secondary structure makes the peptide bonds more accessible to proteolytic enzymes
  2. denaturation of protein generally results in a reduction in its solubility
  3. enzymatic activity may be decreased or lost
  4. viscosity generally increases, gelation may occur
  5. crystallization is no longer possible
39
Q

what is the difference in agregation and gelation

A

agregation protein comes together; gelation fols to get a 3 dimension structures and water makes a creamy substance

40
Q

factors contributing to denaturation

A

the most COMMON factor is HEAT.

others : ph, ionic strength, chemical agents, surface forces, combinations of the above

41
Q

what the effect of pH can do

A

it affecs the overall charge of the molecule which affects the electrostatic bond contributions to the tertiary structure

42
Q

what happens with hydrogens bond breakers and give an example

A

compounds that can effectively compete with the peptide linkage for H bonds can readil disrupt both tertiary and secondary structure. EX: urea

43
Q

what can also disrupt H bonds

A

alcohols and acetone

44
Q

how can detergents contribute to denaturation

A

theyr are able to bridge the hydrophobic and hydrophilic regions of the protein and result in the opening of the structure of the protein

45
Q

how organic solvent denature proteins

A

they turn the env hydrophobic - can turn the protein macromolecule inside out

46
Q

how surface forces denature proteins

A

thy reduce surface tension resulting in the formation of a foam .

Protein molecules actively rearrange themselves structurally to reduce their free energy with hydrophobic groups facing air and hydrophilic groups facing into the water - this arrangement can cause denaturation

47
Q

what are some of the reactions that proteins do

A
  1. non enzymatic browning
  2. cross linking reactios
  3. formation of lysinoalanine
48
Q

explain non enzymatic browning

A

foods that have a lot of proteins undergo browning when they are heated under low moisture conditions (MAILARD REACTION)

49
Q

Maillard reaction involves what

A

an aldehyde group of a reducing sugar and a free amino group of an amino acid or the free amino group on a peptide or protein, such as lysine

50
Q

explain cross linking reactions

A

reducing sugars are mainly absent, the crosslinking of proteins can occur at higher temepratires by the formations of amide bonds between COOH and NH2 groups on side chains of amino acid reidues

51
Q

explain the formation of lysinoalanine

A

the preparation of protein concentrates and isolates often calls for the treatment of proteins with alkali in hte presence oh heat to modify the properties

52
Q

what are the degrative reactions of proteins and explain

A

proteolysis - results in a reductuon in molecular weight and loss of functionality

putrefaction- associated with microbial spoilage. It involves degradation of free amino acids produced by proteolytic enzymes secreated by spoilage microorganisms

53
Q

what are deaminases and decarboxylase and what they do

A

they are enzymes that remove amine groups and carboxyl groups

54
Q

what amino acid makes fish smell bad

A

trimethylamine (TMA)

55
Q

water binding in protein is associated with what

A

ionic species present (NH3 and COO) and hydrogen bonding sites (C=O, N-H)

56
Q

what is moisture sorpton isotherm

A

3 levels water binding that can be associated with most proteins

57
Q

continue the phrase

a protein’s ability to bind water is a function of its… compososition, overall structure and charge

A

amino acid

58
Q

processing operations that involve removal of water can affect proteins what does it does?

A

freenzing and drying

59
Q

what can freezing do to the proteins

A

changes in the structure. There is a loss of water binding capacity- loss of desirable texture

60
Q

what does drying do to proteins

A

denaturing and or browning

61
Q

what is drum drying

A

extensive denaturation and extensive browning if sugars are present

Food Chemistry (11 decks)

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