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Animal Nutrition AnSc 315 > Proteins > Flashcards

Proteins Flashcards

1
Q

what is protein

A
  • organic compound in food or feed that contains N
  • meat, fish, eggs and some plants
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2
Q

what do animals require

A
  • they require amino acids not proteins
  • proteins are made up of the essential amino acids
  • if all the amino acids required for the synthesis of animal proteins are not present at the time of protin synthesis, no proteins are made
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3
Q

what is the importance of amino acids

A

40% of body protein in skeletal muscle = important for structure or locomotion

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4
Q

what are the major functions of amino acids

A
  • catalysts
  • messengers
  • structural elements
  • immunoprotectors
  • transporters
  • buffers
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5
Q

what are some major catalyst enzymes

A
  • hydrolases - cleaves compounds
  • isomerases - transfer atoms in a molecule
  • ligases (synthases) - join compounds
  • oxidoreductases - transfer electrons
  • transferases - moves functional groups
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6
Q

whar do enzymes do

A

speed up the rate od reaction

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7
Q

what are messengers

A
  • hormones
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8
Q

what are structural elements

A
  • contractile proteins = skeletal muscel (actin/myosin)
  • fibrous proteins - keretin, skin, hair, nail strength
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9
Q

what are immunoprotectors

A
  • immunoproteins (antibiodies)
  • identifying antigens and protect body
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10
Q

how do proteins act as buffers

A
  • amino acids in proteins accept hydrogens when the pH is low
  • hydrogen gets bind to amino group and goes from N2 -N3 and pH rises
  • amino acids in proteins donate hydrogens when the pH is too high (H ions are released and pH goes down)
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11
Q

what do amino acids influence

A
  • influence farm animal productivity (growth, production of milk and eggs)
  • animal health and fertility ( immunoproteins = animals that are protein defficient will be immuno deficient and more succeptible to disease, ammonia toxicity
  • infertility in dairy cows= over feed protein, excesssive ammonia is produced and abosorbed, creating toxic environment
  • feeding cost and animal production
  • environmental consequences = excretion of nitrogen into the environment (ammonia)
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12
Q

what is a basic structure of an amino acid

A

carboxlic
ride chain ( what makes amino acids Different from one another)
amino group (with accepted H atom)
central carbon

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13
Q

what is an essential amino acid

A
  • body cannot synthesis in adequTE AMOUNTS, so it must be added to the diet
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14
Q

non essential amino acid

A
  • building blocks are present in the body, can be made and doesnt need to be added in the diet
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15
Q

what type of amino acid isomers will be recognized by enzymes

A

L over D
- some D-AA can be converted to L AA (commercial DL - methionine produced by industrial process)

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16
Q

what D AA cannot be converted

A
  • D - lysine
  • lysine produced by fermentation so that only the L isomer is produced
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17
Q

what is peptide bonds

A
  • AA link together to form peptides
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18
Q

what are polypeptides

A

less then or equal to 20

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19
Q

what are proteins

A

equal to or greater then 20

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20
Q

what is a primary structure

A
  • AA sequence
  • polypeptide backbones do not differ
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21
Q

what is a secondary structure

A
  • folding of polypeptide chains into coiled or pleated structures
  • determined by what AAs are involed in making protein
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22
Q

what is a tertiary structure

A
  • 3- dimensional structure of the protein (electrostadic connections)
  • strong covalent bonding between cysteine residues - disulfide bridges
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23
Q

what is a quaternary structure

A
  • assembly of 2 or more different proteins by forces other than covalent bonds
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24
Q

what determines protein structure

A
  • order of amino acids
  • RNA creates genetic cross over that determines protein
  • important factor in determining protein nutritional value
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25
Q

what does an a helix do for secondary structure

A
  • straight chains of A.A determine the protein content
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26
Q

what do B sheets do

A
  • major impact on digestibility
  • the more beta sheets there are the more extensive attractions/ bonds limit the acess of enzymes as they are much more folded = making them less digestible
  • most sheets are low b sheets except feather meal - feather meal needs to be hydrolysed first for better digestion
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27
Q

what are teriary and quaternary strutures more involved with

A
  • more involved with protein functionality than animal nutrition
  • keratin and collagen = elastic structure
  • hemoglobin = blood oxygen transport
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28
Q

what are exogenous sources of proteins

A
  • plant - derived ingredients = soybean, soybean meal, peas, canola meal* and cereal grains
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29
Q

what are endogenous proteins

A
  • desquamated mucosal cells
  • digestive enzymes, glycoproteins, mucins
  • microbes = hind gut, most will be lost in the feces
30
Q

what are the three objectives in protein digestion

A
  • digest dietary protein
  • absorb constituent AA
  • reclaim digestive enzymes
31
Q

overview of protein digestion

A
  • no digestion in the mouth
  • starts in the stomach
  • absorbed mostly in the SI - duodenum and jejunum
32
Q

what

A
33
Q

breaks protein down in the stomach

A

acid (HCL) and pepsin when it gets activated
- the inactive form of pepsin is pepsinogen
- muscular contractions (peristalsis ) also assist with mechanical break down

34
Q

what happens to the proteins in the stomach

A
  • the proteins need to be denatured to increase the surface area
  • HCL does that
  • proteins unfold
    the stomach pH is 1-2
35
Q

how is protein digested in the small intestine

A
  • acidic chyme enters the small intestine - stimulating enterocytes
  • release of pancreatic juice - secretin and CCK
  • pro-enzymes, bicarbonate, water and electrolytes are released
    pancreatic enzymes are released - trypsinogen(trypsin) chymotrypsinogen (chymotrypsin) procarboxypeptidases A and B (carboxypeptidases A B) proelastase, collagenase
36
Q

what is the difference between endopeptidases and exopeptidases

A

endopeptidases - digestive polypeptide from the middle
exopeptidases - digestive polypeetide from the ends

37
Q

how are AA and peptides absorbed

A
  • across intestinal brush border memebrane
  • AA absorbtion ( through passive diffusion, transporter-dependent absorbtion)
  • peptide transport ( >60% of AA absorbed by peptides
    Pept 1
    H dependent
38
Q

how do endogenous protein losses occur

A
  • mostly enzyme secretion (20-70%) of protein from the diet
  • if lost in excess, negative N balance even through dietart protein is adequate
  • protease reclamation to reabsorb AA
39
Q

what is a trypsin inhibitor

A
  • changes the shape of trypsin
  • protein inhibitor present in many plant products
  • causes a significant decrease of protein digestion in monogastrics
  • heat labile
40
Q

what is a Tannins

A
  • phenolic compounds that bind, precipitate protein, reduce digestibility
  • they are heat labile - destroyed by heat
  • reduce solubility and reduce digestion in the small intestine
41
Q

what is a maillard reaction

A
  • free sugars, lysine react in presence of heat, moisture = makes protein less soluable, reduces digestibility
    lysine becomes unavailable
  • heat decreases protein soluability
42
Q

what are the most used amino acids in the small intestine

A
  • glutamine, glutamate and aspartate
43
Q

how are amino acids absorbed into the extra intestinal tissues

A
  • amino acids enter portal vein to liver
  • used by liver ( 50% AA released from portal vein) can be used by other tissues
44
Q

what is the post absorbtion of AA

A
  • plasma AA rise after the meal
  • AA pool available for metabolism
  • more non essential amino acid in pool
45
Q

what happens during protein takeoever

A
  • continous process of synthesis, degradation (liver, skeletal muscles)
  • ks = protein synthesis kd = protein degration
  • is ks> kd then protein accretion occurs
  • rapidly growing broilers
    if kd >ks animals will loose weight
46
Q

why does catabolism of amino acids occur

A
  • normal part of tissue turnover - 20-25% of AA from tissue proteolysis
  • disposal of excess(has to be degraded) AA from dietary protein - AA imbalance
  • starvation or inadequate CHO, energy intake ( limited CHO - increases AA but lipids are going to be targeted first)
  • catabolism states
47
Q

what is a transamination reaction

A
  • amino acids are synthesized
  • disposal of access amino acid by taking amonia and turning it into a amino group
48
Q

what is oxidative deamination

A
  • always have the release of free ammonia (always takes place in the liver)
  • complete release of amino group as amonia
49
Q

what is ammonia toxicity in famr animals

A
  • extremely toxic to CNS
  • ruminants - excessive absorbtion of ammonia from rumen
  • non ruminants - excessive protein intake, low arginine diets in monogastrics
    -genetic defects in urea cycle
50
Q

what is the urea cycle

A
  • NH3 combines with CO2 or HCO3 to form carbamoyl phosphate
  • reacts with ornithine to form citrulline
  • aspartate reacts with citrulline to form argininosuccinate
  • is cleaved to form fumarate and arginine
  • urea is formed and ornithine is reformed from cleavage of arginine
51
Q

what is the fate of urea

A
  • urinary excretion - major form of N secretion
  • secretion into the GIT - urea recycling in ruminants
  • milk secretion (milk urea- nitrogen)
52
Q

what are the 4 ways the carbon skeleton is used

A
  • the C skeleton from any AA can be used to generate energy for the Kreb Cycle
  • for some AA their carbon skeleton can exclusively be used for glucose synthesis through glucogenesis
  • any AA whos carbon skeleton end up as Acetly CoA are ketogenic products of a ketone body and fatty acids
  • Fourth group of AA that are both glucogenic and ketogenic. their pathways are dependent on animal requirement
53
Q

what is a heat increment

A

energy lost through evaporation

54
Q

what type of diet is poor in finishing animals

A

high protein
- want high carbs or high lipids

55
Q

what are amino acid and protein requirements

A
  • common nutrient deficiency ( inadequate protein/AA, energy intake = forces body to catabolize AA) imbalanced AA profile - AA deficiency
  • reduces performance = poor growth, poor feed efficiency, negative N balance, low birth weight, low milk production, low egg production
56
Q

what happens to humans with a protein deficiency

A

energy is adequate
- serum protein is severly decreased (swollen abdomne is present because of the low protein osmotic pressure pulls water out of blood into the tissue
- often occurs in children after weaning in famine areas

57
Q

what is marasmus

A
  • protein and energy malnutrition
  • more severe then kwashiorkor
  • tissue protein loss is serum protein, liver, then muscle = extremely low body weight
58
Q

what are amino acid requirements of monogastrics

A
  • adequate AA intake for protein accretion, milk production and growing fetus
  • maximize lean meat deposition
  • protein synthesis is an “all or nothing” event = need correct amounts of proportions to take place
  • specicies, genotype, age, level of production, environmental factors
  • genetics determine animals capacity for lean meat deposition
  • nutrition determines if the genetic capacity is reached
  • different genetics have different requirements for AA
59
Q

what are the two major facotrs that effect protein quality

A
  • AA content of protein relative to the requirement of an animal (primary protein structure)
  • digestibility of the protein
60
Q

what are the concepts of the first limiting amino acid

A
  • AA supplied in dietary protein in the lowest amount relative to animal requirement
  • feed amino acid composition
  • animal requirements
  • limiting AA determines level of production
61
Q

what is the barrel analogy

A
  • only fill the barrel to the minimum requirement of wine without it spilling
62
Q

what do pigs require for AA

A
  • lysine
63
Q

why does poultry require methionine

A
  • poultry feathers are hight in methionine = they require a larger requirement
64
Q

what are problems with first limiting AA

A
  • takes account of deficiencies but no excesses (excess protein costs energy to metabolize)
  • supplimenting first limiting AA may not give optimal growth ( second third are also important)
65
Q

what is the ideal protein concept

A
  • perfect balance of EAA that will meet the requirements for maintenance, production
  • lysine is always set at 100% (other EAA expressed as a % of lysine)
  • allows for the calculation of the requirement of all AA if lysine requirement is kown
66
Q

advantages of using ideal protein concept

A
  • balanced EAA composition can be fed
  • maximum protein accretion and synthesis is supported (maximize growth, reduce days on feed, faster turnover)
  • avoid under feeding of AA (maximize growth)
  • avoid over feeding of AA (lower cost and less nitrogen excretion)
  • can reduce dietary CP requirement
  • only need to know the requirement for lysine (everything else you can calculate)
  • reduce feed costs, increase profitability
67
Q

why is lysine set to 100 in ideal protein

A
  • usually limiting EAA in cereal - based diets
  • no metabolic function other then as a component of protein (lysine requirements can be easily determined (exclusively used for protein synthesis)
  • lysine is easy to analyze
  • lysine contents of most feeds are well known
68
Q

what are ideal protein ratios

A
  • changes because EAA requirements change
  • species, genotype, age, production level, environmental factors
  • as pigs grow, EAA req for maintenance, protein deposit changes
69
Q

amino acid requirements

A

in a growing pig - maintenance requirement is less then production requirement
- EAA requirement mainly determined by the requirement for production (lean deposition)

70
Q

what is total AA vs digestible AA

A
  • % of AA abosorbed in gut differs amount feed ingredients
  • diet formulation based on total levels of dietary AA are inaccurate
  • practical, usually AA composition of feed ingredients available
71
Q

how do you determine lysine requirement

A
  • provide a basal diet that is adequate for all nutrients other then lysine (basal diet deficienct in lysine)
  • add lys-HCl to the basal diet to give different levels of lysine

Animal Nutrition AnSc 315 (9 decks)

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