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Animal Nutrition > Macronutrients Part 3: Protein > Flashcards

Macronutrients Part 3: Protein Flashcards

1
Q

What does dietary protein provide?

A

Energy, essential amino acids, and nitrogen (to make non- essential amino acids)

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2
Q

What are essential amino acids?

A

Essential amino acids are nutritionally required in amounts
the animal cannot synthesize on its own

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3
Q

What physiologic functions is protein important for?

A
  • Enzyme activity/cellular function
  • Barrier/skin function (deficient diet will cause skin to become brittle)
  • Growth and reproduction
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4
Q

How many amino acids are there that are used as building blocks of proteins?

A

There are 20 amino acids that are used as building blocks
for protein or used as free amino acids

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5
Q

What is the structure of an amino acid?

A

Amino acids have an amine group and a carboxyl group
• The side chain determines which amino acid it is

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6
Q

What are the essential amino acids?

A
  • Arginine
  • Histidine
  • Isoleucine
  • Lysine
  • Methionine
  • Phenylalanine
  • Threonine
  • Tryptophan
  • Valine
  • Taurine (cats)
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7
Q

What are the non essential amino acids?

A
  • Alanine
  • Asparagine
  • Aspartate
  • Cysteine
  • Glutamate
  • Glutamine
  • Glycine
  • Hydroxyproline
  • Proline
  • Serine
  • Tyrosine
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8
Q

What are dietary protein sources?

A
  • animal protein (meat, dairy, egg)
  • Plant protein (legume, grain)
  • Microbial protein
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9
Q

What is important to remember about patients protein requirements?

A

Protein requirements differ between species

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10
Q

What is important to remember about protein requirements of cats?

A

• Obligate carnivores such as the cat have
higher protein requirements than many
other species
• Cats cannot regulate deamination of
amino acids- even when protein intake
is low!

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11
Q

If protien requirements are increased, will that also increase essential amino acid requirements?

A

No

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12
Q

What factors would increase protein requirements?

A

• Protein requirements increase in
animals that do much physical activity.

  • Sufficient protein is important to build
    muscle
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13
Q

What is “sports anemia”?

A

Sports anemia is a type of non-
regenerative anemia in athletes where
protein intake is insufficient

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14
Q

What are drivers of palatability in omnivores and carnivores?

A

Protein and amino acids are also drivers for palatability in omnivores and carnivores

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15
Q

What is the specific amino acid that has a strong odor and could drive palatability?

A

Specific amino acids such as methionine have a stronger flavor and odor that can drive palatability

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16
Q

What flabor can cats not taste?

A

Sweet

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17
Q

What are the branch chain amino acids?

A

Valine, leucine and isoleucine

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18
Q

What is important about leucine? What does it do? Where is it found?

A

Leucine is special among the BCAAs because it promotes muscle-protein synthesis
• Leucine is abundant in meat, and no evidence that supplementation beyond the requirement is helpful for muscle hypertrophy

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19
Q

How is crude dietary protien analyzed?

A

Kjeldahl method

• This method provides the weight of nitrogen out the entire amount of matter analyzed

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20
Q

What percent of the weight of amino acids accounts for nitrogen?

A

16%

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21
Q

Where does protein digestion occur?

A

Enzymatic digestion in the stomach and intestines

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22
Q

How is protein broken down? and where are these products absorbed?

A

• Protein is broken down to smaller
peptides, amino acids

• Amino acids are absorbed via
transporter

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23
Q

What occurs to undigested amino acids in the large intestine?

A

• Large intestine: undigested amino acids
are converted by microbes into
ammonia
• which is captured by the liver and
catabolized to urea

24
Q

How are proteins digested in forestomach fermenters?

A

Some nitrogenous compounds passing through the forestomach may be metabolized by microbialvorganisms

• Urea may be metabolized to ammonia and incorporated into bacterial protein

25
Q

What are DIP’s?

A

• This is called Degradable
intake protein (DIP) (usually
highly soluble protein) that is metabolized by microbial organisms.

26
Q

What is UIP?

A

Undegradable intake protein (UIP)
or “rumen bypass protein”

• This protein is usually heat-treated
protein that is not digestible by the microbial enzymes.

Ex: Brewers grains, distillers grains.

27
Q

Where are UIP’s digested then?

A

• Much protein is then digested by abomasal acid and enzymes and the rest by pancreatic enzymes

  • The amino acids are then absorbed in the small intestine as in monogastric species
28
Q

What is the goal when feeding dairy cows?

A

The goal when feeding dairy cows should always be to maximize microbial amino acid production as much as possible and then, supplement with additional amino acids which are expected to escape rumen fermentation.

29
Q

What are NPN’s?

A

Non-protein nitrogen (NPN)
• NPN can be provided in the form of urea as a substitute for protein
($) • This nitrogen is metabolized to ammonia in the rumen and can be
used by bacteria for amino acid synthesis

30
Q

What is the risks of using too much NPN’s

A

Encephalitis/ Neuro signs

Never feed raw whole soybeans and urea together! Soybeans contain an enzyme called urease which breaks down urea into ammonia

31
Q

How is protein digested and absorbed in hindgut fermentors?

A
  • Highly digestible protein is absorbed similarly to omnivores in the small intestines
  • Only limited microbial protein can be absorbed in the large intestines
  • Therefore, hindgut fermenters require dietary protein and essential amino acids in their food (more so than foregut fermenters)
32
Q

How do mammalian neonates cause milk protein to clot in the stomach? What does this clot do?

A
  • Mammalian neonates have rennet, an enzyme complex (pepsin, lipase, rennin) that causes milk protein (casein) to clot in the stomach
  • The process also requires acid and calcium
  • The clot stays in the stomach and gradually dissolves
33
Q

Why are milk replacers often used instead of whole milk, and what is the risk/ downside when doing that?

A
  • Milk replacers are often used instead of whole milk for monetary reasons (cheaper) ($)
    • But… vegetable protein is unlike casein
  • Therefore it does not curd with rennet
  • The excess protein reaches the lower intestines, and can cause diarrhea and overall increased costs on veterinary treatments
34
Q

What occurs with amino acids when no additonal protien is needed?

A

When no additional protein is required, or when some essential amino acids to build protein are missing, amino acids can be deaminized

35
Q

What is released when an amino acid is deaminized?

A

• This releases ammonia

36
Q

What can the carbon skeleton of deaminized amino acids be used to make?

A

• The carbon skeleton can be used to make glucose or acetyl
CoA (fatty acid pathway)

37
Q

What is transamination?

A

Transamination: the transference of an amine group from one amino acid to form another amino acid

38
Q

What can be used as an alternate source of alanine? When does this occur?

A
  • The muscle can be used as a source of alanine that is metabolized to glucose in the liver
  • This occurs during starvation/inadequate energy intake
39
Q

What is biological value? What impacts it?

A
  • Biological value is the ratio between the amount of protein absorbed from the GI tract and the amount of protein that is retained in the body
  • This may be impacted by the relative concentrations of amino acids to form a complete protein
40
Q

What is a protein with a biological value of near 100%?

A

Eggs “ the ideal protein” (High digestibility, High biological value)

41
Q

What factors are taken into consideration when determining the protein quality?

A

Protein quality takes into consideration the biological value and protein digestibility

42
Q

What can cause a protein to have a low biological value?

A

Protein with low biological value may provide amino acids that will be deaminated and form ammonia and then urea

43
Q

What occurs with proteins of low digestibility?

A

Protein with low digestibility (regardless of its biological value) ferment in the large intestines and release ammonia that may be absorbed

• Excess low digestibility protein -> diarrhea, increased ammonia and urea

44
Q

When is high ammonia or urea problematic?

A

Liver disease -> Excess ammonia is not transfered to urea -> Hepatic encephalopathy

Kidney disease-> Excess urea -> Causes vomiting, diarrhea, nauesea, inappetence.

More urea excreted -> Grass burn

45
Q

What is important for management of renal and hepatic diseases?

A

Dietary:

  • Reduced protein • Protein of high biological value and digestibility

• As a result- less protein reaches the large intestines, and less amino acids undergo deamination and less ammonia and urea are formed

Medications:

• Lactulose is often included in therapy of dogs with hepatic disease

46
Q

How is lactulose effective in decreasing issues for dogs with hepatic disease?

A
  • Bacterial degradation in colon reduces colon pH -> retention of ammonia in colon as ammonium
  • migration of ammonia in blood into colon to form ammonium ion
47
Q

What are the examples of protein malnutrition and what symptoms would you see in each?

A

Kwashiorkor: protein malnutrition
• Abdomen appears swollen due to effusion

• Loss of muscle mass

• May be overall sufficient energy intake
Marasmus
• Overall emaciation

• Both protein and energy intake is insufficient

48
Q

What are signs of protien deficiency in pateints?

A

Protein deficiency: hypoalbuminemia -> decreased oncotic pressure ->
ascites/effusion

49
Q

What is Taurine?

A
  • A unique sulfur amino acid
  • It is a free amino acid (not part of a protein)
  • Can be synthesized from other sulfur amino acids: methionine and cysteine
  • Considered essential in cats and human infants
  • Present in high concentrations in the retina and cardiac muscle

• Also conjugated to bile acids

50
Q

What is important to remember about taurine and cats?

A

Cats are very inefficient at converting methionine and cystine to taurine so we still have to supplement it in their diets.

51
Q

What can occur in patients with a taurine deficiency?

A
  • Taurine deficiency can cause heart disease and blindness

• Should not occur in species where it is not an essential amino acid
(other than cats)

52
Q

When may a taurine deficiency be problematic for patients who are not felines?

A
  • Low methionine and cysteine intake
  • Low methionine and cysteine bioavailability/ digestibility/ transformation
  • High taurine loss
53
Q

Where is taurine found in the body? Where are they not found?

A
  • Taurine is present in high amounts in muscle protein and heart tissue
  • It is not present in high amounts in plants commonly used as ingredients in pet food such as legumes and grains
54
Q

What can cause taurine deficiency in dogs?

A
  • Conjugated taurine is recycled with enterohepatic recirculation
  • Shifts in the normal GI microbiota may cause increased taurine loss Taurine
  • Taurine deficiency has been found in dogs, and can occur as a result of diets with low methionine and cysteine
  • Diets with low digestibility
  • Diets with high fiber that change the GI microflora
55
Q

Why can grain free diets lead to taurine deficiencies in dogs?

A
  • Potential for loss of methionine loss or taurine loss thus potential cardiomyopathies.

Animal Nutrition (27 decks)

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