Exam 2 Material Flashcards
hemicellulose
Glycan
Forms hydrogen bonds with cellulose microfibrils to form a matrix/network
Long linear backbone composed of 1 type of sugar (glucose, xylose, mannose) but short side chains are heterogeneous
lignin
Not a carbohydrate
Present in the cell wall, content increases with age of plant
Typically not digestible
Neutral Detergent Fiber (NDF)
After plant samples are washed in a neutral detergent solution, NDF is what remains (Van Soest Method)
Represents the structural cell wall components of the plant (lignin, cellulose, hemicellulose)
Acid Detergent Fiber (ADF)
After samples are washed in an acid detergent solution, ADF is what remains (Van Soest Method)
Represents the least digestible plant cell wall components, including cellulose and lignin
Therefore NDF-ADF=hemicellulose
what is fiber
The portion of the diet that cannot be digested by the ANIMAL (excludes microbes):
- Cellulose
- Hemicellulose
- Lignin
- Etc…
- -Note that much of it is cell wall components
breakdown of carbohydrates by microbes
Microbes can break down alpha- AND beta- linked carbohydrates
They prefer alpha-linked because they are easy to break down, but can break down beta-linked carbohydrates present (which are plentiful in high NDF/ADF diets)
The process of carbohydrate breakdown is called FERMENTATION
what is fermentation
Conversion of carbohydrates to alcohols and carbon dioxide or organic acids using yeasts, bacteria, or a combination thereof, under anaerobic conditions
fermentation by microbes
volatile fatty acids are produced from microbial fermentation of carbohydrates
most important VFA are
Acetic Acid (or acetate) CH3COOH Propionic Acid (or propionate) CH3CH2COOH Butyric Acid (or butyrate) CH3CH2CH2COOH
ruminal production of VFA
Total rate of production and concentration of VFA are directly related to intake of fermentable organic matter
Profile of VFA produced is dependent on feed profile
ruminal absorption of VFA
Taken up by rumen epithelium and transported by passive diffusion
Rate of absorption determined by:
Concentration in rumen fluid (most important)
Rumen fluid pH
VFA chain length
fate of VFAs after they are absorbed into the bloodstream
Propionic acid: converted to GLUCOSE
Butyric acid: converted to beta-hydroxybutyric acid (BHBA) for fatty acid synthesis
Acetic acid: converted to Acetyl CoA for fatty acid synthesis
other sites of microbial fermentation of carbohydrates
We have just learned how microbes ferment carbohydrates to produce VFAs in the rumen, but where else do microbes have this same activity? The colon (especially the cecum) Other non-rumen pregastric chambers (like in the hamster, vole, kangaroo, hippopotamus, hoatzin, etc)
carbohydrate digestion in the large intestine
Microbes live in the large intestine of every animal
These microbes act just like those in the rumen and break down alpha AND beta-linked carbohydrates to VFAs
VFAs are absorbed across the wall of the large intestine
Remember that absorption of nutrients from the large intestine is very inefficient in some animals so is more important for some animals (cecal fermenters) than others
digestion and absorption of alpha-linked carbohydrates by the animal
So we are talking about digestion of which carbohydrates?
- ALL animals have the capacity to digest alpha linked carbohydrates, but some animals rely on it more than others
- Many enzymes secreted by the animal that contribute to hydrolysis
- -Digest starch and glycogen (both alpha linked “storage” polysaccharides)
- -Any alpha linked di-, tri-, oligo- saccharides
what is the dominant VFA produced from cellulose fermentation
acetate
proprionate
butyrate
methane
Acetate
important of carbohydrates to animals
The ultimate source of energy for most animal cells: GLUCOSE
Major source of energy in the diet
Is a higher proportion relative to other sources in herbivore diet than carnivore diet
importance of glucose as a nutrient
Blood glucose: most important vehicle for post-absorptive carbohydrate metabolism
Sources of blood glucose vary with species, time after feeding
non-diet sources of glucose that the animal can use
The diet provides an important source of glucose; however, there are other sources of glucose available to animals via:
- Glycogen breakdown (Glycogenolysis) in the liver
- Glucose synthesis (Gluconeogenesis) in the liver and kidneys
gluconeogenesis
synthesis of glucose from non-hexose precursors
Features:
-Occurs mainly in liver, also in kidneys
-Nonruminants: rate varies inversely with rate of glucose absorption, precursors are of endogenous origin
-Continuous in ruminants…what gluconeogenic precursor did we learn about that would be crucial for these animals?
carbohydrates in animals
mainly glucose and glycogen in animals
glycogen
Form of glucose storage in animals
Same as the starch in plants
Is stored in muscle (~2% of mass) and liver (up to 8% of mass)
-Less than 1% of weight of animal is carbohydrate
Straight chain of alpha1,4 linked glucoses
Further chains branching off by alpha1, 6 bond
metabolic fates of glucose
Catabolism -Glycolysis→ lactate -Oxidation→ Co2 and H2O Anabolism -Glycogen synthesis -Lipid synthesis
what is a protein
chain of amino acids
amino acids
General Properties:
- 20-25 found in common dietary proteins
- -There are a couple hundred-these are just the common ones that form into proteins
- Chemically diverse, but have a common general formula
- Needs NH2 in order to be an amino acid as well as the rest of the repeating head unit
- -Differences is in the R group
- Deamination: removing amine (NH2) group (this turns it into a keto acid)
- Transamination: moving the amine (NH2) group
biological functions and properties of proteins
Principal organic constituents of body organs and lean tissues
Enormous functional diversity
-Cell membrane structure and transport characteristics
Enzymes
-Hormones, paracrine and autocrine factors (chemical messengers)
-Antibodies
-Mechanical support, coord. Motion
Need continuous replacement because of metabolic turnover, rates vary widely with biological activity
-Turnover of amino acids and proteins and enzymes
general features of proteins metabolism
Mostly absorbed and metabolized as free amino acids; some small peptides are also absorbed and metabolized
Major metabolic fates of absorbed amino acids are:
-Protein synthesis
-Catabolism (deamination, oxidation)
amino acid catabolism
always influx…always things being built and always being broken down
Catabolism is increased when:
-Dietary protein intake exceeds requirements
-Composition of absorbed amino acids is unbalanced EX: one or more amino acids is limiting, regardless of total protein intake
-Gluconeogenesis from amino acids is increased EX: starved animals
body does not have the capacity to store amino acids
If you onboard and eat a lot of amino acid rich foods they are going to be disposed of through urine through the process of catabolism
If your body is deficient in one amino acid necessary for the protein chain it won’t be able to build the chan and you will get rid of the one you could’ve used
Amino acids can go through the process of gluconeogenesis to become glucose-only gluconeogenic amino acids can do this
-Can cause muscle loss in starving animals or animals that have diseases
3 major proteolytic enzymes in the animal digestive tract that are responsible for protein breakdown (proteolysis)
- Pepsin
- Trypsin
- Chymotrypsin
regions of protein breakdown in the gut
Pepsin: stomach/abomasum (in gastric compartment where HCl is)
Chymotrypsin and Trypsin: in SI (specifically through the pancreatic duct into the duodenum)
2 major proteolytic enzymes in the animal digestive tract that are responsible for protein breakdown (proteolysis)
pepsin
trypsin
chymotrypsin
pepsin
Produced and secreted from chief cells (within gastric component) as pepsinogen (A ZYMOGEN as pepsinogen (inactive form of pepsin))
Zymogen activated by HCl-cleaves off the “amino acid mask” to make it active pepsin (from inactive pepsinogen)
Zymogen cleaved to release active enzyme at pH 1.5-2
Catalyzes hydrolysis of peptide bonds-breaking bonds between amino acids to liberate free amino acids or small peptide chains
Will digest up to 20% of ingested amide bonds
Preferred cleavage site after N-terminal of Tyrosine, Tryptophan, Phenylalanine, and Leucine
-Specifically removes these amino acids
what is a zymogen
essentially an inactive format of an enzyme
- Typically something needs to be cleaved off to make it active because it is blocking the active site causing it to be inactive-sits as a stable protein that does nothing
- -EX: Pepsinogen→ pepsin
HCl is only released in the gastrointestinal tract which means pepsinogen is also only being released there
HCl and pepsinogen mixes where food is within the GI tract and turn it to pepsin
- Pepsinogen from one cell-chief cell
- HCl from another cell-parietal cell
- -They react and cleave pepsinogen to turn it into pepsin
- -They have to come from different cells!
- -Acting on the digesta!
- -20% of bonds being broken
intestinal digestion
Remember protein breakdown (proteolysis) in the digestive tract is a two stage process, beginning in the stomach and completed in the small intestine by trypsin and chymotrypsin
-Pepsin and then trypsin and chymotrypsin which ensures the very long proteins are properly broken down
trypsin
Produced and secreted from pancreas as inactive trypsinogen (A ZYMOGEN)
If this was secreted as live active proteins it would kill the cell it was in as well as all the cells around it
Flows to duodenum via pancreatic duct
Zymogen cleaved to release active enzyme at pH 8
Catalyzes hydrolysis of peptide bonds (and can activate additional trypsinogen)-cycle!
Preferred cleavage site at carboxyl side of Lysine and Arginine in peptides (except when followed by proline)
Different targeted amino acids htan pepsin!–> To get the most cleavage areas!
chymotrypsin
Produced and secreted from pancreas as inactive chymotrypsinogen (A ZYMOGEN)
Flows to duodenum via pancreatic duct
Zymogen cleaved by trypsin to release active enzyme
Can cleave trypsinogen and chymotrypsinogen
Catalyzes hydrolysis of peptide bonds
Preferred cleavage site at carboxyl side of Tyrosine, Tryptophan, Phenylalanine (and to a lesser extent Leucine, Methionine, and Histidine) in peptides
Specific target! Breaking down long proteins into smaller links
other proteases
Elastase
Carboxypeptidase (A and B)
Aminopeptidase
-These nonspecifically break up peptide chains after pepsin/trypsin/chymotrypsin
metabolism of amino acids in the intestinal cells
Intestinal cells metabolize the amino acids entering form the intestinal lumen
-Large amino acid requirement for these cells
-A different amino acid profile exits the cells into the bloodstream compared to what entered the cells from the intestinal lumen
Whatever the amino acid profile is that is hitting the jejunum doesn’t go straight into blood stream-the intestinal cells metabolize some of it before putting it into the bloodstream
-The digesta is not a good representation as to what enters the bloodstream due to the high need for amino acids for cell metabolism
nitrogen metabolism of nonruminants
whatever doesn’t get absorbed in the jejunum/ileum area is going to be excreted in the feces and won’t have another chance to be absorbed
dietary protein in the ruminant diet
rumen degradable protein (RDP): microbes can degrade it
-slowly degraded RDP
-quickly degraded RDP
rumen undegradable protein (RUP): microbes cannot degrade it
-digestible RUP
-indigestible RUP
slowly degraded RDP
Microbes have better access to this protein than the quickly degraded RDP-this is more efficient
Microbial proteases and peptidases cleave peptide bonds and release amino acids (AA) from slowly degraded rumen degradable protein
AA are deaminated by microbes, releasing NH3 and carbon-skeletons
The formation of NH3 is rapid and there are very few free AA in the rumen
Microorganisms use NH3, C-skeleton and energy to synthesize their own AA (microbial protein)
quickly degraded RDP
Immediately solubilized to ammonia (NH3), which is used by microbes or absorbed across the rumen wall
If its too quick they can’t get it all-not very efficient
Not overly helpful-not much microbe action and a lot is excreted
digestible RUP
Is broken down in the gastrointestinal tract by the animal
Digested in abomasum and small intestine by proteolytic enzymes (pepsin, trypsin, chymotrypsin) similar to non-ruminants