Digestion of protein

Food proteins are hydrolysed to peptides and amino acids

by rumen microorganisms, but some amino acids are
degraded further, to organic acids, ammonia and carbon
dioxide.

The main proteolytic organisms are Prevotella ruminicola,

Peptostreptococci species and the protozoa.

The ammonia produced, together with some small peptides

and free amino acids, is utilised by the rumen organisms to
synthesise microbial proteins.
The ammonia in rumen liquor is the key intermediate in
microbial degradation and synthesis of protein.

If the diet is deficient in protein, or if the protein resists

degradation, then the concentration of rumen ammonia will be low
(about 50 mg/l) and the growth of rumen organisms will be slow;
in consequence, the breakdown of carbohydrates will be retarded.

On the other hand, if protein degradation proceeds more rapidly

than synthesis, then ammonia will accumulate in rumen liquor and
the optimum concentration will be exceeded.

When this happens, ammonia is absorbed into the blood, carried

to the liver and converted to urea.
 Some of this urea may be returned to the rumen via the saliva and
also directly through the rumen wall, but the greater part is
excreted in the urine and thus wasted.
Protein Metabolism

Proteins are synthesised from amino acids, which become available either
from the end products of digestion or as the result of synthetic processes
within the body.
Direct amination may take place as in the case of -ketoglutarate, which
yields glutamate:

α-Ketoglutarate + NH4+ + NADPH(+H+) Glutamate

dehydrogenase

Glutamate + NADP+ + H2O

 The glutamate may undergo further amination to give glutamine but,
more importantly, may undergo transamination reactions with various
keto acids to give amino acids as shown:

Amino acids other than glutamate may undergo such transaminations to produce
new amino acids.
Deamination: Deamination is the removal of amino group from an amino
acid which may be oxidative or nonoxidative.

The first stage in the oxidative degradation of amino acids is the removal of the
amino group by one of two main pathways, oxidative deamination or
transamination.
In transamination the amino group is transferred to the -carbon atom of a keto
acid, usually -ketoglutarate, resulting in the production of another keto acid and
glutamate.The reactions are catalysed by enzymes known as aminotransferases
Nonoxidative deamination: These reactions are catalyzed by amino
acid dehydratase and also require vitamin B6.
Serine Pyruvate + NH4+
Threonine Alpha- Ketoglutarate + NH4+
Aspartic acid Fumaric acid + NH4+
Deamination of amino acids occurs in all the organs of
the body but primarily in the liver. In most other tissues
the ammonia is converted to glutamine or alanine (in
muscle) before being transported to the liver and
regenerated. In mammals the ammoniais then converted
into urea.
Disposal of Excess Amino Acids

The extra amino acids are promptly metabolized

often within hours.

The ammonia is converted to urea in liver and

excreted.

Urea is formed in the liver through Krebs-

Henseleit cycle.
Steps of urea cycle.
1 Formation of carbomyl phosphate. Enzyme required is
carbamoyl phosphate synthetase.
2 Formation of citrulline from CP and ornithine. Enzyme
is ornithine- carbamoyl transferase.
3 Formation of argininosuccinate and arginine. A second
amino group is transferred from aspartic acid to
carbamoyl keto group of citrulline, to produce
argininosuccinate. Enzyme needed is argininosuccinate
synthetase. Argininosuccinate cleaves argininosuccinate to
give arginine and fumarate.
4 In the presence of an enzyme, arginase and magnesium,
arginine yields one molecule of urea and of ornithine. The
regenerated ornithine can participate in the next turn of the
cycle. There is a net loss of 1 ATP per mole of urea
synthesized from glutamic acids.