SRI VENKATESWARA VETERINARY UNIVERSITY COLLEGE

OF VETERINARY SCIENCE, PRODDATUR.

DEPARTMENT OF ANIMAL NUTRITION

Submitted To : Dr.Balakesava Reddy Submitted by : Neha Mommela

Assistant professor PV/19-30
◦ Proteins are complex organic compounds of high molecular weight.
◦ They contain C, H, O and N.
◦ Presence of N distinguishes them from carbohydrate and fat.
◦ In addition, some proteins have sulphur and phosphrous.

Elementary composition of protein :

Carbon Hydrogen Nitrogen Sulphur Phosphorous

51-55 % 6.5-7.3 % 15.5-18 % 0.5-2% 0-15 %

Proteins are polymers of amino acid, which vary in relative amounts and
kind from protein to protein.

They vary in size, shape, suitability and biological function.

There are around 200 naturally occurring amino acids, among them only
20 are commonly found in most of the proteins and up to 10 amino acids
are not adequate to meet the metabolic needs.
◦ Amino acids are organic compounds that contain amino (–NH2) and
carboxyl (–COOH) functional groups, along with a side chain (R group)
specific to each amino acid.
Aliphatic, aromatic and Heterocyclic amino acids
• Based on the number of amino and carboxyl group present. They are
(a)Mono-amino, mono-carboxylic acids -Glyceine,alanine,valine,lucerne,isolucine
(b)Mono-amino, dicarboxylic acids - Aspartic, Glutomic acid
(c)Diamino, monocarboxylic acids-Arginine, lysine
According to their catabolic fates as
• Glucogenic
• Ketogenic-leucine and lysine
• Glucogenic (or) ketogenic.-phenylalanine, isoleucine, tyrosine, threonine.
◦ From nutritional point of view, they are classified as
essential and non-essential amino acids.

Non-essential amino acid/Dispensable

• They can be synthesized from whatever precursor available
• Eg: Amino nitrogen.

Essential or Indispensable amino acids

• They are unable to synthesize in body. Hence, needs to be supplied
through diet.
• ALL MP HIV TT
• Synthesis of cell protoplasm
• For the repair of wear and tear
• Synthesis of Bile acid
• Synthesis of Hormones, enzymes, milk proteins
• Synthesis of Melanin
• Formation of Rhodopsin
• Supply of energy
• Precursor for many of the biological compounds
Non-ruminants: Amino acid availability is critical in the nutrition.
• Since, they do not have the ability to synthesise certain essential amino
acids.
• The requirement of individual amino acid have to be calculated to avoid a
deficiency or excess.

In Ruminants: The dietary protein is subjected to microbial attack in the

rumen and synthesize microbial protein which is digested in small intestine.
Proteolytic Inhibitors:
Soyabean trypsin inhibitor

Increased secretion of trypsin due to binding of

trypsin to the inhibitor

hypertrophy of pancreas

growth depression
(loss of amino acid in enzyme secreted by hyperactive pancreas and excreted in faeces)
Over heating of protein
Maillard reaction or browning reaction:
Aldehyde group of reducing sugar
+
ε-amino group of lysine
growth depression

lysine unavailable
• High quality protein: Those proteins whose amino acid molecules are
more nearly approximate the needs of the animal.
Eg.: animal protein.
• Low quality protein: Which do not meet the needs of the animal.
Eg. Plant protein
• Dispensable Amino acids:They make up to 40% of tissue protein and are
of quantitatively important.
Not all must be synthesized as the diet can provide many. If there is short
supply, the cells with an adequate supply of amino nitrogen and a source of
carbon and energy will make up the deficit.
• Non protein nitrogenous compounds. Those contain elemental nitrogen
in them but are not proteins.

• These are not associated with proteins.

Eg: free amino acids, amines, amides, urea, nitrates etc.,

• The primary aspect distinguishing ruminants and non-ruminants

digestivesystem is ability to utilize NPN compounds.
• NPN compounds are important for ruminants.

• In feeds all nitrogen is not a true proteins but contain NPN compounds

• about 20-30% of the whole nitrogen in field grass,

• 50% of the nitrogen in silages and
• 40-50% of the whole nitrogen in roots, nodes etc.,Is NPN compounds.
Enzyme Production site Splits peptide bond pH of optimal activity
adjacent to
Trypsia stomach Tryptophan, 1.8 - 2.0
phenylalanine, tyrosine,
methionine, leucine

Trypsin pancreas Arginine, Lysine 8-9

Chymotrypsin pancreas phenylalanine, tyrosine, 8-9
methionine
Elastase pancreas Aliphatic amino acids 8-9

Carboxypeptidase A pancreas Aromatic amino acids 7.2

Carboxypeptidase B pancreas Arginine, Lysine 8.0

Aminopeptidase intestine Amino acid with free 7.4

NH₂. group
• @ small intestine
• Na dependant active transport.
• Pyridoxine enhances amino acid transport across cell membrane.
• Amino acid transport system for neutral, basic and acid Amino acid.
• Members of each group compete among themselves, but not with those of
other groups forabsorption.
• Rate of amino acid absorption depends on amino acid composition of the diet
Note: intestinal epithelium is impermeable to protein. New born mammals absorb protein
(immunoglobulin) in the colostrum.
Ammonia N concentration –
• Rumen degradable protein (RDP)
• Rumen undegradable protein (UDP)
• Microbial protein

Amino acids in the diet undergo :

• Hydrolysis in GI tract (catabolism)
• Amino acids in intestinal lumen (absorption)
• Amino acids in blood (anabolism)
• Intact tissue proteins
• Oxidative degradation of amino acids by two pathways
1.Transamination
2.Deamination
• Amino group is transferred from α- carbon atom of keto acid results in
production of another keto acid.
• Amino group is removed from amino acids.
 Protein deficiency
• Retarded growth in young animals
• weight loss, reduced lean body mass in adults
• impaired reproductive and work performance in adults.
• Skin, hair and hoof problem
• Risk of infections
 THANK YOU

Reference :Applied Nutrition by D.V.Reddy