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FEED FORMULATION

PROTEINS AND AMINO ACIDS


MEMBERS
STUDENT NAME REG NO;

AISU RONALD 19/U/7868/PS


KIVENGERI DENIS 19/U/22205/PS

SEBWATO PAUL 19/U/29651/PS

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OBJECTIVES
• To understand the biochemistry of proteins and
amino acids.
• To understand roles of proteins and amino acids.
• To understand the EEA and NEAA.
• Know the need of proteins and amino acids in feed
formulation.
• Know the deficiency signs of amino acids in a fish
diet.

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INTRODUCTION
• Proteins and amino acids are critical molecules
because of the roles they play in the structure and
metabolism of all living organisms.

• Amino acids are the final product of protein


digestion in animal body systems.

• Amino acids link together by a covalent peptide


bond between the α-carboxyl end of one amino
acid and α-amino end of another forming proteins.
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INTRODUCTION

Peptide chain. Any number of amino acid joined by successive


peptide linkages.

Dipeptide. An oligomer consisting of two amino acids.

Polypeptide. Peptides of two to around 20 amino acid


residues.

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PROTEIN STRUCTURE
PROTEIN STRUCTURE
Made up of chains of Amino acids, forming four
different structure levels;

• Primary structure
• Secondary structure
• Tertiary structure
• Quaternary structure

Note; Any alteration in the structure or sequencing


changes the shape and function of the protein
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CLASSIFICATION OF
PROTEINS
• Fibrous proteins; exist as elongated filamentous chains e.g. the
collagens, elastin, and keratin.

• Globular proteins; include all enzymes, antigens and hormone


proteins, albumins, globulins and histones.

• Conjugated proteins; proteins which yield non-protein groups as


well as amino acids on hydrolysis e.g.
phosphoproteins
Glycoproteins
Lipoproteins
chromoproteins (haemoglobin, haemocyanin, cytochrome, flavoproteins)
and nucleoproteins
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PROTEIN DENATURATION
Proteins can be ‘denatured’ by heat, strong
acid, alkali, alcohol, acetone, urea and by
heavy metal salts

At denaturation, proteins loose their unique


structure which affects their chemical,
physical and biological properties

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PROTEIN SOURCES
Feed ingredient Finfish Crustaceans
Oilseed protein Range of use Mean use Range of use Mean use

Canola meal 2-25 6-18 2-20 4-12

Rapeseed meal 2-25 5-15 2-20 5-15

Cottonseed meal 5-25 10-15 3-20 10-15

Oil palm (kernel) 5-25 10-15 3-20 10-15

Peanut meal 5-25 10-15 3-20 10-15

Soybean meal 5-30 10-20 5-35 10-15

Soybean protein concentrate 2-10 3-5 2-10 3-5

Sunflower seed 2-25 10-15 2-20 6-12

Source: FAO, Rome 2009

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PROTEIN FUNCTIONS
• Repair worn or wasted tissue (tissue repair and maintenance)
and to rebuild new tissue (as new protein and growth).

• Dietary protein is required for the formation of hormones,


enzymes and haemoglobin.

• Proteins form enzymes that catalyze biochemical reactions or


transporters that allow the entry and exit of molecules
through cells.

• Myosin protein (contracting muscles) have a mechanical


function and are capable of generating mechanical forces.

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PROTEIN FUNCTIONS
• Components of cell membranes in form of actin
and tabulin.
• Dietary protein can be catabolized as a source of
energy

• Form part of immunoglobins and antibodies hence


defense against diseases in fish.

• Collagen and elastin form connective tissues

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PROTEIN FUNCTIONS
• Protein deposition promotes weight gain in fish

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GROSS PROTEIN
REQUIREMENT (GPR)
• GPR is highest during initial feeding
• Dependent on size/age and water temperature
• For maximum growth;
Growth stage Tilapia (%) Cat fish (%)

Fry 35-40 40

Fingerlings 30-40 30-45

Mature fish 20-25 25-35


AMINO ACIDS
• Amino acids are
molecules containing
both amine (NH2) &
acidic carboxyl
functional groups (-
COOH).
• General formula being
H2NCHRCOOH
• R-groups influence size,
shape, electrical charge
and other
characteristics
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TYPES OF AMINO ACIDS
• Essential amino acids (EAA); cannot be synthesized within the
animal body . Therefore must be supplied in a ready made
form in the diet.

• Non-essential amino acids (NEAA); can be synthesized in the


body from a suitable carbon source and amino groups from
other amino acids.

• Semi-/conditionally essential AA i.e. tyrosine and cysteine


(synthesized from Phe and Met respectively)
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ESSENTIAL AMINO ACIDS NON-ESSENTIAL AMINO
ACIDS
Arginine Arg Alanine Ala
Histidine His Asparagine Asn
Isoleucine Ile Aspartate Asp
Leucine Leu Glycine Gly
Lysine Lys Glutamine Gln
Methionine Met Glutamate Glu
Phenylalanine Phe Proline Pro
Threonine Thr Serine Ser
Tryptophan Trp Tyrosine Tyr
Valine
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AMINO ACIDS &
METABOLISM
• Beside their role as the building blocks of protein, amino acids
also have a variety of roles in metabolism.

• Important in many other biological molecules such as;

Forming parts of coenzymes,


Precursors for the biosynthesis
Structural molecules (e.g., heme, chitin, and purine bases)
Metabolic intermediates (e.g., acetate and pyruvate)
Neurotransmitters & hormones
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AMINO ACID CATABOLISM
• End products of amino acid catabolism are ammonia,
carbon dioxide & bicarbonate.

• Deposition of amino acids into body protein represents


between 25%-50% of total amino acid consumed.

Breakdown of amino acids


Removal of amino acid group (deamination)
Conversion of the carbon skeletons into citric acid cycle
intermediates.
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AMINO ACIDS IN FEED
FORMULATION
• When formulating feeds with diets deficient in
digestible EAA requirements of fish;

Increase the total protein level of the diet

Supplementation with crystalline amino acids

Use of combination of different protein sources


with different amino acid profiles.

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DEFICIENCY SIGNS
Lysine. Deficient in plant-based protein sources.
Reduced growth and feed efficiency
Dorsal and caudal fin erosion, poor growth

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DEFICIENCY SIGNS
Sulfur-amino acids (methionine and cysteine)
Cataracts in salmonoids
Excess Met is toxic

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DEFICIENCY SIGNS
Branched chain amino acids (leucine, isoleucine
and valine)
Neurological deformities

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DEFICIENCY SIGNS
Histidine
Poor growth performance and food utilization,
lordosis, high stress response
Excess histidine leads to extensive necrosis in
epithelial cells.

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DEFICIENCY SIGNS
Tryptophan
Scoliosis, lordosis, elevated Ca, Mg and Na
concentrations

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DEFICIENCY SIGNS
Taurine (Cysteine derivative)
• Green liver disease

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CONCLUSION
• Different Protein sources have different amino acids
composition therefore it is important to understand
the nature of protein sources that are to be
incorporated into fish feeds for maximum protein
deposition.

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REFERENCES
• Buxbaum, E. (2007). Fundamentals o f Protein Structure and
Function. New York: Springer.
• NRC (2011). Nutrient requirements of fish and shrimp.
Washington, D.C. The National Academies Press.
• Afonso JM, Montero D, Robaina L, Astorga N, Izquierdo MS
and Ginés R. 2000. Association of a lordosisscoliosis-
kyphosis deformity in gilthead seabream (Sparus aurata)
with family structure. Fish Physiol Biochem 22, 159-163.
• Prabu, E;Felix,S; Felix,N; Anilan, B and Ruby, P.(2017). An
overview on significance of fish nutrition in aquaculture
industry.IJFAS,5(6):349-355.

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