2.

2 PROTEIN
Protein are composed of chains of amino acids joined by
peptide bonds.
About 20 amino acids are known.
Each amino acid has at least one amine and one acid
functional group as the name implies.

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The different properties result from variations in the structures of
different R groups.
The R group is often referred to as the amino acid “side chain”.
A distinctive side chain attached to the carbon at the center of
the backbone
◦ Gives identity and chemical nature to each amino acid

(also called the carboxyl group)

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The formation of peptide bond – a condensation reaction

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The different amino acids have interesting
properties because they have a variety of
structural parts which result in different
polarities and solubility.
Polypeptide and proteins are held together by
amide bonds between the amino-end on one
amino acid molecule, and the carboxylate-end of
another amino acid molecule.

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Structures of Amino Acids

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Zwitterion
Amino acid physical properties indicate a “salt-like”
behavior.
Amino acids are crystalline solids with relatively high
melting points, and most are quite soluble in water and
insoluble in non-polar solvents.
In solution, the amino acid molecule appears to have a
charge which changes pH

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An intramolecular neutralization
reaction leads to a salt-like ion
called a zwitterion. The accepted
practice is to show the amino
acids in the zwitterion form
◦ The carbonyl can lose a H ion to become
negatively charge
◦ The amine group can accept a H ion to
become positively charge.

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PROTEIN CLASSIFICATION
Simple proteins
◦ It yield only amino acid on hydrolysis
◦ Eg: albumin, globulins, glutelin, prolamins, scleroproteins,
histone and protamines.

Conjugated proteins
◦ Conjugated protein contain an amino acid part combined with
a non protein material such as lipid, nucleic acid or CHO
◦ Eg: phosphoprotein (casein of milk and egg yolk)

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Derived protein
◦ These compound obtained by chemical or enzymatic methods, and can be divided
into primary and secondary derivatives.
◦ For example: rennet-coagulated casein (primary derivatives)
◦ Proteoses, peptone and peptides (secondary derivatives)

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PROTEIN STRUCTURE
Four levels of protein structure exits:
1. Primary
2. Secondary
3. Tertiary
4. Quaternary

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Primary
Primary structure – sequence linear of amino acids from N-terminal to C-
terminal
NCC-NCC-NCC-NCC-NCC-NCC-NCC
The sequence of amino acids… ala-gly-phe-gly-arg-ala-ala-leu

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Secondary
Single polypeptide chain.
H bonding to side groups of amino acids several places away, forms folded or
coiled structure

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Tertiary
This three dimensional conformation is held together by variety of interactions
between amino acid side chains. These interactions include:
◦ Hydrogen bonding
◦ Van der Waals forces
◦ Disulphide bonding

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Quaternary

These protein are made of two or

more smaller unit of polypeptide.
Two or more tertiary proteins join
up

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Protein Denaturation
Unfolding structure (due to H bonds breaking) without disrupting
covalent bonds
Denaturation of proteins involves the disruption and possible
destruction of both the secondary and tertiary structures
Since denaturation reaction are not strong enough to break the
peptide bonds, the primary structure (sequence of amino acids)
remains the same after a denaturation process
Original properties of protein will change during denaturation
(eg. Function will be stopped; solubility in water will decreases).

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Protein denaturation in food preparation
Roasting of meat: denatures the protein such as actin, myosin
and myoglobin
Cooking egg: denatures egg white protein including ovalbumin
Whipping egg whites: denatures some of the protein and helps
stabilise egg white foams
Changing degree of acidity-disrupt the salt briges. This reaction
occurs in the digestive system, when the acidic gastric juices
cause the curdling (coagulating)of milk

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Protein denaturation in food preparation
Changing concentrations of mineral salts- also disrupt the salt briges, high
affinity and attraction for sulphur and will also lead to the denaturation of
protein
Freezing process

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FUNCTIONAL PROPERTIES OF
PROTEIN
Buffering
Emulsification
Enzymes
Solubility
Foaming
Gelation
Water-Holding-Capacity
Fat reduction
Viscosity
Hydrolysis
Flavour binding
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