Food Composition and

Chemistry
Proteins
PROTEINS
• Proteins are complex organic molecules made up of carbon, hydrogen
oxygen, and nitrogen. Most proteins also contain sulphur and
phosphorus along with traces of other elements.
• Basic Structure of Proteins: Proteins are made up of amino acids
which are organic acids with a carboxyl group (COOH) and amino
group (NH2) attached to a carbon atom. R is the functional group
which differentiates one amino acid from another.
• Peptide Linkage The carbon of the carboxyl group of one amino acid
combines with the nitrogen group or amino group of another amino
acid with the loss of one molecule of water. This bond which unites
the two amino acids is called a peptide bond.
 Protein Structure and Conformation
• All proteins are made up of many amino acids joined by peptide
bonds
• A dipeptide contains two amino acids joined by a peptide bond. A
polypeptide contains several amino acids joined by peptide bonds.
• Proteins are usually much larger molecules, containing several
hundred amino acids. They can be hydrolyzed, yielding smaller
polypeptides, by enzymes or by acid digestion
• The amino acid side chains (R groups) project alternately from either
side of the protein chain.
• Proteins are described as having four types of structure— primary,
secondary, tertiary, and quaternary structure—and these build on
each other. The primary structure determines the secondary structure
and so on.
• The primary structure (protein primary structure) of a protein is the specific
sequence of amino acids joined by peptide bonds along the protein chain.
This is the simplest way of looking at protein structure.
• The secondary structure (protein secondary structure) of a protein refers to
the three-dimensional organization of segments of the polypeptide chain.
• Important secondary structures include the following: • Alpha helix:
ordered structure. • Beta pleated sheet: ordered structure. • Random coil:
disordered structure.
• The alpha (α) helix is a corkscrew structure, with 3.6 amino acids per turn. It
is stabilized by intrachain hydrogen bonds; that is, the hydrogen bonds
occur within a single protein chain,
• The oxygen and hydrogen atoms that comprise the peptide bonds are
involved in hydrogen bond formation.
• The α-helix is a stable, organized structure. It cannot be formed if proline is
present, because the bulky five-membered ring prevents formation of the
helix.
• The beta (β) pleated sheet is a more extended conformation than the -helix.
It can be thought of as a zigzag structure rather than a corkscrew.
• These sheets are linked together by interchain hydrogen bonds. (Interchain
hydrogen bonds occur between adjacent sections of the protein chains).
Again, the hydrogen and oxygen atoms that form the peptide bonds are
involved in hydrogen bond formation.
• The random coil is a secondary structure with no regular or ordered pattern
along the polypeptide chain. This is a much more flexible structure than
either the α-helix or β-pleated sheet. It is formed when amino acid side
chains prevent formation of the α-helix or β-pleated sheet. This may occur if
proline is present or if there are highly charged regions within the protein.
• A protein may contain regions of α-helix,
β-sheet, and random coil at different
places along the chain.
• The tertiary structure of a protein refers to the three-dimensional organization of
the complete protein chain. In other words, it refers to the spatial arrangement of a
protein chain that contains regions of α-helix, β-sheet and random coil.
• There are two types of protein tertiary structure: • Fibrous proteins • Globular
proteins
• Fibrous proteins include structural proteins such as collagen (connective tissue
protein) or actin and myosin, which are the proteins that are responsible for muscle
contraction
• Proteins with a fibrous tertiary structure contain a large amount of ordered
secondary structure (either α-helix or β-sheet).
• Globular proteins are compact molecules and are spherical or elliptical in shape, as
their name suggests. These include transport proteins, such as myoglobin, which
carry oxygen to the muscle. The whey proteins and the caseins, both of which are
milk proteins, also are globular proteins
• Globular tertiary structure is favored by proteins with a large number of
hydrophobic amino acids.
• Protein quaternary structure, or the quaternary protein
structure, involves the noncovalent association of protein
chains. The protein chains may or may not be identical.
Examples of quaternary structure include the actomyosin
system of muscles and the casein micelles of milk.
Classification of Protein
• Classification of proteins based on structure
• 1. Fibrillar or fibrous proteins (a) The helix of the protein molecule is stretched.
For example, in muscle myosin the helix is stretched but elastic. In collagen the
helix is stretched to a great extent and is inelastic. (b) They are relatively
insoluble in water and are resistant to acid, alkalis, and moderate heat.
• 2. Globular proteins (a) The helix is bent to give a compact shape, e.g., egg
albumin, globin of haemoglobin, and globulin in meat and pulses. (b) These
proteins are soluble in water and water solutions containing acids, alkalis, salt,
and also in alcohols. They are easily affected by heat. This is due to the fact that
the cross-links holding the helix are weak and hence slight increase in
temperature, or a change in pH, disrupts these crosslinks causing the chains to
unfold, i.e., protein gets denatured.
• Classification based on characterization
• 1. Simple proteins Those which yield amino acids on hydrolysis, e.g.,
albumin in egg white, zein in maize, keratin in hair, and globin in
haemoglobin.
• 2. Compound or conjugated proteins Those proteins which are
combined with a non-protein molecule, e.g., haemoglobin (protein +
haeme), casein (protein + phosphoric acid), mucin (protein +
carbohydrate), and lipoprotein (protein + lipid).
• 3. Derived proteins Those produced by the action of acids, alkalis,
heat, or enzymes on native proteins.
• Classification based on function
• 1. Complete proteins or first class proteins Complete proteins contain
all the essential amino acids. They promote growth and maintain
essential body processes, as kinds and amounts of amino acids are
proportional to body needs, for example, animal proteins from milk,
egg, fish, and meat.
• 2. Partially complete or second class proteins These do not contain all
the essential amino acids in required amounts. So they are capable of
maintaining life but cannot promote growth, e.g., gliadin of wheat.
• 3. Totally incomplete proteins These are deficient in a lot of amino
acids. They are incapable of meeting both major functions of growth
and repair of proteins, e.g., zein in maize and gelatin.
DENATURED PROTEINS
• Denaturation is defined as any non-proteolytic modification in the original
structure of the native proteins, giving rise to definite changes in physical,
chemical, and biological properties.
• Denaturation is brought about by the following: 1. Denaturing agents, such as
acids, alkalis, salts 2. Increase in temperature 3. Extensive beating
• Stages in Heat Denaturation 1. Unfolding of helix of the protein molecules as the
cross-links holding the helix is disrupted. 2. R groups are exposed. Rebonding takes
place between adjacent R groups of protein molecules leading to aggregation of
the molecules, bringing about increased viscosity (1st stage). In 2nd stage, protein is
said to have coagulated, i.e., water is held in the capillary spaces formed by united
protein molecules. If the liquid separates from the coagulated protein, the protein
is said to be, ‘precipitated’ or ‘flocculated’, i.e., ‘curdling’ takes place (3rd stage of
denaturation).
Factors Affecting Denaturation
• pH Denaturation is brought about by controlling pH and occurs at the
IEP when the protein is unstable.
Caseinogen is dispersed as a sol in milk. When milk turns sour (pH 4.6 ;
IEP), it curdles (3rd stage in denaturation). 2. Egg albumin is colloidally
dispersed as a sol. It has a pH of 7.2-7.8. But when the pH is reduced to
4.6 (its IEP) by adding vinegar to water used for poaching eggs, the egg
coagulates faster.
• Heat When egg white is heated at 60°C the protein ovalbumin gets
denatured. As temperature increases, coagulation takes place and egg
white separates out as a solid.
• Surface denaturation This is brought about by mechanical means,
e.g., beating egg white or milk to a foam. Surface denaturation of the
protein takes place leading to pellicle or skin formation. This stabilizes
the foam (pellicle is seen when foam has subsided).
• Salts When present in a high concentration it precipitates proteins out
of solution and disperses them, e.g., cured ham baked in white sauce.
The high salt concentration of the ham can cause the milk in white
sauce to curdle.
• Moisture Low moisture levels cause less denaturation than higher
moisture levels at the same temperature.
Functional properties of specific protein rich
foods
• Gelatin : Gelatin is a partially degraded protein prepared from collagen.
Collagen is the intercellular cementing substance between cells. It is a
hydrophilic colloid. Gelatin contains a large proportion of amino acids
which have a great affinity for water. The long thin fibres of gelatin help in
forming firm gels at low temperatures.
• Polar groups on gelatin molecule bind water molecules in layers forming a
shell around the molecule.
• A concentration of 1-2% gelatin can form a firm gel, which does not melt at
normal serving temperature. Excess gelatin forms a stiff rubbery gel.
• Pieces of baked fish skins, when cooled on the baking pan, stick to it
because of conversion of collagen in the skin of fish to gelatin.
• MILK : Milk is a solution of sugar lactose, and water soluble vitamins and minerals.
It is a colloidal dispersion of protein and an emulsion of fat in water. Water
accounts for 87% of milk.
• Proteins in milk are of two types: 1. Casein - alpha, beta, and kappa caseins 2.
Serum or whey proteins — lactalbumin and lactoglobulins.
• They are of colloidal dimensions and make milk opaque. Casein is colloidally
dispersed in milk as calcium phosphocaseinate. Casein molecules form micelles by
ageregating with calcium and phosphorus.
• Heat denatures and coagulates serum or whey proteins which settle to the
bottom of the container. Casein is insensitive to heat.
• The colour and flavour of condensed milk is because of browning caused by
lactose and milk protein (refer Maillard browning )
• Effect of pH on milk: Fresh milk has a pH of 6.6. Acidity is increased
when acid is added to milk, e.g., while making paneer, or acidity
formed due to natural souring by lactic acid bacteria which ferment
lactose to lactic acid, lowering the pH of milk. This reduces the
stability of casein micelles and it coagulates, forming a gel. This is
because addition of acid neutralizes the charge on protein.
• EGGS
• Egg White | Nine proteins are dispersed as a sol in egg white. The two
albumins, ovalbumin and conalbumin, which form 70% of the proteins
are fibrous proteins. Lysozyme is a globular protein and ovomucin
gives thickness to the egg white. The protein avidin in raw egg white
binds biotin making it unavailable.
• Egg Yolk , Proteins and lipids are the major constituents of dispersed
phase in the yolk. Many proteins are present as lipoproteins. Some
lipoproteins contain lecithin, which is a natural emulsifying agent.
Cholesterol is also present in the yolk.
• Effect of Heat on Egg Proteins Except for ovomucoid, all other egg
white proteins are denatured by heat and get coagulated. The
transparent viscous sol of egg white turns white and opaque, and
forms a gel with water trapped inside. The yolk, which is a thick liquid,
becomes a solid with a mealy texture when denatured by heat. Egg
white begins to coagulate at 60°C and is complete at 65°C, while the
yolk starts to coagulate at 65°C and is coagulated at 70°C. Heating
beyond this temperature shrinks and toughens the coagulated egg
protein.
• Role of Protein in Breadmaking Bread is made from wheat, which is milled into
flour. Wheat flour from hard wheat is higher in protein and is used for
breadmaking, while soft wheat is low in proteins and yields a weak flour which is
suitable for cakes and biscuits.
• The principal protein in bread is gluten which is a protein complex made up of
more or less equal amounts of glutenin and gliadin proteins.
• When flour and water are kneaded together, the gluten complex starts forming
and an elastic dough is formed. This dough is extensible and when yeast produce
carbon dioxide gas, gluten is stretched and forms air cells. On application of heat,
the gluten coagulates and forms a fairly rigid cellular structure. The gluten
matrix, thus, forms the foundation of the structure of all bakery products.
Excessive mixing of the dough can weaken the gluten structure.
• MEAT: Flesh food includes meat, poultry, and fish. The term meat is
used for red meats from animal sources, such as beef, veal, pork, lamb,
or mutton.
• Meat is composed of 15-20% protein of high biological value, 5-40% fat,
B-complex vitamins, iron, and phosphorus.
• The simplest structure in meat protein is the protein molecules, myosin
and actin, which form myofilaments. Thick myofilaments are myosin
and thin myofilaments are actin. Connective tissue consisting mainly of
ground substance, collagen, and little elastin is found between each
fibre. When meat is cooked, collagen is hydrolysed to gelatin.
COMMERCIAL USES OF PROTEINS
• The major role of protein in food preparation includes the ability of proteins to:
• Form foams
• Bind water and form viscous sols and gels
• Get coagulated by heat
• Exhibit emulsifying properties
• Show enzymatic activity
• Egg, milk, and gelatin are used for gels, foams, whips, souffles, meringues,
custards, cakes, puddings, confections, soups, sauces, and gravies.
• Soya bean proteins, protein isolates from oilseed cakes, single cell protein, and
milk proteins are being widely used today by the food processing industry.