FUNCTIONAL PROPERTIES OF

PROTEINS
PRESENTED BY:-
BAISHALI PANDEY
A4312615050
BTECH. FOOD TECH.
 What are proteins ?
• Proteins are large, complex molecules that play many critical roles in the body.
• Proteins are made up of hundreds or thousands of smaller units called amino acids,
which are attached to one another in long chains.
• The sequence of amino acids determines each protein’s unique 3-dimensional
structure and its specific function.
• Each of these amino acids has a fundamental design composed of a
central carbon (also called the alpha carbon) bonded to: a hydrogen,
a carboxyl group, an amino group , a unique side chain or R-group.
 Levels of Protein Structure
Structural features of proteins are usually described at four levels of complexity:
• Primary structure: the linear arrangement of amino acids in a protein and the location of
covalent linkages such as disulphide bonds between amino acids.
• Secondary structure: areas of folding or coiling within a protein; examples include alpha
helices and pleated sheets, which are stabilized by hydrogen bonding.
• Tertiary structure: the final three-dimensional structure of a protein, which results from a
large number of non-covalent interactions between amino acids.
• Quaternary structure: non-covalent interactions that bind multiple polypeptides into a
single, larger protein. Haemoglobin has quaternary structure due to association of two alpha
globin and two beta globin polyproteins.
FUNCTIONAL PROPERTIES OF PROTEINS
Hydration Properties:
• PDI (Proteins Dispersibility Index) –It is a means of comparing the solubility of
a protein in water, and is widely used in the soybean product industry.
• WHC (Water Holding Capacity)-WHC is a physical property and ability of a food
structure to prevent water from being released from the 3-D structure of the
protein. It plays a major role in formation of food texture , in meat products and
baked dough.
• OHC (Oil Holding Capacity)-WHC represents the quantity of oil the proteins
powder is apt to retain. The results are expressed as the number of times the
proteins powder is able to retain its weight of oil.
Structural & textural properties (Rheology)

• Viscosity-It is a key ingredient in determining protein stability. Protein stability is a critical

factor in protein drug formulation, drug efficiency, and storage shelf life. When proteins
become unstable, molecules unfold and aggregate, causing the viscosity of the protein to
increase.
• Visco-elasticity- The viscoelasticity is characterized at oscillating mode by a DHR2
rheometer from TA Instruments. The results are expressed by defining the G’ (elastic) and
G’’ (viscous) moduli.
• Gelling properties- The gelling capacity of food proteins is an important functional attribute
for food manufacturing. Together with pectin,starches and gums they form strong
gels. Gelation is a basic process in the processing of various foods, milk gels, meat and fish
products, fruit jellies, pie and cake fillings, coagulated egg white and others.
Surface properties (Emulsifying & foaming)

• Emulsifying properties- Protein emulsifying activity is the ability of a protein to

participate in emulsion formation. The emulsifying capacity is the ability of protein
solution to emulsify oil. These play an important role in he development of new
sources of plant protein products for used as foods.
• foaming properties- The property of proteins to form stable foams is important in
the production of variety of foods. The most widely used protein foaming agents
are egg white,gelatins,gluten etc. Proteins vary significantly in their foaming
properties such as serum albumin is an excellent foaming agent while purified
ovalbumin is poor.Proteins in foams contribute to the uniform distribution of fine
air cells in the structure of foods.
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