EPF 4602

BIOMATERIAL POLYMER
TECHNOLOGY

RUZANNA BT AHMAD SHAPII

(158983)
NOR DALILA BT HASHIM (156293)

WHAT IS PROTEIN?
Protein
is
a
large
biological
molecule consisting of one or more
chains of amino acids.

STRUCTURE OF PROTEIN
LINEAR
STRUCTURE

linear arrangement of amino acids

Linked by covalent linkages such as
disulfide bonds between amino acids.

SECONDARY
STRUCTURE

folding or coiling within a protein;

examples include alpha helices and
pleated sheets
stabilized by hydrogen bonding

TERTIARY
STRUCTURE

three-dimensional structure of a
protein
have a large number of non-covalent
interactions between amino acids.

QUARTENARY
STRUCTURE

bind multiple polypeptides into a

single, larger protein
Hemoglobin has quaternary structure
due to association of two alpha
globin and two beta globin
polyproteins.

STRUCTURE OF PROTEIN

CLASSIFICATIO
N OF PROTEIN

Simple proteins

Conjugated proteins

chains of amino acid units

only joined by peptide
linkages.
Examples are : Egg albumin,
serum globulins, glutenin in
wheat, coryzenin in rice,
tissue globulin, etc.

composed of simple
proteins and non protein
material.
The non-protein material is
called prosthetic group or
cofactor
Examples are Mucin in
saliva (prosthetic group,
carbohydrate), casein in
milk (prosthetic group,
phosphoric acid),
haemoglobin in blood
(prosthetic group, iron
pigment), etc.

Simple Protein

Conjugated Protein

made up of polypeptide chains that run parallel to the axis

held together by strong hydrogen and disulphide bonds
can be stretched and contracted like a thread
usually insoluble in water.
Examples are : a-keratin (hair, wool, silk and nails); myosin
(muscles); collagen (tendons, bones), etc.

Globular
proteins

Fibrous
proteins

have more or less spherical shape (compact structure)

a-helics are tightly held up by weak attractive forces of
various types: Hydrogen bonding, disulphide bridges, salt or
ionic bridges.
usually soluble in water.
Examples are: Insulin, pepsin, haemoglobin, cytochromes,
albumins, etc.

PHYSICAL
PROPERTIES OF
PROTEIN

SIZE AND SHAPE

Size of protein usually measured in molecular
weight (mass).
Molecular weight of protein is the mass of one
mole of protein usually measured in units
daltons.
It can be estimated by methods including
electrophoresis, gel filtration, and more
recently by mass spectrometry.
Most proteins have a mass between 10 and
100 kilodaltons (kD).
A small protein consists of about 50 amino
acids while larger proteins may contain 3,000

HYDROPHOBICITY
Hydrophobic means fear of water.
In aqueous solutions, proteins tend to fold
so that areas of the protein with
hydrophobic regions are located in internal
surfaces next to each other and away from
the polar water molecules of the solution.

 Polar groups on the amino acid are

called hydrophilic (water loving)
because they will form hydrogen
bonds with water molecules.
The number, type and distribution of
nonpolar amino acid residues within
the
protein
determines
its
hydrophobic character.

SOLUBILITY
Solubility is the amount of a solute that
can be dissolved in a solvent.
The 3-D structure of a protein affects its
solubility properties.
For example:
Cytoplasmic
proteins
have
mostly
hydrophilic (polar) amino acids on their
surface and are therefore water soluble,
with more hydrophobic groups located on
the interior of the protein, sheltered from
the aqueous environment.

In contrast, proteins that reside in the lipid

environment of the cell membrane have mostly
hydrophobic amino acids (non polar) on their
exterior surface and are not readily soluble in
aqueous solutions.

Any changes to condition such as buffer, solvent

type, pH, ionic strength and temperature will
cause protein to lose the solubility.

ISOELECTRIC POINT
The isoelectric point (pI) of a protein
is the pH where the net charge on
the protein is zero.
Proteins have different isoelectric
points because of their different
amino acid sequences.
They can be separated by adjusting
the pH of a solution.

APPLICATION
OF PROTEIN

FOOD INDUSTRY
Gelling agent
- Give shape and structure to food.
Emulsifiers
- Emulsions in food are mixtures of oil and
water.
- Mayonnaise contains oil and water. The
emulsifier keeps these mixed and
without it
the oil and water separate.

 Foaming agent
- Material that facilitates formation of
foam.
Thickeners
- Thickening agents make foods
thicker.

CRYSTALIZATION
To form a high-quality crystal, a
protein must be immobilized in a
lattice in a consistent conformation
with limited dynamic motion.
Protein surface properties play a
determining
role
in
controlling
crystallization
behavior
because
formation of tight, geometrically
precise intermolecular contacts is
required for lattice stability.

FABRIC FROM ELASTIN

Elastin is a matrix protein. It holds the cells
together into tissues and provides natural
support and flexibility.
It gives skin and blood vessels their
elasticity.
Elastin will serve as a scaffold which can
be sewed or glued in the place of a
missing part.
It will hold the artery or organ closed and
intact while at the same time it can also
be populated by the body's own cells

SOY PROTEIN-BASED
PLASTICS
Blending soy protein with polyesters using
a polyvinyllactam as a compatibilizer
successfully made soy protein-based
plastics.
The
blends
were
processed
by
compounding extrusion and injection
molding.
Blends made from soy protein flour
produced plastics with the lowest water
absorption.

Thank you