Denaturation of Proteins

Denaturation of proteins involves the disruption and possible destruction of both the
secondary and tertiary structures. Since denaturation reactions are not strong enough to break
the peptide bonds, the primary structure (sequence of amino acids) remains the same after a
denaturation process. Denaturation disrupts the normal alpha-helix and beta sheets in a protein
and uncoils it into a random shape.
Denaturation occurs because the bonding interactions responsible for the secondary structure
(hydrogen bonds to amides) and tertiary structure are disrupted. In tertiary structure there are
four types of bonding interactions between "side chains" including: hydrogen bonding, salt
bridges, disulfide bonds, and non-polar hydrophobic interactions. Which may be disrupted.
Therefore, a variety of reagents and conditions can cause denaturation. The most common
observation in the denaturation process is the precipitation or coagulation of the protein.
Heat:
Heat can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. This occurs
because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and
violently that the bonds are disrupted. The proteins in eggs denature and coagulate during
cooking. Other foods are cooked to denature the proteins to make it easier for enzymes to digest
them. Medical supplies and instruments are sterilized by heating to denature proteins in bacteria
and thus destroy the bacteria.
Retrieved September 4 2015 http://chemistry.elmhurst.edu/vchembook/568denaturation.html
Isoelectric point
(Biochem) the pH value at which the net electric charge of a molecule,such as a protein or amin
o acid, is zero
Isoelectric point
The pH at which the electrolyte concentration of an amphoteric substancesuch as protein is elect
rically zero because the concentration of its cationform equals the concentration of its anion form
.
Retrieved September 4 2015 http://dictionary.reference.com/browse/isoelectric+point
The characteristic pH of a solution at which the net charge on protein is zero (positive and negative charges
are equal) is defined as theisoelectric point (pH). The isoelectric point of a protein is animportant property
because it is at this point that the protein is least soluble, and therefore unstable.
Milk Proteins :
There are several types of proteins in milk.
The major milk proteins are unique to milk.
- not found in any other tissue
Milk proteins, particularly caseins, have an appropriate amino acid
composition for growth and development of the young.
Other proteins in milk include an array of enzymes, proteins involved in
transporting nutrients, proteins involved in disease resistance (antibodies and
others), growth factors, etc.
The total protein component of milk is composed of numerous specific proteins.
The primary group of milk proteins are the caseins. There are 3 or 4 caseins in
the milk of most species; the different caseins are distinct molecules but are
similar in structure. All other proteins found in milk are grouped together under
the name of whey proteins. The major whey proteins in cow milk are betalactoglobulin andalpha-lactalbumin.
The major milk proteins, including the caseins, -lactoglobulin and alactalbumin, are synthesized in the mammary epithelial cells and are only
produced by the mammary gland. The immunoglobulin and serum albumin in
milk are not synthesized by the epithelial cells. Instead, they are absorbed from

the blood (both serum albumin and the immunoglobulins). An exception to this
is that a limited amount of immunoglobulin is synthesized by lymphocytes
which reside in the mammary tissue (called plasma cells). These latter cells
provide the mammary gland with local immunity.
Caseins have an appropriate amino acid composition that is important for
growth and development of the nursing young. This high quality protein in cow
milk is one of the key reasons why milk is such an important human food.
Caseins are highly digestible in the intestine and are a high quality source of
amino acids. Most whey proteins are relatively less digestible in the intestine,
although all of them are digested to some degree. When substantial whey
protein is not digested fully in the intestine, some of the intact protein may
stimulate a localized intestinal or a systemic immune response. This is
sometimes referred to as milk protein allergy and is most often thought to be
caused by -lactoglobulin. Milk protein allergy is only one type of food protein
allergy.
Caseins is composed of several similar proteins which form a multi-molecular,
granular structure called a casein micelle. In addition to casein molecules, the
casein micelle contains water and salts (mainly calcium and phosphorous).
Some enzymes are associated with casein micelles, too. The micellar structure
of casein in milk is an important part of the mode of digestion of milk in the
stomach and intestine, the basis for many of the milk products industries (such
as the cheese industry), and the basis for our ability to easily separate some
proteins and other components from cow milk. Casein is one of the most
abundant organic components of milk, in addition to the lactose and milk fat.
Individual molecules of casein alone are not very soluble in the aqueous
environment of milk. However, the casein micelle granules are maintained as a
colloidal suspension in milk. If the micellar structure is disturbed, the micelles
may come apart and the casein may come out of solution, forming the
gelatinous material of the curd. This is part of the basis for formation of all
non-fluid milk products like cheese.

It is casein. The protein precipitates (milk curdles) because the protein reaches it's isoelectric
point. Some amino acids have charges and pH affects these charges. When the pH is at a point
when there is no total charge on the protein, it is at its isoelectric point. Without a charge, the
protein can't interact as well with water and loses its hydration shell so solubility is at its lowest
at this point. It interacts with the other protein molecules instead and causes precipitation. The
pH in milk changes over time because lactic acid bacteria in the milk produce lactic acid which
lowers the pH of the milk.
http://ansci.illinois.edu/static/ansc438/Milkcompsynth/milkcomp_protein.htm