NTRODUCTION

Proteins are essential constituents of all organisms. It can be isolated from their
nativesource and then purified by different methods. These techniques depends on the
differences inthe molecular weight, sizes, charges, solubility and their acid-base behavior.
(1)
Egg white is the common name for the clear liquid contained within anegg.It is formed
fromthe layers of secretions of the anterior section of the hen's oviduct during
the passage of
thee g g . I t f o r m s a r o u n d e i t h e r f e r t i l i z e d o r u n f e r t i l i z e d e g g . I t c
o n s i s t s m a i n l y o f a b o u t 15%proteinsdissolved in water. Its primary natural purpose
is to protect theegg yolkand provideadditional nutrition for the growth of theembryo, as it is
rich in proteins and also of high nutritionalvalue.
(3)
MATERIALS AND METHODS
The first procedure of the experiment was the isolation of ovoglobulin and ovalbumin from
theegg white. The egg white was carefully separated from the yolk of one
medium-sized chickenegg. The volume of the egg white was measured in a pre-weighed
graduated cylinder and then itwas weighed on the analytical balance. The isolated egg white
was divided, and three-fourth wasused for the isolation and the remaining was for
the characterization of egg white proteins. A3.06g of NaCl powder was added for
every 10ml of the divided egg white sample. Stirred gently,until there were no precipitation of
ovoglobulin was observed. Then it was filtered with a cheesecloth to separate the filtrate.
The residue was transferred to pre-weighed filter paper to dry. Thenthe dried sample was
weighed and the percent yield was calculated for ovoglobulin. The filtrateplaced on a beaker
was added 2-3 drops of 0.200M acetic acid and subjected to heat to boil untilovalbumin
precipitates. Then the residue was transferred to pre-weighed filter paper to dry. Thenthe
dried sample was weighed and the percent yield was calculated for the ovalbumin.The
remaining isolated egg white sample was used for the qualitative test and denaturationof
protein. It was diluted with equal volume of phosphate buffer and then filtered with
cheesecloth.For the qualitative test of protein, a 1.00ml of egg white solution was transferred
to four separate