KENDRIYA VIDYALAYA

DHARMAPURI
CHEMISTRY INVESTIGATORY PROJECT
ON

TO STUDY OF DENATURATION OF MILK AND EGG

PROTEIN

SUMBITTED BY
NAME:
CLASS: XII-A
ROLL NO: 12A
 Certificate

This is to certify that master of class XII-A has done the project in Chemistry
on ‘TO STUDY OF DENATURATION OF MILK AND EGG PROTEIN’ for the
partial fulfillment of AISSCE 2022-2023

INTERNAL EXAMINER -
EXTERNAL EXAMINER -
PRINCIPAL -
 Acknowledgement
I place my sincere thanks to my chemistry teacher
Mrs. M.THENDRALPRIYA, MSc, B.Ed. for the valuable guidance and
his advice to complete my work successfully

Special thanks of mine go to my colleagues. Who helped me a lot in completing

the project by giving interesting ideas, thoughts & made this project easy and
accurate. I wish to thank my parents for their undivided support & interest who
inspired me & encouraged me to go my own way, without which I would be
unable to complete my project. And at last by no means the least I would thanks
to god who made all the things possible
 INDEX
SR.NO CONTENTS PAGE NO

I Certificate

II Acknowledgement

III Aim

V Introduction

VI Material Required

VII Procedure

VIII Observation
IX Photos
X Result
XII Bibliography
AIM:-
TO STUDY OF DENATURATION OF MILK AND EGG
PROTEIN
INTRODUCTION
Protein denaturation:
Denaturation is a process in which proteins or nucleic acids
lose the quaternary structure, tertiary structure, and secondary
stn1cture which is present in their native state, by application of
some external stress or compound such as a
• Heat,
• Strong acid or base,
• A concentrated inorganic salt,
• An organic solvent (e.g., alcohol or chJorofom1),
• Radiation.
If proteins in a living cell are denatured, this results in
disruption of cell activity and possibly cell death. Protein
denaturation is also a consequence of cell death.
Denatured proteins can exhibit a wide range of
characteristics, from conformational change and loss of
solubility to aggregation due to the exposure of
hydrophobic groups. Denatured proteins lose their 3D
structure and therefore cannot function.
Protein folding is key to whether a globular or membrane
protein can do its job correctly; it trust be folded into the right
shape to function. However, hydrogen bonds, which play a big
part in folding, are rather weak and thus easily affected which can
denature the protein.
Denaturation at levels of protein
structure:
1. In quaternary structure denaturation, protein sub-units are
dissociated and/or the spatial arrangement of protein subunits
is disrupted.
2. Tertiary structure denaturation involves the disruption of:
• Covalent interactions between amino acid side-chains (such as
disulfide bridges between cysteine groups)
• Non-covalent dipole-dipole interactions between polar amino
Acid side-chains (and the su1Touuding solvent)
• Van der Waals (induced dipole) interactions between
nonpolar amino acid side-chains.
3. In secondary structure denaturation, proteins lose all regular
Repeating patterns such as alpha-helices and beta-pleated sheets,
and adopt a rando1n coil configuration.
4. Primary structure, such as the sequence of amino acids held
Together by covalent peptide bonds, is not disrupted by
denaturation.

1 2 3 4

LEVELS OF PROTEINS
TO FIND:
• What happens when a protein denatures?
• Do all protei11 denature at the sa1ne te1nperature?
• What ten1perature does albumin denature at?
• What te1nperature does casein denature at?
• Why might protein denature at different ten1perature?

MATERIALS REQUIRED:
► Bunsen burner
► Beaker
► Glass rod
► Milk power
► Egg
► Distilled water
► Matchstick
► Then1101neter
► Tripod stand
► Wire gauge
PROCEDURE:
1. DENATURATION OF EGG PROTEIN:
• Break an egg and separate the egg yolk from the egg white. Collect
egg white in a separate beaker and yolk in separate beaker.
• Place the breaker containing egg white on the Bunsen beaker and
heat it.
• Place the the1mon1eter in the beaker. Make sure the thermometer
does not touch the botto1n of the beaker.
• Note the te1nperature when the texture of the egg white changes.

2. Denaturation OF MILK PROT.EIN:

• Prepare two cups of 1nilk using 1nilk powder. Follow the
instruction given in the packet to prepare the milk.
• Collect the prepared milk ill the beaker.
• Place the thermometer in the beaker. Make sure the thermometer
does not touch the bottom, of the beaker.
• Note the te1nperature of the milk when skims are formed over the
top or when the texture changes.
OBSERVATION:
Egg protein:
• The protein (albumin) bad changed its texture at 36 degree Celsius.
Milk protein:
• The milk protein (casein) had changed its texture at 83 degree
Celsius.

COLLECTED EGG ALBUIIN HEATING THE EGG ABLUMIN

DENATURED EGG ALBLUN MILK PREPARED USING MILK

POWDER
BOILING OF MILK DENATURED MILK
(CHECKING TUE TEMPERATURE)
RESULT:
• Through this experiment we can conclude that
• When protein denatures, denaturation disrupts the normal a-
helix and p sheets in a protein and uncoils it into a random
shape.
• All protein denatures at different temperatures, as some
proteins are known to resist very high te1nperature and do
not denature, while other denature at lower te1nperature.
• the egg protein denatures at 36 degree Celsius
• The milk protein denatures at 83 degree Celsius
Protein denatures at different temperatures because n1elting
temperature varies for different proteins, but temperatures
above 41°C (l05.8°F) will break the interactions in 1nany proteins
and denature them. Factors other than heat can also denature
protein. Changes in pH affect the chemistry of amino acid
residues and can lead to denaturation.
BIBLIOGRAPHY:
 www.biochemistry.com
 Www.milkfacts.com
 www.education.com
 www.livesience.com