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Republic of the Philippines UNIVERSITY MISSION

UNIVERSITY VISION CAVITE STATE UNIVERSITY  


“Cavite State University shall provide
Biga 1, Silang, Cavite excellent, equitable and relevant
The premier University in
historic Cavite recognized for 046 513-5706/046 513-3965 educational opportunities in the arts,
excellence in the development science and technology through
of globally competitive and ✉ cvsusilang@cvsu.edu.ph quality instruction and responsive
morally upright individuals. research and development activities. It
shall produce professional, skilled and
morally upright individuals for global
competitiveness.”
DEPARTMENT OF ARTS AND SCIENCES
SECOND SEMESTER 2022-2023

CHBH13: BIOCHEMISTRY FOR HEALTH SCIENCES


LABORATORY WORKSHEET 3
Denaturing Proteins

Name: __________________________________________ Group No.: ____________


Course and Section: _________________________ Date: _______________

INTRODUCTION

Proteins are large molecules made up of small amino acids. Common proteins used in cooking are albumen
and casein; eggs are mostly albumen; and milk is largely casein. Proteins are held in a natural shape due to the
interaction of side groups on the amino acids from one part of the molecule to another area of the molecule. These
interactions may be hydrogen bonds or disulfide bonds.

Denaturation is a process in which proteins lose their structure when attacked by forces like a strong acid,
heat, or a solvent like alcohol. We can denature the proteins by disrupting the hydrogen bonds that are within the
structure. When this happens, the overall shape of the protein changes, and new properties can be observed. The
shape of a protein is associated with food processing properties, such as solubility, gel formation, and enzyme activity.

Denaturation in the egg whites will change the albumin from clear to white. We will explore how the following
denatures egg albumen as well as milk casein.

 Heat (thermal) – done by cooking


 Acids & bases – can form ions on
some side groups of amino acids
 Organic compounds – form their
own hydrogen bonds with the
amino acids
OBJECTIVES

At the end of this activity, you will be able to:


 explore what protein denaturation is,
 perform the different methods of denaturing the protein found in egg white (albumen) and milk (casein),
 recognize the chemical and physical causes of protein denaturation.

MATERIALS
• mixing bowls • 1 to 2 teaspoons of baking powder (NaHCO 3)
• teaspoon • 2 kalamansi
• whisk/fork • 3 teaspoons of milk
• cups • hand soap
• 1 to 2 eggs • hand towels/paper towels
• 1 to 2 teaspoons of table salt (NaCl)

PROCEDURE: Follow the succeeding instructions. Observe and complete the data to show the results.

I. Denaturation by Ionic Compound: NaCl (table salt)

1. Crack an egg and separate the egg yolk and the egg white. Keep all the egg
white in a bowl. Make sure that the egg yolk does not contaminate the egg
white.
2. Take 2 teaspoons of egg white from the bowl and put it on a cup. Add
approximately 1 teaspoon (~ 15 grams) of NaCl to the cup containing an egg
white and stir thoroughly.
3. Keep adding the NaCl until you notice a change in the egg white. Take picture
1.
4. Record your observation in the Egg Albumen Data Table

II. Denaturation by Base: NaHCO3 (Sodium Bicarbonate or Baking Soda)

1. Place 1 teaspoon of egg whites in a cup from the egg white bowl.
2. Add approximately 1 teaspoon NaHCO3 to the cup containing an egg white and stir thoroughly.

5. Keep adding ½ teaspoon of NaHCO3 at a time until you notice a change in the egg white. Take picture 2.
3. Record your observation in the Egg Albumin Data Table.

III. Denaturation by Acid: Citric Acid (Kalamansi Juice)

1. Place 1 teaspoon of egg whites in a cup from the egg white bowl.
2. Add approximately 1 teaspoon (~5 ml) kalamansi juice to the cup containing an egg white and stir.
3. Keep adding the kalamansi juice a ½ teaspoon at a time until you notice a change in the egg white. Take picture 3.
4. Record your observation in the Egg Albumin Data Tabl
IV. Procedure for Milk (Casein) Denaturation:

1. Place 3 teaspoons (~15 ml) of milk into a cup.


2. Add approximately 1 teaspoon (5ml) of kalamansi juice in the
cup containing the milk and stir.
3. Keep adding the kalamansi juice a ½ teaspoon at a time until
you notice a change in the milk. Take picture 4.
4. Record Observations on the Milk Table.

RESULTS AND OBSERVATIONS

I. Paste the pictures taken during the experiment in the boxes below. (20pts)

Picture 1 Picture 2

Picture 3 Picture 4
II. Record your observations in the table below. (20 pts)

TABLE 1: EGG ALBUMEN DATA

ADDED OBSERVATIONS

NaCl – Ionic Compound

NaHCO3 – Base

Lemon Juice – Acid

TABLE 2: MILK CASEIN DATA

ADDED OBSERVATIONS

Lemon Juice – Acid

DISCUSSION QUESTIONS:

1. What happens when a protein denatures? (2 pts)

2. What does denature mean and why does a denatured protein no longer function normally? (3 pts)        

3. Which method appeared to have the most dramatic denaturing effect on egg albumen? Why do you think this
method had a greater effect? (5 pts)

4. Among the methods you tested, which would be more likely to be used in the food industry? Explain your answer.
(5 pts)

5. Drugs that are proteins, such as insulin, must always be injected rather than taken by mouth. Explain why. (5 pts)

CONCLUSION: (10pts)

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