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Laboratory Report Presented to

Senior High School Department
St. Augustine Academy of Pampanga
Floridablanca, Pampanga

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In Partial Fulfilment of the

Requirements for the Second Quarter

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By:

Grade 11 STEM
St. Gregory the Great
Francesca Gener
Nabeel Buallay
Carl Gabriel Domingo
Rachelle Guttierez
John Michael Manalansan
_____________________

To:

Mrs. Abigael M. De Guzman

Subject Teacher

October 22, 2019

Transfer Task in General Chemistry

I. TITLE OF THE TRANSFER TASK

Denaturation of Proteins

II. PURPOSE

 The objective of this experiment is to experiment with different methods of denaturing the protein

found in egg white using ionic compounds, acids, and bases. The purpose of this experiment is to

determine the different substances that denatured egg white proteins and to understand the results

of protein denaturation and how food texture changes as a result of it.

III. BACKGROUND

According to our research, proteins are built of folded chains of compounds called amino acids.

The process that causes a protein to lose its shape is known as denaturation. Denaturation is usually

caused by external stress on the protein, such as solvents, inorganic salts, exposure to acids or bases, and

by heat. 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.

Transfer Task in General Chemistry

IV. MATERIALS AND PROCEDURES

Materials that we used:

 Egg (5)
 Lemon juice
 Table salt
 Alcohol
 Baking soda
 Hot water
 Plastic cups (6)

Procedures:

 Crack an egg over the first plastic cup and separate the yolk and white. Use two plastic cups,

keeping all the whites in one of the cups. Make sure that your yolks do not contaminate the

whites, so be careful.

 Put the whites on each (5) plastic cups.

 Then ready all the materials which will be putted on each plastic cups with an egg white.

 Put a pinch of table salt and put it in the cup and go to the next cup while waiting something to

happen.

 Next, pour the alcohol on the second cup and you’ll already see the result.

 After that, go heat some water or we must prefer that ready your hot water before you do this

experiment. Then, pour some hot water on the cup and you’ll see a visible result.

 Next, cut your lemon in between and crush the juice and put it in the cup.

 Meanwhile, grab the baking soda and put two tablespoon or one tablespoon of baking soda in the

cup and stir it very well to see some reaction or result.

 After you did all these procedures, look at your work and you will see the result.

 Also, don’t forget to clean your workplace.

Transfer Task in General Chemistry

V. RESULTS AND DISCUSSION

A. HOT WATER- Whenever eggs are cooked with heat, the egg whites turn from clear to white, and the

gel becomes more rubbery. If the heat is way too high, the proteins in the egg white form more and more

bonds, squeezing some of the water out of the protein network and making the egg white rubbery.

B. TABLE SALT- Adding salt in the egg white speeds up the process by which the egg whites solidify

and stops the seepage. The salt looks like foam after some minutes when we put the salt in the egg white.

C. BAKING POWDER- For what we know egg white and baking powder are used in baking. What we

saw is that after we mixed it the baking soda made a fluffy texture and started to rise up. A small amount

of baking soda can react in the eggs, producing bubbles baking soda.

D. LEMON JUICE- Bubbles did form around the egg shell and foam slowly built up at the surface,

however this came after an hour we did the experiment.

E. RUBBING ALCOHOL- Alcohol also denatures proteins. It does this the same way as heat, by

breaking the bonds that hold parts of the protein in a folded shape. The result is almost the same when

you add hot water on the white. But not as the rubbery one, it looks like a soft white cotton that’s been

putted on the water. The longer time for denaturation with alcohol is simply because it spreads more

slowly than heat.

Transfer Task in General Chemistry

VI. POST LAB QUESTIONS:

1. What happens when a protein denatures?

Proteins become denatured due to some sort of external stress, such as exposure to acids, bases,

inorganic salts, solvents, or heat. There are reactions from the materials that we’ve put. Structures are

altered but the peptide bonds of the primary structure between the amino acids are left intact. Essentially,

the protein becomes unfolded and ceases to function.

2. Which method appeared most dramatic denaturing effect on egg albumin? Why do you think this

method had greater effect?

Putting hot water in the egg white is the method that appeared most dramatic denaturing effect on

egg albumin. The heat from the hot water denatures the albumin protein in the liquid egg white and it

becomes insoluble.

3. Of the methods you tested, which would be more likely to be used in the food industry? And why?

The eggs and baking soda because they are used in baking some good bread that we eat every day.

Eggs contribute to the overall flavor of whatever you’re making. Eggs contribute to browning of the

bread. Eggs on the cake or bread along with the starches in flour help form the overall structure of your

baked goods.

4. Why heat and alcohol are used to disinfect medical equipment?

In medicine, a combination of ethanol or rubbing alcohol and heat can be used to sterilize medical

instruments by killing bacteria and viruses. This occurs through a process known as protein denaturation.

Alcohol is used to disinfect surgical equipment and other items which need to be made sterile before re-

use because bugs can't live in alcohol. Heat is used for the same purpose.
Transfer Task in General Chemistry

5. Why might living organisms want to keep their proteins from denaturing?

The denaturation of many proteins, such as egg white, is irreversible. A common consequence of

denaturation is loss of biological activity (e.g., loss of the catalytic ability of an enzyme). Living

organisms wants to keep their proteins from denaturing because it will loose it's biological activity

6. In this activity, why was it important to have egg whites that we did not cook or add alcohol to?

We did not cook or put alcohol with the egg whites to keep its proteins intact, because cooking or

adding alcohol will not make proteins go back to its original state, it's irreversible

VII. HYPOTHESIS

Does temperature have an effect of denaturing proteins? How do you tell if a protein is denatured?

Can protein denaturation be reversed? When the temperature is increased the hydrogen bonds and

between the protein structures begins to break causing the protein to unfold and the activation site to

become inactive. The higher the temperature the less time this will take to happen. When a protein is

denatured, secondary and tertiary structures are altered but the peptide bonds of the primary structure

between the amino acids are left intact. Since all structural levels of the protein determine its function, the

protein can no longer perform its function once it has been denatured. If the denaturing was very gentle,

when the denaturing agent is removed, the original attractions between the amino acids reshape the

protein and it can resume its function. More often, denaturation is so extreme that it cannot be reversed.

Proteins that have coagulated cannot become re-natured. Organic solvents like hand sanitizers can also

denature protein. Your hand sanitizer kills germs by denaturing the proteins in them. Would cold

temperature denature proteins? Proteins are stable only over a limited range of temperature and pressure.