Members: Date performed: July 22, 2019

Alvaran, Angelou France Date submitted: July 24, 2019

Costelo, Chezka
Fernandez, Dan Floyd

Laboratory Report #5 “Protein Solubility and pH”

Introduction:
Protein is a macronutrient that is essential to building muscle mass. Chemically, protein is
composed of amino acids, which are organic compounds made of carbon, hydrogen, nitrogen,
oxygen or sulfur. At the surfaces of proteins are amino acid residues that interact with water. The
surface of a protein has a net charge that depends on the number and identities of the charged
amino acids, and on pH. At a specific pH the positive and negative charges will balance and the
net charge will be zero. This pH is called the isoelectric point, and for most proteins it occurs in
the pH range of 5.5 to 8.

Objective: To study the effect of pH on the solubility of proteins

Methodology:

The following laboratory apparatuses were used during the experiment:

 Test Tubes
 Graduated Cylinder
 Glass Tubing
 Test Tube Rack
 Test Tube Brush

Procedure:

We placed 3 ml portions of albumin solution in four separate test tubes. To the first, we
added 3 ml distilled water; to the second, 3 ml of NaOH solution; to the third, 3 ml of Na 2CO3;
and to the fourth, 3 ml of HCl. Then, we observed the appearance of each mixture and compared
their degrees of turbidity with the original albumin solution.

Results:

For the 3 ml of albumin solution added with 3 ml distilled water, the solution appeared to
be the haziest; indicating having the highest turbidity among the four solutions.
 For the 3 ml albumin solution added with 3 ml of NaOH, it appeared to be the clearest or
unclouded; indicating having the lowest turbidity among the other solutions.

For the 3 ml albumin solution added with 3 ml of Na2CO3, the solution appeared to be
less clear than the second solution.

For the 3 ml albumin solution added with 3 ml of HCl, the solution appeared less hazy or
cloudy compared to the first solution.

Discussion:

Conclusion:

A protein has its lowest solubility at its isoelectric point. If there is a charge at the protein
surface, the protein prefers to interact with water, rather than with other protein molecules. This
charge makes it more soluble. Without a net charge, protein-protein interactions and precipitation
are more likely.

Documentation:

From left to right, albumin with distilled water, albumin with NaOH,
albumin with Na2CO3, albumin with HCl
References:

What Is Protein?. (2015, December 10). Retrieved from https://www.livescience.com/53044-

protein.html

Protein Solubility. (n.d.) Retrieved from http://www.chemistryexplained.com/Pr-Ro/Protein-

Solubility.html