Acid-Base Properties of Amino Acids
Denaturing and Precipitating Proteins
Enzymatic Activity of Glucose Oxidase
HIV-1 Protease: An Enzyme at Work
Studying Enzyme Kinetics Using Catalase
Binding of Coomassie Brilliant Blue to Egg Albumin
Breaking Down Sucrose Using Invertase
Color Reactions of Amino Acids
Effect of pH on Protein Solubility
Enzyme Catalyzed Decomposition of Hydrogen Peroxide
Enzyme Kinetics: Experiments With Catalase
Halting the Briggs-Rauscher Reaction
Hydrolysis of Wool in Strong Base
What Color is Egg White
Description: Riboflavin fluorescence in egg white is quenched because it is bound to a riboflavin binding protein. The excess protein can be titrated with free riboflavin to a fluorescent end-point. If the protein is denatured, the solution becomes fluorescent.
Source: Journal of Chemical Education – Vol. 65
Year: 1988 Vol: 65 Page: 184
Keywords: Riboflavin, Egg white. Proteins, Fluorescence, Titration, UV Light
Rating: 
Hazard: Low
- Use of UV light
- No toxic reagents in use
Effectiveness: Good
- Results are clearly observable without guidance
- Somewhat connected to course material
- Clear contrast between systems behavior
- Time to results is medium
Difficulty: Medium
- Procedures with some intermediate steps to result
- Some concerted or timed manipulation
- Volume-dependent addition/ titration
- Use of scientific equipment
Safety Precautions:
- Eye protection required
- Gloves recommended
- Use of UL approved three-prong plug and outlet
- Absorbent material on hand
Class: Biochemistry, Titrations
Division: General, Biological Chemistry
Return to Biological Chemistry Demonstrations