| THE CASE OF THE MISSING YOLK |
PROBLEM:
Grandma calls one night. She was making your favorite lemon meringue pie when she realized the meringue was not as fluffy as usual. Knowing your background as a food chemist, grandma wants to know if you can figure out why her meringue is flat.
BACKGROUND INFORMATION:
Any foam (shaving cream, Dream Whip®, or Silly String®) can be identified as a two phase-colloidal dispersion in which the gas phase (nitrogen or air) is dispersed and enrobed by a thin film of foaming (surface active) agent, in a liquid phase. For a protein to be a successful foaming agent, it must be able to stabilize the new surface area that is continuously created during the making of foam. Therefore, the physical properties of proteins will play a major role in the production and performance of foam.
Egg white has been successful as the major foaming protein used in the food industry. The industry uses egg white as a functional ingredient in food products that require foams in several products including cakes, soufflés, meringues, candy and other suitable products that require air bubble incorporation. The success is due to the capacity of egg whites to form uniform foams of good volume while ensuring foam stability in the presence of other compounds and also upon heating. This reflects the unique combination of proteins with different physical properties that occur in egg whites.
The egg white foams have large interfacial foam areas, and this makes them unstable. The foam can break apart by 1) leakage of liquid phase due to pressure differences, 2) air coalescence from small to large bubbles and 3) rupture of liquid phase separating air bubbles. Low interfacial tension, high viscosity of liquid phase and strong elastic film of absorbed protein will stabilize the foams.
Several factors, in addition to the protein, affect the foaming properties of proteins. These include protein concentration, pH, temperature, salt, sugars and lipids.
During drying of egg white, the minute quantities of lipids (approximately 0.1%) from contaminating egg yolk, if present, can interfere with the conformation of adsorbed protein films by placing themselves at the air/water interface thus reducing the foaming ability of egg white.
OBJECTIVE:
MATERIALS:
SAFETY AND DISPOSAL:
There are no real safety issues or concerns regarding this lab, except do not put raw egg in your mouth. There is a remote possibility of Salmonella contamination in raw eggs. Wash hands thoroughly after finishing the lab.
TIME:
Approximately one hour.
PROCEDURES:
Foam Density = Weight of foam ÷ Volume of foam
% Change in Volume = (
Wt. of 100 ml protein - Wt. of 100 ml of foam) x 100
% Change in Volume = (
Wt. of 100 ml of foam
EXTENSION:
Foam Stability Determination: Determine the weight of the remaining foam and place it on cheesecloth in a large funnel at room temperature. Collect the liquid (drip) into a 100-ml pre-weighed beaker and note the weight of the egg white drip plus beaker at 10-minute intervals for 60 minutes. Plot the weight of egg white drip against time. Estimate the time taken for 50% of the foam to drip from this plot.
Stability Index = Time to attain 50% (w/w) drainage
| Time | 0 min. | 10 min. | 20 min. | 30 min. | 40 min. | 50 min. | 60 min. |
| Weight of drip |
Plot the weight of egg white drip (Y axis) against time (X axis)
C. Sucrose Addition and Meringue Preparation
1) The egg white (80 g) is whipped at setting 10 for 2min, the speed is
decreased to setting 6 and sucrose (45 grams) added in three increments at four
second intervals. The whipping is continued at setting 10 for 6min. The
stability index of meringue is determined as described under foam stability
determination. Sucrose is a soluble polar compound, which increases bulk
viscosity of egg white liquid, thereby improving foam stability.
| Time | 0 min. | 10 min. | 20 min. | 30 min. | 40 min. | 50 min. | 60 min. |
| Weight of drip |
Plot the weight of egg white drip (Y axis) against time (X axis)
QUESTIONS:
FOR ADDITIONAL INFORMATION CONTACT:
Dr. Navam Hettiarachchy
REFERENCES:
Altschull, A.M. and H.L. Wilcke. 1985. New Food Proteins. Vol. 5. Academic press Inc., New
York, NY. p. 155-161.
Fennema, O.R. 1985, 2 nd ed. Food Chemistry. Marcel Dekker Inc., New York, NY.
Chapters 5 and 14. pps 246-369 and 829-855.
Halling, J.H. 1981. Protein-stabilized foams and emulsions. CRC Critical Review in Food Science
and Nutrition. pps 155-203.
Hettiarachchy, N.S. and G.R. Ziegler (Eds.) 1994. Protein Functionality in Food Systems. IFT
Basic Symposium Series, Marcel Dekker Inc., New York. Chapter 6, p. 181-208.
Johnson, J.M. and M.E. Zabik. 1981. Egg Albumin Protein Interactions in an Angel Food Cake
System. J. Food Sci. 46:1231-1222, 1236.
Poole, S., S. West and C.L. Walters. 1984. Protein-protein Interactions: Their Importance in the
Foaming of Heterogeneous Protein Systems. J. Sci. Food Agric. 35: 701-711.