Abstract
Gelatin! It's hard to think of another food that is used as frequently on the dinner table as off. You can find it in all sorts of sweet foods, from ice cream, yogurt, and gummy bears, to marshmallows and yellow colorings for sodas. Off the table, it shows up in glues, photographic paper, playing cards, crepe paper, medicine capsules, hair gels, and professional lighting equipment. From the kitchen to the theater—what a range of uses! In this cooking and food science fair project, you'll investigate how to change the strength of gelatin gels. What makes a gel weak and quivery, or strong and tough? Find out how gelatin can go from blubbery to rubbery!Objective
To determine how additives—like acids, sugars, salt, and milk—affect the strength of a gel.
Introduction
Wiggly, jiggly gelatin! Of all the foods we eat, this one seems to have magical powers, suspending fruits; molding into towering, translucent sculptures; transforming from a solid into a liquid as soon as a spoonful hits the warmth of our mouths. It's not magic, but special gelatin molecules that are responsible for these food tricks. Gelatin comes from collagen, the main protein in connective tissue, which is a specialized, fibrous tissue in animals that connects other tissues together. Ligaments, for example, which connect bones to bones, or tendons, which connect muscles to bone, are both rich in collagen. Other good sources are skin, bone, fascia, and the extracellular matrix that provides structural support for many cells. Collagen is so widespread and useful that it is the most common protein in the animal kingdom (which includes humans), making up about 50 percent of the total body protein content of most animals.
Imagine that you have a single strand of hair or a piece of thread several inches long. If you pull on each end at the same time (if you create a tensile force), then you might be able to break the hair or thread. But what happens if you take three strands of hair, or three pieces of thread, and braid or roll them together first to make a small rope-like fiber before you try pulling on them? You'll find that the tiny rope is much harder to break. This is similar to what happens with collagen. A collagen molecule is made up of three chains of amino acids that are wound tightly together to form a triple helix. The collagen molecule is then further strengthened by cross-links within the triple helix (which are like the rungs on a ladder). The collagen molecules are then bundled into fibrils and the fibrils into collagen fibers which are, like rope, very strong in tensile strength and are good at supporting and connecting tissues together.
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| Figure 1. This image shows how the tensile strength of a single strand of thread can be increased by braiding it with two other strands of thread. |
If you add heat to tissues containing collagen though, the collagen fibers can be taken apart. At around 140°F, the bonds of the triple helix are broken. The collagen molecules can no longer hold their shape and they collapse. The three individual protein chains within each collagen molecule separate and disperse. These individual strands are the gelatin.
If animal tissues are cooked in water slowly over several hours, the collagen in all the connective tissues will have time to break down, and the gelatin will disperse and dissolve into the water, along with the other meat juices, forming a broth or soup stock. When the concentration of that gelatin reaches around 1 percent or more by weight in the broth, a gel can form as the hot stock cools down to around 100°F, the melting temperature of gelatin. At this temperature, the strands of gelatin will begin to return to their coiled shape that they had when they were inside the collagen. Individual coils will pair up, and then form trios, making double and triple helixes again. This reassembly of the gelatin molecules forms a network that can trap liquid, turning the broth into a solid gel. You might have seen this in action if your parents have cooked a roast and put it in the refrigerator with the juices. When it's hot, the juices were flowing. But when it cools in the refrigerator, the juices congeal and form a weak gel. At a 1 percent concentration of gelatin, the gel that forms is delicate and will break easily when handled. Around 3 percent concentration, the gel becomes firmer and more rubbery.
The strength or firmness of a gelatin gel depends upon several factors:
In this science fair project, you will investigate how common additives influence gel strength. Do acids, like lemon juice, turn your gel into a quivering, fragile blob? Does sugar stiffen your gel and make it as tough and rubbery as a bouncy ball? It's time to find out!
Terms, Concepts and Questions to Start Background Research
Bibliography
This source describes the physiologic and chemical properties of collagen:
Materials and Equipment
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Experimental Procedure
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| Figure 2. This photo show the test instrument lying on top of the mold lid, ready to be inserted into the molds. |
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| Figure 3. This photo shows the test instrument inserted into one of the molds and resting on the surface of the gelatin. The next step will be to add quarters to the cup to push the stick toward the bottom of the mold. |
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| Figure 4. This photo shows the test instrument after it has fully passed through the Popsicle mold and the cup is resting on the lid. |
Data Table: Number of Quarters Required to Cut Through Mold
| Additive to Gelatin Mold | Control (nothing added) | Acid Added (example) | Sugar Added (example) | Salt Added (example) |
| Trial 1 | ||||
| Trial 2 | ||||
| Trial 3 | ||||
| Average of trials |
Variations
Credits
Kristin Strong, Science Buddies
Last edit date: 2009-01-04 10:06:00
If you like this project, you might enjoy exploring careers in Cooking & Food Science.
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