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American Chemical Society's Weekly Press Pac


Jay Heinecke, M.D.
University of Washington
Seattle, Washington 98195
Phone: 206-543-3158

ARTICLE #3 EMBARGOED FOR: Wednesday, Aug. 22, 5:30 p.m., Eastern Time

Hoofing it toward a safer source of collagen

Scientists are reporting an advance toward turning corn plants into natural factories for producing collagen, a protein widely used in food, medical and other products. The advance may lead to a safe, inexpensive source of the protein for manufacturers who now rely on material obtained from slaughterhouse waste, according to researchers.

Collagen is a component of skin, tendon, bone, cartilage and connective tissue of humans and other animals. Gelatin derived from collagen is a jelly-like substance used in a wide array of food products, ranging from ice cream and gelatin desserts to vitamin capsules, cosmetics and absorbable surgical sponges. To get the collagen, manufactures process the bones, hooves and tissues of cows and pigs that have been slaughtered for meat.

Responding to concern about the possible presence of infectious agents in animal by-products, scientists have been working on ways to produce human collagen from transgenic plants. These genetically engineered plants have the human gene that produces collagen. However, finding ways to recover and purify the protein, which is produced only in very low levels in plants, has remained a challenge.

Now, Charles Glatz and colleagues say they have developed a better process to harvest human collagen from transgenic corn. The method uses a three-step filtration system to separate the collagen from other corn proteins and maximize yields. Recent tests show the new purification method yields five to 10 times more collagen from corn than previous extraction methods, Glatz says.


Contact: Michael Woods
American Chemical Society

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