Collagen and biogenic materials

Did you know that collagen can develop a tensile force of 100 megapascal if water is eliminated, which is 300 times as much as that of a muscle. Human as well as animal bodies above all owe their strength this fibre-forming protein, the collagen. Large amounts of it are contained in bones, tendons, ligaments or the skin. Like all proteins, collagen is composed of a complex arrangement of individual components hierarchically, too.


Like all proteins, collagen is composed of a complex arrangement of individual components hierarchically, too. Basis is the collagen molecule. Three of these chain-like proteins form a triple helix which looks like a cord. Many of these "cords" connect to form thicker "ropes" so-called collagen fibrils. With a thickness of about 100 to 500 nanometres the fibrils are, however, one hundred thousand times thinner than real ropes. In the fibrils, adjacent collagen molecules are not located flush against each other but displaced causing a staggered arrangement. This results in alternating more or less dense zones along the fibril. Many fibrils in turn are tied to collagen fibres.

Understanding the behaviour of the collagen fibres in a matrix under most different ambient conditions is the basis for utilizing it as raw material. The most common application, of course, is leather which develops through tanning of hides. In addition, collagen can also be gained and processed in a way to utilize it for applications in medical engineering, for medical and cosmetic products or for the food industry.

Already the founding fathers of our institute dealt with the raw material collagen in order to develop new leather qualities on its basis. Already at that time a high materials expertise was necessary to understand tanning processes. Today's high scientific level in collagen research at our institute can be derived from this fact. During the past years also vegetable raw material sources have been added.

In this section the following tests are frequently searched:

Moisture content

Hydroxyproline content

Volatile substances




FILK Freiberg Institute gGmbH
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09599 Freiberg


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