Studies on the Microbiological Degradation of Wool
1950
Stahl, William H. | McQue, Bernard | Mandels, Gabriel R. | Siu, R.G.H.
Measurements of the susceptibility of various keratins and fibrillar proteins to digestion by a keratinolytic fungus were made. Both normal and modified proteins were used. Digestion of the following fibrillar proteins by Microsporum gypseum over a 21-day period was, from the highest percentage digestion to the lowest: collagen, feather, hoof, wool, horn, horsehair, mohair, and silk. The primary factors which determine the rate of digestion of fibrillar proteins were found to be the chemical composition and the molecular architecture. In keratins, the degree of poly merization assumes the greatest importance. The higher the degree of polymerization, pri marily attributed to the disulfide cross-linkages, the more resistant the keratin is to enzymic digestion. Histological complexity of keratinaceous tissues and geometrical structure of the keratin molecule do not influence the rate significantly.
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