Keratinases: hydrolysis of keratinous substrates by three enzymes of Trichophyton mentagrophytes
Yu, R.J.; Ragot, J.; Blank, F.
Experientia 28(12): 1512-1513
1972
ISSN/ISBN: 0014-4754 PMID: 4654231 Document Number: 51692
Results showed that all 3 keratinases are most active with guinea-pig hair as substrate, keratinase III digests horse and rabbit hair and keratinase I rat hair, but less effectively. All 3 hydrolyse powdered hair more rapidly than cut hair because the former provides greater surface area of medulla and cortex. When human keratins were used as substrates, callus was readily hydrolyzed by all 3 whereas nails were only moderately digested. Hair from children and adults was rather resistant. The results could indicate that keratinases from zoophilic dermatophytes have a stronger effect on animal than on human keratins and that the highly developed host-parasite relationship of the dermatophytes could well be explained by the substrate specificity of their keratinases.