CHARACTERIZATION OF AN EXTRACELLULAR KERATINASE OF TRICHOPHYTON SIMIIAND ITS ROLE IN KERATIN DEGRADATION

The ability of Trichophyton simii HN 50, isolated from the Ghana Bird Sanctuary, Bharatpur, India, to produce extracellular keratinase was s tudied. Enzyme was produced on a keratin salt broth medium at pH7 and a temperature of 28 +/- 1 degrees C. Enzyme secretion was best at 15 d ays of incubation. Asparagine and keratin were repressive to enzyme yi eld in comparison to gelatin. No relationship was observed between enz yme release and biomass. Exogenous sugars suppressed keratinase produc tion in descending order as follows: glucose > mannose > maltose > ara binose > fructose. The enzyme showed ability to degrade all of the 3 k eratin substrates. Buffalow skin was best degraded in the absence of g lucose while chicken feathers were the least degraded in its presence.