Extracellular protease expression in Microsporum gypseum complex, its regulation and keratinolytic potential

Abstract

Two soil isolates of Microsporum gypseum were studied for the production of extracellular proteases. Both the strains secreted protease on glucose-gelatin medium. The enzyme activity peaked on day 15 at 28°C. Asparagine repressed protease yield. Sugars caused catabolite repression of protease formation. Protease activities of both the isolates were significantly affected by incubation period, culture media and carbohydrates used. Both the strains grew on the skin bait and caused a gravimetrically measurable loss of the substrate. Despite less pronounced differences in the keratinase levels, great variations occured in the amount of keratin degraded by two isolates. Keratinase production as well as loss in substrate mass was better in glucose-lacking flasks than those containing the sugar. Although the rate of keratin degradation was independent of enzyme production, statistically positive correlations were recorded between loss in substrate mass: yielded dry mycelial weight and substrate degradation: keratinase levels.

Chemoselective fluorination and chemoinformatic analysis of griseofulvin: Natural vs fluorinated fungal metabolites

“…55, 56 As shown in Tables 2 and S15, compound 10 retained the activity of 1 , while 7 showed a slight decrease in activity. Compound 10 has previously been reported to retain the activity of 1 against the plant pathogen Botrytis alii , 35 but its activity against dermatophytes, particularly M. gypseum , has not been reported.…”

Optimization of Conditions for Feather Waste Biodegradation by Geophilic Trichophyton ajelloi Fungal Strains towards Further Agricultural Use

“…This was demonstrated by Mini, et al [ 53 ] and Anbu, et al [ 54 ] in cultures of Aspergillus flavus and Scopulariopsis brevicaulis strains, who reported a decrease in keratinase activity in the presence of glucose and xylose, respectively. Anbu, et al [ 54 ] and Singh [ 55 ] explained this effect by the catabolic repression of proteolytic enzymes by exogenous carbohydrates. Anbu, et al [ 56 ] reported the accumulation of organic sulfur-containing end products as another reason for the inhibition of keratinase activity in fungal cultures.…”

Keratinolytic Properties of Aspergillus clavatus Promising for Biodegradation

“…This fact is obviously associated with a better investigation of these organisms as objects of scientific research and biotechnological processes in comparison with fungal models, although filamentous fungi are also capable of secreting hydrolases that destroy keratin [ 21 ]. Most of the accumulated knowledge about fungal keratinases relates to enzymes synthesized by dermatophytes [ 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 ], while data on keratinolytic enzymes of micromycetes that do not cause dermatophytosis remain scarce [ 9 , 21 ].…”