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Extracellular protease expression in Microsporum gypseum complex, its regulation and keratinolytic potential
1Department of Botany, Shri Chitragupta PG College, Mainpuri, India. singhcj1@rediffmail.com
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 occurred 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.
Insights
This study investigated Microsporum gypseum protease and keratinase production. Glucose-lacking conditions enhanced keratin degradation, highlighting optimal enzyme activity for dermatophyte research.
Area of Science:
- Mycology
- Enzymology
- Biochemistry
Background:
- Microsporum gypseum is a dermatophyte known to degrade keratin.
- Extracellular proteases and keratinases are key enzymes involved in dermatophyte pathogenesis.
- Understanding the factors influencing enzyme production is crucial for antifungal research.
Purpose of the Study:
- To investigate the production of extracellular proteases and keratinases by two soil isolates of Microsporum gypseum.
- To determine the effects of culture conditions, carbohydrates, and amino acids on enzyme yield.
- To assess the correlation between enzyme activity and keratin degradation capacity.
Main Methods:
- Culturing Microsporum gypseum isolates on glucose-gelatin medium.
- Measuring protease and keratinase activity over 15 days at 28°C.
- Assessing keratin degradation using skin bait and gravimetric analysis.
- Analyzing the impact of asparagine and various carbohydrates on enzyme production.
Main Results:
- Both isolates produced extracellular proteases, with peak activity on day 15 at 28°C.
- Asparagine repressed protease yield, and sugars induced catabolite repression.
- Significant variations in keratin degradation were observed between isolates, despite similar keratinase levels.
- Keratinase production and substrate mass loss were higher in glucose-lacking media.
- Positive correlations were found between substrate mass loss, dry mycelial weight, and keratin degradation with keratinase levels.
Conclusions:
- Protease and keratinase production by Microsporum gypseum are influenced by nutritional factors and incubation conditions.
- Absence of glucose favors enhanced keratin degradation, suggesting specific metabolic pathways.
- Variations in keratinolytic activity among isolates warrant further investigation for understanding dermatophytosis.
- The study provides insights into optimizing enzyme production for potential biotechnological or therapeutic applications.
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