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Exocellular proteases of Malbranchea gypsea and their role in keratin deterioration
1Department of Botany, St. John's College, Agra, India.
Abstract:
Malbranchea gypsea IMI 338,168 isolated from the soils of Keoladeo National Park, Bharatpur was studied for its ability to produce exocellular proteases on glucose-gelatin medium at pH 7; 28 degrees C. The fungus was observed to be a potent producer of such enzymes. Protease production was optimal at 15 days of incubation. Asparagine was repressive to protease expression. No relationship existed between the amount of enzyme production and increase in biomass. Exogenous sugars suppressed enzyme production in descending order as follows: glucose > mannose > maltose > arabinose > fructose. The enzymes expressed showed the ability to degrade three keratinous substrates tested. Buffalo skin was the most actively degraded substrate when exogenous glucose was present, and was also the most resistant to degradation in the absence of glucose. The rate of keratin deterioration was independent of enzyme activity. Production of protease enzymes especially keratinases is ecologically important in a place like a National Park because such enzymes degrade keratinous detritus derived from mammals and birds. Accumulation of such materials can be a cause of pollution and can provide a breeding spot for various types of pathogens.
Insights
Malbranchea gypsea, a soil fungus from Keoladeo National Park, produces potent proteases. These enzymes effectively degrade keratinous materials, which is ecologically significant for waste decomposition in the park.
Area of Science:
- Environmental microbiology
- Fungal enzyme technology
Background:
- Keoladeo National Park harbors diverse microbial communities.
- Understanding enzyme production by soil fungi is crucial for ecological processes.
Purpose of the Study:
- To investigate the protease production capabilities of Malbranchea gypsea.
- To assess the keratin degradation potential of the produced enzymes.
Main Methods:
- Culturing Malbranchea gypsea on glucose-gelatin medium.
- Optimizing protease production conditions (pH, temperature, incubation time).
- Testing enzyme activity on various keratinous substrates.
Main Results:
- Malbranchea gypsea is a potent exocellular protease producer, with optimal production at 15 days.
- Protease production was repressed by asparagine and suppressed by exogenous sugars (glucose being most repressive).
- The enzymes degraded buffalo skin, with glucose enhancing degradation, and showed ecological importance in keratinous waste decomposition.
Conclusions:
- Malbranchea gypsea efficiently produces proteases, including keratinases.
- Enzyme production is influenced by nutrient availability and environmental factors.
- These fungal enzymes play a vital role in the natural decomposition of keratinous materials in national park ecosystems.