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.
journal_name
Mycopathologiajournal_title
Mycopathologiaauthors
Singh CJdoi
10.1023/a:1006968600404keywords:
subject
Has Abstractpub_date
1998-01-01 00:00:00pages
147-50issue
3eissn
0301-486Xissn
1573-0832journal_volume
143pub_type
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