Exocellular proteases of Malbranchea gypsea and their role in keratin deterioration.
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.
Singh
C J
CJ
Department of Botany, St. John's College, Agra, India.
D000818:Animals; D001673:Biodegradation, Environmental; D003470:Culture Media; D010450:Endopeptidases / Q000378:metabolism*; D007194:India; D007633:Keratins / Q000378:metabolism*; D020036:Onygenales / Q000201:enzymology* / Q000254:growth & development; D010447:Peptide Hydrolases / Q000378:metabolism; D012867:Skin / Q000378:metabolism; D012988:Soil Microbiology
D003470:Culture Media; D007633:Keratins; D010450:Endopeptidases; D010447:Peptide Hydrolases; C035855:keratinase