Characterization of Crude Protease Produced by Pleurotus Eryngii ATCC 90888.
Abstract
In this study, research was carried out to characterize protease produced by Pleurotus eryngii ATCC 90888. Maximum protease production was noted at 22 °C, pH was adjusted to 6.5 after 96 hours. Sucrose and casein were used as carbon and nitrogen sources. Protease activity was characterized in terms of reaction time, enzyme and substrate concentration, pH, temperature, stability of enzyme (pH & temperature), activator and the inhibitors. Proteases produced by Pleurotus eryngii shown highest activity when 0.5 mL and 1.5% enzyme volume and substrate concentration respectively were used and reaction was incubated for 60 min. However, protease was active at 60 °C and pH 8, but enzyme was found to be stable at about 80 °C. Enzyme was also activated with divalent metal ions as well as with sulphur group (Cysteine, Mercaptoethanol).
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