Enhanced production of protease from Bacillus subtilis AP-CMST W3 and its application in leather processing and silver recovery

In the present study, Bacillus subtilis AP-CMST W3 was isolated from an estuarine environment for the production of protease for various biotechnological applications. The process parameters were optimized to enhance the production of protease by the candidate organism. Protease production was found to be optimum in the presence of 0.5% maltose, 0.5% casein, 0.1% magnesium chloride, 3% sodium chloride, at pH 7.0 and 40 °C. The enzyme was purified by the combination of ammonium sulphate precipitation, dialysis and sephadex G-75 gel filtration chromatography. The molecular weight of the purified enzyme was estimated as 21 kDa. The purified enzyme demonstrated appreciable activity at higher temperature (40 °C) and pH 7.0. The enzyme showed potent activity on various surfactants and detergents. It dehaired goat skin and hydrolyzed the gelatine layer of used “X” ray film. These properties reinforce the possibility of inclusion of protease from B. subtilis AP-CMST W3 in leather processing industry.