• Kumar, Anupam

Abstract

Alkaline proteases hold a great potential for application in the food, detergent and leather industries due to the increasing trend to develop environmental friendly technologies. In this study, an attempt is made to isolate and characterise the bacteria from the protein rich soil sample as well as to optimise the culture conditions for the production of protease enzyme. The molecular sequencing of the bacterium and the phylogenetic tree formulated revealed the presence of Serratia marcescens. In the subsequent phase effect of temperature, pH, activator and inhibitor was also studied on the activity of protease enzyme by using casein and hair as substrates. The enzyme further was shown to have the ability to remove the blood from the blood stained surgical instruments as well as to recover silver from the X ray film. The optimum production of protease by Serratia marcescens was observed at pH 10 and temperature 37°C. The presence of CaCl2 (activator) increased the enzyme activity and the presence of HgCl2 (inhibitor) reduced the protease activity. The protease enzyme was able to act on casein and hair as well as able to remove the blood from the surgical instruments. Treatment of X-Ray films with protease resulted in the silver bound with gelatin being stripped off in to the reaction mixture at pH 10 and temperature 40oC. The alkaline protease enzyme obtained in the present study by using Serratia marcescens is found to be stable and active in alkaline condition, so could be of significant use for detergent and leather processing technology as well as for dehairing and silver recovery.

Topics

• impedance spectroscopy
• silver
• phase