Optimization of Extracellular Alkaline Protease Enzyme from Bacillus Sp

Proteases are very important industrial enzymes, which contribute about 60% of the total world enzyme market. Among the various proteases, bacterial proteases are the most significant, compared with animal and fungal proteases (Rahman et al., 1994) and among bacteria, Bacillus sp are specific producers of extra-cellular proteases (Coolbear et al., 1992; Banerjee et al., 1999). These enzymes have wide industrial application, including pharmaceutical industry, leather industry, manufacture of protein hydrolizates, food industry and waste process in industry (Pastor et al., 2001). Thermostable proteases are advantageous in some applications because higher processing temperatures can be employed, resulting in faster reaction rates, increase in the solubility of non gaseous reactants and products, and reduced incidence of microbial contamination by mesophilic organisms. Enzymes from extreme thermophiles are not only stable at high temperature, but also to organic solvents, detergents and charotropic agents. This opens up the possibility of using enzymes in the presence of denaturing substrates or products, and in stringent conditions generally (Coolbear et al., 1992; Beg and Gupta 2003). Proteases secreted from thermophilic bacteria are thus of particular interest and have become increasingly useful in a range of commercial applications (Singh et al., 2001; Adams and Kelly 1998). The present investigation describes the isolation and selection of thermophilic bacteria capable of producing extracellular alkaline protease and the effect of different sources of protein on the production of protease.