Abstract
A total of sixty-four bacterial isolates producing enzyme protease were isolated and screened from soil samples obtained from industries. A new potent solvent stable and alkaline protease producing isolate PI-C4 was isolated from Ghazipur Poultry waste site which was identified to be Bacillus cereus based on 16S rDNA sequence analysis. Consensus sequence of 1398 bp of the strain PI-C4 has been deposited in GenBank with accession number KM211501. Furthermore, the PI-C4 enzyme was subjected to precipitation using ammonium sulphate (70% saturation), dialysis and was further concentrated by ion exchange chromatography which resulted in purification fold of 2.47 and 57.7% yield. The alkaline protease was found to be 46 kDa. Enzyme PI-C4 was also characterized with respect to temperature and pH and was found to be active at pH 9.0 and 450C. The protease possesses significant stability (64.7-82.2%) in the presence of surfactants tested. The alkaline protease possesses higher stability in solvent DMSO (107%) followed by acetone (91%) and isopropanol (82%). The protease could therefore be useful for various applications like enzymatic leather treatment, feather degradation and recovery of silver.
Highlights
The proteases (EC 3:4, 11-19, 20-24, 99) are hydrolytic enzymes performing the role of catalyzing the peptide bonds and are found to be vital component of all life forms available on earth (Polgar, 1989)
The present study includes the isolation of protease producing strain C4 from poultry waste site and its identification as Bacillus cereus Proteolytics Index (PI)-C4 secreting a solvent tolerant alkaline protease
The isolate PI-C4 possessed maximum zone of hydrolysis seen on skim milk agar plates, confirming it to be significant protease producing isolate
Summary
The proteases (EC 3:4, 11-19, 20-24, 99) are hydrolytic enzymes performing the role of catalyzing the peptide bonds and are found to be vital component of all life forms available on earth (Polgar, 1989). Protease enzymes possess immense importance because of their much needed remarkable enzyme stability and activity at higher temperature and pH. Bacillus strains have the potential to secret higher level of enzyme proteases possessing significant proteolysis activity and wider range of stability (Kuberan et al, 2010; Ghasemi et al, 2011). As there is increase in demand and potential usefulness of Bacillus proteases for various applications, detailed screening needs to be carried out in samples collected from industries to get new sources of proteases with novel properties. The present study includes the isolation of protease producing strain C4 from poultry waste site and its identification as Bacillus cereus PI-C4 secreting a solvent tolerant alkaline protease. This study involves purification of the alkaline Bacillus protease and its characterization
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