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PURIFICATION AND CHARACTERIZATION OF NOVEL SOLVENT STABLE BACILLUS CEREUS PI-C4 PROTEASE FROM POULTRY WASTE.
- Source :
- Journal of Microbiology, Biotechnology & Food Sciences; Apr/May2020, Vol. 9 Issue 5, p865-869, 5p
- Publication Year :
- 2020
-
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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 13385178
- Volume :
- 9
- Issue :
- 5
- Database :
- Complementary Index
- Journal :
- Journal of Microbiology, Biotechnology & Food Sciences
- Publication Type :
- Academic Journal
- Accession number :
- 142733005
- Full Text :
- https://doi.org/10.15414/jmbfs.2020.9.5.865-869