Purification and sequence identification of alkaline protease produced from Bacillus subtilis KHS-1 (MTCC No. 10110)
Journal Title: Journal of Pharmacy Research - Year 2011, Vol 4, Issue 9
Abstract
The protease from Bacillus subtilis KHS-1 was purified to homogeneity by two step procedure involving ammonium sulfate precipitation and sephadex G-200 gel permeation chromatography. The molecular mass was determined approximately as 26.3 kDa by SDS PAGE and 2D gel electrophoresis and activity staining of the protease by casein zymography. Molecular mass was also determined by MALDI TOF-TOF that approximately corresponds to the mass determined by SDS PAGE and amino acid sequence of the protease was obtained by tandem mass spectrometry (MS/MS). The observed and predicted amino acid sequence of KHS-1 shows homology with the serine proteases of BSn5 from Bacillus subtilis, s t r .168 f rom B.subtilis, BPN from Bacillus amyloliquefaciens, BAJ from Bacillus sp. (41479) and ADK f rom Bacillus sp. ( 1 1 0 4 3 ) .
Authors and Affiliations
D. P. N. Rama Krishna * , N. Gopi Reddy, S. V. Raja Gopal
Keywords
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