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Purification and characterization of an extreme halothermophilic protease from a halophilic bacterium Chromohalobacter sp. TVSP101 BJM
Vidyasagar,Malashetty; Prakash,S.; Mahajan,Vineet; Shouche,Yogesh S.; Sreeramulu,K..
An extreme halophilic bacterium was isolated from solar saltern samples and identified based on biochemical tests and 16S r RNA sequencing as Chromohalobacter sp. strain TVSP101. The halophilic protease was purified using ultrafiltration, ethanol precipitation, hydrophobic interaction column chromatography and gel permeation chromatography to 180 fold with 22% yield. The molecular mass of the protease determined by SDS PAGE was 66 kDa. The purified enzyme was salt dependent for its activity and stability with an optimum of 4.5 M NaCl. The optimum temperature for maximum protease activity was 75°C. The protease was optimally active at pH 8 and retained more than 80% of its activity in the range of pH 7-10. Sucrose and glycine at 10% (w/v) were the most...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Chromohalobacter sp. TVSP101; Halothermophilic protease; Purification; Organic solvents; Osmolytes.
Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822009000100002
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