Please use this identifier to cite or link to this item: http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/5159
Title: PURIFICATION AND CHARACTERIZATION OF AN EXTREME HALOTHERMOPHILIC PROTEASE FROM A HALOPHILIC BACTERIUM CHROMOHALOBACTER SP TVSP101
Authors: Vidyasagar, M
Prakash, S
Mahajan, V
Shouche, YS
Sreeramulu, K
Keywords: Chromohalobacter sp TVSP101
halothermophilic protease
purification
organic solvents
osmolytes
Issue Date: 2009
Publisher: SPRINGER
Citation: BRAZILIAN JOURNAL OF MICROBIOLOGY , Vol. 40 , 1 , p. 12 - 19
Abstract: 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 effective osmolytes, retained 100% activity in the absence of NaCl. The activity was completely inhibited by ZnCl2 (2 mM), 0.1% SDS and PMSF (1mM). The enzyme was not inhibited by 1mM of pepstatin, EDTA and PCMB. The protease was active and retained 100% it activity in 10% (v/v) DMSO, DMF, ethanol and acetone.
URI: 10.1590/S1517-83822009000100002
http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/5159
Appears in Collections:1. Journal Articles

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