| Registro completo |
| Provedor de dados: |
BJM
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| País: |
Brazil
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| Título: |
Purification and characterization of an extreme halothermophilic protease from a halophilic bacterium Chromohalobacter sp. TVSP101
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| Autores: |
Vidyasagar,Malashetty
Prakash,S.
Mahajan,Vineet
Shouche,Yogesh S.
Sreeramulu,K.
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| Data: |
2009-03-01
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| Ano: |
2009
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| Palavras-chave: |
Chromohalobacter sp. TVSP101
Halothermophilic protease
Purification
Organic solvents
Osmolytes
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| Resumo: |
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.
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| Tipo: |
Info:eu-repo/semantics/article
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822009000100002
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| Editor: |
Sociedade Brasileira de Microbiologia
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| Relação: |
10.1590/S1517-83822009000100002
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| Formato: |
text/html
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| Fonte: |
Brazilian Journal of Microbiology v.40 n.1 2009
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| Direitos: |
info:eu-repo/semantics/openAccess
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