Data/hora: 06/06/2024 11:27:09

Provedor de dados: | 58
País: | Brazil
Título: | Purification and characterization of an extreme halothermophilic protease from a halophilic bacterium Chromohalobacter sp. TVSP101
Autores: | Vidyasagar,Malashetty; Prakash,S.; Mahajan,Vineet; Shouche,Yogesh S.; Sreeramulu,K.
Data: | 2009-03-01
Ano: | 2009
Palavras-chave: | Chromohalobacter sp. TVSP101; Halothermophilic protease; Purification; Organic solvents; Osmolytes.
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.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822009000100002
Editor: | Sociedade Brasileira de Microbiologia
Relação: | 10.1590/S1517-83822009000100002
Formato: | text/html
Fonte: | Brazilian Journal of Microbiology  v.40 n.1 2009
Fonte: | info:eu-repo/semantics/openAccess