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Characterization of Leptospira borgpetersenii isolates from field rats (Rattus norvegicus) by 16S rRNA and lipL32 gene sequencing BJM
Vedhagiri,Kumaresan; Natarajaseenivasan,Kalimuthusamy; Prabhakaran,Shanmugarajan G.; Selvin,Joseph; Narayanan,Ramasamy; Shouche,Yogesh S.; Vijayachari,Paluru; Ratnam,Sivalingam.
The main goal of this study was to evaluate the prevalence of leptospirosis among field rodents of Tiruchirappalli district, Tamil Nadu, India. In total 35 field rats were trapped and tested for seroprevalence by the microscopic agglutination test (MAT). Isolation of leptospires was performed from blood and kidney tissues and characterized to serovar level. Genomospecies identification was carried out using 16S rRNA and lipL32 gene sequencing. The molecular phylogeny was constructed to find out species segregation. Seroprevalence was about 51.4 %, and the predominant serovars were Autumnalis, Javanica, Icterohaemorrhagiae and Pomona. Two isolates from the kidneys were identified as serovar Javanica of Serogroup Javanica, and sequence based molecular...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Leptospirosis; Leptospira borgpetersenii; LipL32; 16S rRNA.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822010000100022
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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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