Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/34865
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dc.contributor.authorPathak, Anupama P.-
dc.contributor.authorRathod, Mukundraj G.-
dc.date.accessioned2016-07-21T05:32:54Z-
dc.date.available2016-07-21T05:32:54Z-
dc.date.issued2015-07-
dc.identifier.issn0975-1033 (Online); 0379-5136 (Print)-
dc.identifier.urihttp://nopr.niscair.res.in/jspui/handle/123456789/34865-
dc.description1104-1111en_US
dc.description.abstractFive efficient protease producing moderate thermophiles were isolated from Unkeshwar (19°85’ N and 78°25’E) thermal spring located in Nanded district of Maharashtra. The isolates were identified as Bacillus firmus, Bacillus aminivorans, Bacillus sterothermophilus, Bacillus brevis and Pseudomonas oleovorans using biochemical techniques. Being an efficient protease producer, Pseudomonas oleovorans was selected and further identified using 16s rRNA molecular analysis method as ‘Uncultured bacterium clone APP30’ and sequence was deposited in genebank nucleotide repository under accession number KC733812. The protease extracted and partially purified from APP30 showed remarkable caseinolytic activity at 55° C temperature and pH 9.0. The extracted protease also showed stability in presence of Chloroform, Ethanol, Butanol, Hexane, Toluene and Triton X-100 at 1 % (v/v) concentration and compatibility with different commercial detergents. Efficient destaining of blood stained cotton cloth piece was also recorded by partially purified protease. Enhanced proteolytic activity was observed in presence of CaCl2, MgSO4, KCl and NaCl at 1 % (w/v) concentration. Characterization of partially purified protease was carried out. Molecular weight of partially purified protease was determined as 28 kda.en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rightsCC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJMS Vol.44(07) [July 2015]en_US
dc.subjectUnkeshwar thermal springen_US
dc.subject16S rRNA gene sequencingen_US
dc.subjectThermostable alkaline proteaseen_US
dc.subjectMEGA 6.06en_US
dc.titleA report on thermostable alkaline protease producing bacteria from a terrestrial thermal springen_US
dc.typeArticleen_US
Appears in Collections:IJMS Vol.44(07) [July 2015]

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