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2.
Int J Syst Evol Microbiol ; 60(Pt 12): 2867-2870, 2010 Dec.
Article in English | MEDLINE | ID: mdl-20081011

ABSTRACT

A Gram-negative, rod-shaped bacterial strain, NII-0905(T) [corrected], that was motile by gliding was isolated from soil of a dense forest collected from the Western Ghats of India and its taxonomic position was established. Strain NII-0905(T) [corrected] contained MK-7 as the major menaquinone and anteiso-C(17 : 0), anteiso-C(15 : 0), iso-C(16 : 0) and iso-C(15 : 0) as the major cellular fatty acids. The DNA G+C content of strain NII-0905(T) [corrected] was 51.47 mol%. 16S rRNA gene sequence-based phylogenetic analysis confirmed the placement of strain NII-0905(T) [corrected] in the genus Pontibacter and strain NII-0905(T) [corrected] exhibited 93.9-96.3 % 16S rRNA sequence similarity with type strains of species of the genus Pontibacter. On the basis of genotypic and phenotypic evidence, strain NII-0905(T) [corrected] is considered to represent a novel species of the genus Pontibacter, for which the name Pontibacter niistensis sp. nov. is proposed. The type strain is NII-0905(T) [corrected](=NCIM 5339(T) =CCTCC AA 209057(T)).


Subject(s)
Cytophagaceae/classification , Forests , Phylogeny , Soil Microbiology , Bacterial Typing Techniques , Base Composition , Cytophagaceae/genetics , Cytophagaceae/isolation & purification , DNA, Bacterial/genetics , Fatty Acids/chemistry , India , Molecular Sequence Data , RNA, Ribosomal, 16S/genetics , Sequence Analysis, DNA , Vitamin K 2/analogs & derivatives , Vitamin K 2/chemistry
3.
Curr Microbiol ; 57(6): 638-42, 2008 Dec.
Article in English | MEDLINE | ID: mdl-18810538

ABSTRACT

Multiple proteases were produced and partially purified from an alkali-thermotolerant novel species of Streptomyces (i.e., Streptomyces gulbargensis DAS 131) after 48 h of growth at 45 degrees C. The enzyme preparation exhibited activity over a broad range of pH (4-12) and temperature (27-55 degrees C). Optimum activity was observed at a pH of 9.0 and a temperature of 45 degrees C. Starch and protease peptone was found to be a good source of carbon and nitrogen to enhance the enzyme activity. Two active zones in the range of 19 to 35 kDa were detected on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE).


Subject(s)
Bacterial Proteins/isolation & purification , Bacterial Proteins/metabolism , Peptide Hydrolases/isolation & purification , Peptide Hydrolases/metabolism , Streptomyces/enzymology , Bacterial Proteins/chemistry , Electrophoresis, Polyacrylamide Gel , Enzyme Stability , Hydrogen-Ion Concentration , Peptide Hydrolases/chemistry , Proteome/analysis , Substrate Specificity , Temperature
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