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Phylogenetic tree constructed with the neighbour-joining method according to 16S rDNA gene sequence evolutionary distance among Bacillus sp. TULH and the type strains of recognized members of the genus Bacillus

Phylogenetic tree constructed with the neighbour-joining method according to 16S rDNA gene sequence evolutionary distance among Bacillus sp. TULH and the type strains of recognized members of the genus Bacillus

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The present study is aimed at assessing the ability of the microbial community of hot water spring to produce different industrial important enzymes. Identification was based on biochemical, morphological measures and response of different growth parameters.15 potential isolates of different thermostable enzyme producer were obtained during primary...

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... rDNA gene sequence analysis indicated that isolate no. 2 was phylogenetically related to members of the genus Bacillus. The phylogenetic tree ( Figure 6) also indicated that isolate no. 2 clustered with Bacillus species and this cluster was strongly supported (100%). Bacillus isolate no. 2 16S r RNA sequence was publicly deposited with accession no. ...

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... Hot water springs were formed as a result of geothermic central heating due to which ground water oozes out from the earth crust [1]. Alkaline/freshwater thermal springs are categorized as extreme hot environments which are niche of diversity of thermophilic bacteria [2]. ...
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23 Study was aimed at screening and characterizing thermostable amylase-producing bacteria from water 24 and sediment samples of unexplored hot spring.. Four thermophilic isolates were characterized using 16S 25 rDNA sequencing and identified as Anoxybacillus mongoliensis (MBT001), Anoxybacillus 26 flavithermus (MBT002), Bacillus (MBT004) and MBT003 gave resemblance to both Anoxybacillus 27 mongoliensis and Anoxybacillus flavithermus. Amylase activity was measured and biosynthesis was 28 observed at 7 pH, 70 °C, 1.25% substrate concentration, 300 µL of inocula size after 48 hours of 29 incubation. Optimum amylase activity (4.4 U/mL) and stability (3.3 U/mL) was observed with 1.5 % 30 soluble starch at 70 °C. Maximum activity (3.7 U/mL) and stability (1.5 U/mL) was obtained at pH 8. 31 Enzyme activity increased in the with MgSO 4 and CaCl 2. Amylase was stable with surfactants and 32 detergents for 30 minutes and improved washing ability of the detergent. Thermostable bacteria are 33 excellent source of amylase which can be used commercially 34