Anoxybacillus ayderensis sp. nov. and Anoxybacillus kestanbolensis sp. nov.

Dülger, Sabriye; Demirbağ, Zihni; Beldüz, Ali Osman

doi:10.1099/ijs.0.02863-0

Cited by 75 publications

(48 citation statements)

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“…4), respectively. The similar optimum temperature value was obtained for Anoxybacillus ayderensis NCIMB 13972T (Dulger et al 2004) and Anoxybacillus contaminans DSM 15866T (De Clerck et al 2004) as 50…”

Section: Dsm 2641 and Anoxybacillus Pushchinoensis Dsm 12423supporting

confidence: 54%

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Isolation and production of thermostable α-amylase from thermophilic Anoxybacillus sp. KP1 from Diyadin hot spring in Ağri, Turkey

Bekler

Güven

2014

Biologia

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A novel amylolytic enzyme producing thermophilic bacterial strain KP1 from the Diyadin hot spring water in Agri, Turkey, was isolated in the present study. Phylogenetic analysis based on the partial 16S rRNA gene, biochemical and physiological tests revealed that the strain KP1 belongs to the genus Anoxybacillus. The pH and temperature optima for the α-amylase production by Anoxybacillus sp. KP1 were 8.0 and 50• C, respectively, where the maximum growth was obtained at the 28 th hour of incubation and the highest α-amylase activity was obtained at the 40 th hour of incubation (8979.6 U/mL). The optimum pH and temperature for the enzyme activity were 8.0 and 60• C, respectively. The maximum α-amylase production was secreted in the presence of 2% (w/v) soluble starch (10837.7 U/mL). Among the various organic and inorganic nitrogen sources tested, while keeping the beef extract concentration constant, casamino acid (14310.6 U/mL), urea (14126 U/mL), and tryptone (13217.2 U/mL) at a concentration of 2% gave the maximum α-amylase production. The enzyme activity was enhanced in the presence of 1.5 mM Mn 2+ (123%), whereas it was strongly inhibited 1.5 mM by Hg 2+ . Inhibition by 89% was obtained also with sodium dodecyl sulphate (1%). The enzyme was found to be relatively stable at a range of pH and temperature.

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Section: Dsm 2641 and Anoxybacillus Pushchinoensis Dsm 12423supporting

confidence: 54%

“…In later studies, Belduz et al (2003) and Dulger et al (2004) Chai et al (2012) also isolated thermophilic Anoxybacillus sp. DT3-1 and SK3-4 from two hot springs in Malaysia.…”

Section: Dsm 2641 and Anoxybacillus Pushchinoensis Dsm 12423mentioning

confidence: 99%

Isolation and production of thermostable α-amylase from thermophilic Anoxybacillus sp. KP1 from Diyadin hot spring in Ağri, Turkey

Bekler

Güven

2014

Biologia

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“…The name given to the genus suggests that species assigned to it thrive under anoxic conditions, and, indeed, the first species classified as members of the genus Anoxybacillus were aerotolerant anaerobes (Pikuta et al, 2000). Nevertheless, at the time of writing, from the 22 species of the genus Anoxybacillus, 16 are facultative anaerobes (Atanassova et al, 2008;Belduz et al, 2003;Cihan et al, 2011Cihan et al, , 2014Dai et al, 2011;De Clerck et al, 2004;Dulger et al, 2004;Kevbrin et al, 2005;Namsaraev et al, 2010;Poli et al, 2006;Schaffer et al, 2004;Yumoto et al, 2004;Zhang et al, 2011), five are strict aerobes (Coorevits et al, 2012;Derekova et al, 2007;Inan et al, 2013;Poli et al, 2009;Zhang et al, 2013) and one is an aerotolerant anaerobe (Pikuta et al, 2000). Species that belong to the genus Anoxybacillus share common characteristics, mainly concerning their major fatty acids (iso-C 17 : 0 and iso-C 15 : 0 ), the rod shape of the vegetative cells and the terminal/subterminal position of their endospores.…”

mentioning

confidence: 99%

“…Besides the phenotypic similarities, species that belong to the genus Anoxybacillus share common ecological characteristics, too. All of them are thermophiles or moderate thermophiles, with the majority of the species isolated so far originating from thermal springs (Atanassova et al, 2008;Belduz et al, 2003;Cihan et al, 2011Cihan et al, , 2014Dai et al, 2011;Derekova et al, 2007;Dulger et al, 2004;Inan et al, 2013;Poli et al, 2009;Yumoto et al, 2004;Zhang et al, 2011Zhang et al, , 2013. The aim of this study was to describe a novel species of the genus Anoxybacillus isolated from a geothermal reservoir.…”

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confidence: 99%

Anoxybacillus geothermalis sp. nov., a facultatively anaerobic, endospore-forming bacterium isolated from mineral deposits in a geothermal station

Filippidou

Jaussi

Junier

et al. 2016

International Journal of Systematic and Evolutionary Microbiology

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A novel endospore-forming bacterium designated strain GSsed3 T was isolated from deposits clogging aboveground filters from the geothermal power platform of Groß Schönebeck in northern Germany. The novel isolate was Gram-staining-positive, facultatively anaerobic, catalase-positive and oxidase-positive. Optimum growth occurred at 60 C, 0.5 % (w/v) NaCl and pH 7-8. Analysis of the 16S rRNA gene sequence similarity indicated that strain GSsed3 T belonged to the genus Anoxybacillus, and showed 99.8 % sequence similarity to Anoxybacillus rupiensis R270 T , 98.2 % similarity to Anoxybacillus tepidamans GS5-97 T , 97.9 % similarity to Anoxybacillus voinovskiensis TH13 T , 97.7 % similarity to Anoxybacillus caldiproteolyticus DSM 15730 T and 97.6 % similarity to Anoxybacillus amylolyticus MR3C T . DNA-DNA hybridization (DDH) indicated only 16 % relatedness to Anoxybacillus rupiensis DSM 17127 T . Furthermore, DDH estimation based on genomes analysis indicated only 19.9 % overall nucleotide similarity to Anoxybacillus amylolyticus DSM 15939 T . The major respiratory menaquinone was MK-8. The polar lipid profile consisted of phosphatidylethanolamine, phosphatidylglycerol, diphosphatidylglycerol, one unknown phosphoglycolipid and one unknown phospholipid. The predominant cellular fatty acids were iso-C 15 : 0 , iso-C 17 : 0 , C 16 : 0 , iso-C 16 : 0 and anteiso-C 17 : 0 . The peptidoglycan type was A1g meso-Dpm-direct. The genomic DNA G+C content of the strain was 46.9 mol%. The phenotypic, genotypic and chemotaxonomic characterization indicated that strain GSsed3 T differs from related species of the genus. Therefore, strain GSsed3 T is considered to be a representative of a novel species of the genus Anoxybacillus, for which the name Anoxybacillus geothermalis sp. nov. is proposed. The type strain of Anoxybacillus geothermalis is GSsed3 T (=CCOS808 T =ATCC BAA2555 T ).

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“…In this paper, we describe for the first time the cloning and characterization of thermophilic L-ribulokinase from Anoxybacillus kestanbolensis AC26Sari. Dulger et al (2004) isolated and identified Anoxybacillus kestanbolensis AC26Sari from the Çamköy mud hot spring in the province of Çanakkale, Turkey. A. kestanbolensis AC26Sari was used as the source of chromosomal DNA and thermophilic L-ribulokinase.…”

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confidence: 99%

Cloning, purification, and characterization of a thermophilic ribulokinase from Anoxybacillus kestanbolensis AC26Sari

Tokgöz¹,

İnan²,

Beldüz³

et al. 2014

Turk J Biol

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IntroductionAnoxybacillus is a relatively new genus compared to the well-studied genera Geobacillus or Bacillus. The genus Anoxybacillus represents aerobic or facultatively anaerobic, neutrophilic, obligately thermophilic, endospore-forming bacteria (İnan et al., 2011). Most of the reported data have revealed that the members of this genus produce interesting enzymes that are thermostable and tolerant to alkaline pH. Some of the well-studied enzymes were discovered through partnerships with industry; for example, the raw starch-degrading amylase was discovered by a Novozyme team (Viksø-Nielsen et al., 2006), and the BfιI RE was discovered by New England Biolabs (D'Souza et al., 2004;Goh et al., 2013).L-ribulokinase (RK; EC 2.7.1.16) is 1 of 3 major enzymes of the arabinose catabolic pathway. L-arabinose is 1 of the major polysaccharide components in plant cell walls and among the most abundant monosaccharides in nature. Furthermore, its utilization pathway in bacteria has been investigated extensively (Zhang et al., 2012). The arabinose regulon is 1 of many gene systems in Escherichia coli and the regulon consists of 4 operons, araBAD, araC, araE, and araFGH, which are responsible for L-arabinose catabolism, gene regulation, low-affinity transport, and high-affinity transport, respectively (Englesberg and Wilcox, 1974;Lichenstein et al., 1987). In the lowaffinity transport system, the transporter, the araE gene product, is bound to the inner membrane and utilizes the electrochemical potential to transport arabinose. The araFGH genes encode arabinose-specific components of a high-affinity transport system, ABC transporters. These are 3 proteins of the ATP-binding cassette transporter family. AraF is the periplasmic arabinose-binding protein, AraG is the ATP-binding component, and AraH is the membrane-bound component (Schleif, 2010). AraC acts directly as an inducer or an activator of gene expression.The araBAD operon encodes 3 different enzymes required for catabolism of L-arabinose, which are responsible for the conversion of L-arabinose into D-xylulose-5-phosphate. AraA, as an isomerase (L-arabinose isomerase), converts arabinose to L-ribulose; AraB, as a kinase (L-ribulokinase), phosphorylates L-ribulose; and AraD, as an epimerase (L-ribulose-5phosphate 4-epimerase), converts L-ribulose-phosphate

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Anoxybacillus ayderensis sp. nov. and Anoxybacillus kestanbolensis sp. nov.

Abstract: Two thermophilic bacilli were isolated from mud and water samples of the Ayder and Kestanbol hot springs in the provinces of Rize and Canakkale, respectively, in Turkey. Strains AB04 T and K4 T were sporulating, Gram-positive, rod-shaped bacteria. These isolates were moderately

Cited by 75 publications

References 4 publications

Isolation and production of thermostable α-amylase from thermophilic Anoxybacillus sp. KP1 from Diyadin hot spring in Ağri, Turkey

Isolation and production of thermostable α-amylase from thermophilic Anoxybacillus sp. KP1 from Diyadin hot spring in Ağri, Turkey

Anoxybacillus geothermalis sp. nov., a facultatively anaerobic, endospore-forming bacterium isolated from mineral deposits in a geothermal station

Cloning, purification, and characterization of a thermophilic ribulokinase from Anoxybacillus kestanbolensis AC26Sari

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