Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing bacterium isolated from Mount Rittmann (Antarctica)

Poli, Annarita; Esposito, Enrico; Lama, Licia; Orlando, Pierangelo; Nicolaus, Giancarlo; Appolonia, Francesca de; Gambacorta, Agata; Nicolaus, Barbara

doi:10.1016/j.syapm.2005.10.003

Cited by 93 publications

(49 citation statements)

References 31 publications

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“…• C, which is comparable to those de- scribed for other Anoxybacillus α-amylases (Poli et al 2006;Farahmand et al 2009;Chai et al 2012;Kikani & Singh 2012). These are the properties considered to be very important for industrial starch liquefaction.…”

Section: Dsm 2641 and Anoxybacillus Pushchinoensis Dsm 12423supporting

confidence: 75%

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: 75%

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 activity of each enzyme, protease, 8) amylase, 9) lipase, 9) gelatinase, 10) urease, 11) phosphatase, 12) cellulase, 13) chitinase, 7) and -glucosidase, 14) was measured according to methods described in these previous reports.…”

Section: Abstract: Extracellular Enzymes; Thraustochytrids;mentioning

confidence: 99%

Extracellular Enzymes Produced by Marine Eukaryotes, Thraustochytrids

Taoka

Nagano

Okita

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…This report describes purification, biochemical characterization and immobilization of a thermostable α-amylase by the extremophile Anoxybacillus amylolyticus, strain MR3CT [8], a thermophilic species isolated in Antarctica and its production, either in Submerged Fermentation (SmF) and Solid State Fermentation (SSF) conditions. The enzyme production were investigated in relation to different kinds of raw vegetable waste biomass, i.e.…”

Section: Introductionmentioning

confidence: 99%

Use of Agro Waste Biomass for α-Amylase Production by Anoxybacillus amylolyticus: Purification and Properties

Finore

Donato²,

Poli³

et al. 2014

J Microb Biochem Technol

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Knowledge accumulated from fundamental and applied studies on Anoxybacillus suggests that this genus can serve as a good alternative in many applications related to starch and lignocellulosic biomasses, waste treatment, enzyme technology, and bioenergy production.We investigated the purification, biochemical characterization and immobilization of a thermostable α-amylase from the thermophilic Anoxybacillus amylolyticus, strain MR3CT, isolated in Antarctica and its production on vegetable wastes. In particular, the rhizome from Arundo donax, waste biomass of Cynara cardunculus and potato peels were tested either in Submerged Fermentation (SmF) and Solid State Fermentation (SSF) conditions.The amylase from A. amylolyticus, with a molecular weight of about 60 kDa, displayed an optimum enzyme activity at 60°C and pH 5.6. Moreover, by retaining up to 70% of total activity after 48 h at 60°C, it showed high thermostability in the presence of 2 mM calcium ion. The immobilized enzyme maintained the 48% of its initial activity after the sixth reuse. The optimal conditions for its production in SmF were achieved at 60°C for 24 h with 1% of rhizome from Arundo donax, which was about 2126 U/gds. SSF cultures reached maximum α-amylase yield (102 U/gds) when grown on waste biomass of Cynara cardunculus as substrate, with a substrate-water ratio of 1:1 (w/v), and incubation at 60°C for 4 days. In this study, rhizome of A. donax resulted to be a good substrate for amylase production in SmF thus allowing a cheaper alternative to obtain amylolytic enzymes. Indeed by using rhizomes from A. donax as growth substrate it was possible to recovery an amylase activity level higher than that obtained by synthetic complex medium. Amylase production was also investigated under SSF conditions by using the above listed wastes as sole carbon source for A. amylolyticus growth. Under these conditions, C. cardunculus gave a higher enzyme yield per reactor volume.

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Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing bacterium isolated from Mount Rittmann (Antarctica)

Cited by 93 publications

References 31 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

Extracellular Enzymes Produced by Marine Eukaryotes, Thraustochytrids

Use of Agro Waste Biomass for α-Amylase Production by Anoxybacillus amylolyticus: Purification and Properties

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