Highly thermostable and alkaline α-amylase from a halotolerant-alkaliphilic Bacillus sp. AB68

Aygan, Ashabil; Arikan, Burhan; Korkmaz, Hatice; Dincer, Sadik; Çolak, Ömer

doi:10.1590/s1517-83822008000300027

Cited by 45 publications

(45 citation statements)

References 25 publications

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“…It was also found that 1% SDS inhibited the amylase activity by 89%. Aygan et al (2008) reported that SDS was the most effective effector that shows the proportion of the hydrophobic amino acid composition of the enzyme. Chai et al (2012) determined that the α-amylase activity was strongly inhibited in the presence of 1% SDS.…”

Section: The Inhibition By Hgmentioning

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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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: The Inhibition By Hgmentioning

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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“…Amylases of almost similar molecular weight have been reported from B. cereus NY-14 (Yoshigi et al, 1985), Bacillus subtilis (Uyar et al, 2003), and Bacillus sp. AB 68 (Aygan et al, 2008). Endoamylases are almost exclusively single subunit proteins, however, some amylases especially those having large molecular weight are found to possess more than one subunit as reported in Pyrococcus furiosus (Laderman et al, 1993) and Bacillus sp.…”

Section: Molecular Weightmentioning

confidence: 98%

“…Thermostable amylases having temperature optima between 50 to 60°C have also been isolated from a number of sources including Bifidobacterium adolescentis (Lee et al, 1997), Aspergillus oryzea (Ramachandran et al, 2004), B. subtilis (Bezerra et al, 2006) and Bacillus sp. AB68 (Aygan et al, 2008). The themostable alpha amylases isolated from various species of Bacillus have been preferred for use in starch processing industry (Nigam and Singh, 1995) Figure 3B depicts that enzyme had maximum activity at pH 5.5 (358.84 U/ mL).…”

Section: Temperature and Ph Optima And Km Valuementioning

confidence: 99%

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Purification and characterization of extracellular acidophilic -amylase from Bacillus cereus MTCC 10205 isolated from soil

Kumari¹,

Jain²,

Malhotra³

2013

Afr. J. Microbiol. Res.

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Amylase from Bacillus cereus MTCC 10205 was purified 20.41 with 11.82% recovery by ammonium sulfate precipitation, gel filtration chromatography through Sephadex G-100 and ion-exchange chromatography on diethylaminoethyl (DEAE)-cellulose. The final enzyme preparation was pure to near homogeneity as judged by native-polyacrylamide gel electrophoresis (PAGE). The enzyme had a molecular weight of 55 kDa as determined by gel filtration and a single band of 55 kDa as determined by sodium dodecyl sulfate-polycrylamide gel electrophoresis showing it to be a monomer. The purified enzyme had temperature optima of 55°C and pH optima of 5.5. The enzyme retained 72% of its original activity after 90 min of incubation and exhibited gradual loss in activity when incubated at higher temperature. At 60°C after 90 min of incubation, the enzyme was completely inactive. The enzyme appeared to be quite stable at 4°C as it could be stored upto five days with 10% loss in activity, whereas at 35°C, the enzyme lost 28% of its activity just after three days of storage. Inhibition studies revealed SH groups to be involved at the active site of the enzyme.

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“…After developing the products with a solvent system of butanol-acetic acid-water (3:1:1) by volume, the spots were visualized by spraying it with 20% Sulphuric acid in ethanol and baking it in an oven at 120 ºC for 30 min. The procedure of Aygan et al, (2008) with slight modification was followed.…”

Section: Thin Layer Chromatography (Tlc)mentioning

confidence: 99%

Production and Improvement of Alkaline α - Amylase by Bacterial Isolate from Chilika Lake

Sirisha¹,

Priyadarshini²,

Ray³

2017

Int.J.Curr.Microbiol.App.Sci

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Highly thermostable and alkaline α-amylase from a halotolerant-alkaliphilic Bacillus sp. AB68

Cited by 45 publications

References 25 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

Purification and characterization of extracellular acidophilic -amylase from Bacillus cereus MTCC 10205 isolated from soil

Production and Improvement of Alkaline α - Amylase by Bacterial Isolate from Chilika Lake

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