Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6

Arikan, Burhan; Nisa, Unaldi; Coral, Gökhan; Çolak, Ömer; Aygan, Ashabil; Gülnaz, Osman

doi:10.1016/s0032-9592(03)00037-2

Cited by 264 publications

(175 citation statements)

References 39 publications

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“…Mukesh et al [8] reported α-amylases stability over a wide range of pH 4 to 11. The optimum pH 7.0 and above for α-amylase activity from B. subtilis, B. licheniformis, B. amyloliquefaciens and thermophilic Anoxybacillus flavithermus has been reported [16,[22][23][24][25][26]] pH 8.0 optimum has been reported for amylase activity from Thermus sp., Bacillus KSM-K38 and Bacillus spp [27,28] Wide range (pH 3.5 to 12) optimum pH for α-amylases has been reported [7,[29][30][31][32]. The result obtained from this study agrees with the findings of Agülo˘glu Fincan and Bukhari and Rehman [32,33] who reported pH 7.0 optimum for purified α-amylase from Bacillus subtilis from local environment.…”

Section: Elutionsupporting

confidence: 88%

Purification and Characterization of α-Amylase from Bacillus subtilis Isolated from Cassava Processing Sites

David¹,

Femi²,

Gbenga³

et al. 2017

J Bioremediat Biodegrad

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This study was designed to purify and characterize of α-amylase from pure strain of Bacillus subtilis. The crude α-amylase was purified by ammonium sulphate precipitation, then loaded on DEAE Sephadex A-50 ion exchange chromatography and gel filtration. The effect of pH, temperature and metal ions were investigated on the purified enzyme. The single protein band on SDS-PAGE suggested that the enzyme was homogenous. Two different activity peaks were observed in ion exchange chromatography designated pool A and pool B with the 8% and 4% yield, 15.93 and 6.44 purification fold and specific activity 2.55 μmol/min/mg and 1.03 μmol/min/mg respectively. The two fractions revealed the same optimum pH 7.0 for the α-amylase activity while the enzyme was relatively stable at pH 4.0 and 7.0 between 20 to 40 minutes and 60 to 80 minutes for pool A and pH 8.0 between 40 and 100 minutes for pool B. At 40°C, optimum temperature was reached, and amylase activity was maintained at 75% and 70% temperature stability between 60 to 80 minutes for pool A and B, less than 20%, the residual activity at 60°C and 70°C was recorded. The incubation of α-amylase with Na + and Zn 2+ ions enhanced/activate the enzyme activity correspondingly, Al 3+ and K + ions exhibited varied degree of inhibition while Ca 2+ and Hg 2+ ions caused total inhibition on α-amylase activity. The ability of purified α-amylase from Bacillus subtilis under wide range of temperatures and pH suggests its applications in industries and bioremediation of effluent discharge on food processing sites.

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Section: Elutionsupporting

confidence: 88%

Purification and Characterization of α-Amylase from Bacillus subtilis Isolated from Cassava Processing Sites

David¹,

Femi²,

Gbenga³

et al. 2017

J Bioremediat Biodegrad

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“…It is degraded by amylolytic enzymes. Although amylases originate from different sources (animals, plants and microorganisms), microbial amylases generally meet industrial demands best, due to their short growth period and productivity (6). Its extensive application in food, starch liquefaction, saccharification, detergent, brewing, paper, textile and distilling industries, has led to a greater stress for the increase in the indigenous production of α-amylase (12).…”

Section: Introductionmentioning

confidence: 99%

Comparative study on production of α-Amylase from Bacillus licheniformis strains

Divakaran¹,

Chandran²,

Chandran³

2011

Braz. J. Microbiol.

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Alpha amylase (α-1, 4-glucan-glucanhydrolase, EC 3.2.1.1), an extracellular enzyme, degrades α, 1-4 glucosidic linkages of starch and related substrates in an endo-fashion producing oligosaccharides including maltose, glucose and alpha limit dextrin (7). The present study deals with the production and comparative study of production of α-amylase from two strains of Bacillus licheniformis, MTCC 2617 and 2618, by using four different substrates, starch, rice, wheat and ragi powder as carbon source by submerged fermentation. The effect of varying pH and incubation temperature, activator, inhibitor, and substrate concentration was investigated on the activity of α-amylase produced by MTCC strain 2618. The results shows that the production of the α-amylase by the B.licheniformis strain MTCC 2618, using four different substrates were found to be maximum (Starch 3.64 IU/ml/minutes, Rice powder 2.93 IU/ml/minutes, Wheat powder 2.67 IU/ml/minutes, Ragi powder 2.36 IU/ml/minutes) on comparing the enzyme production of two strains. It was also observed that the maximum production was found on the 3 rd day (i.e. 72 hr) and characterization of crude enzyme revealed that optimum activity was at pH 7 and 37°C.

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“…The extensive application of amylases in the food, starch liquefaction and saccharification, detergent, textile, paper, brewing and distilling industries has paved a way for their large-scale commercial production (Gupta et al, 2003). Although amylases originate from different sources (plants, animals and microorganisms), microbial amylases generally meet industrial demands best, due to their short growth period, productivity and thermostability (Burhan et al, 2003). Today, a large number of microbial amylases are available commercially and they have almost completely replaced chemical hydrolysis of starch in the starch processing industry (Pandey et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

“…Microbial amylases are produced mainly from cultures of Aspergillus, Bacillus, Clostridium, Pseudomonas, Rhizopus and Streptomyces species (Pandey et al, 2000). Because of the industrial importance of amylases, there is an increasing worldwide interest in the screening of new microorganisms producing amylases suitable for new industrial applications (Burhan et al, 2003;Gupta et al, 2003). Rhizobia are gram-negative soil bacteria belonging to the family Rhizobiaceae that are capable of infecting and nodulating the roots of their hosts, leguminous plants.…”

Section: Introductionmentioning

confidence: 99%

Partial characterization of amylases of two indigenous Central Amazonian rhizobia strains

Oliveira

Andrade

2010

Braz. arch. biol. technol.

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Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6

Cited by 264 publications

References 39 publications

Purification and Characterization of α-Amylase from Bacillus subtilis Isolated from Cassava Processing Sites

Purification and Characterization of α-Amylase from Bacillus subtilis Isolated from Cassava Processing Sites

Comparative study on production of α-Amylase from Bacillus licheniformis strains

Partial characterization of amylases of two indigenous Central Amazonian rhizobia strains

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