A novel thermostable, acidophilic α-amylase from a new thermophilic “Bacillus sp. Ferdowsicous” isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization

Asoodeh, Ahmad; Chamani, Jamshidkhan; Lagzian, Milad

doi:10.1016/j.ijbiomac.2010.01.013

Cited by 110 publications

(62 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: Elutionmentioning

confidence: 99%

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: Elutionmentioning

confidence: 99%

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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“…In general, the exploitation of casein by LAB is initiated by a cell-envelope proteinase (CEP) that degrades the protein into oligopeptides that are subsequently taken up by the cells via specific peptide transport systems for further degradation into shorter peptides and amino acids by a concerted action of various intracellular peptidases (Kunji et al, 1996;Christensen et al, 1999). Although most LAB are unable to degrade starch because of the lack of the amylolytic activity, a few exhibit this activity and are qualified as amylolytic lactic acid bacteria (ALAB) which are able to decompose starchy material through the amylases production during the fermentation processes (Asoodeh et al, 2010). Most amylolytic LAB isolated belong to the Lactobacillus genus, while few studies reported the existence of amylolytic activity in some strains of Bifidobacterium isolated from the human large intestinal tract (Ji et al, 1992;Lee et al, 1997).…”

Section: Starch Protein and Lipid Digesting Capabilitiesmentioning

confidence: 99%

In vitro evaluation of probiotic potential of five lactic acid bacteria and their antimicrobial activity against some enteric and food-borne pathogens

Gad

El-Baky

Ahmed

et al. 2016

Afr. J. Microbiol. Res.

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Lactic acid bacteria (LAB) present many important properties in food manufacturing, such as improvement of physical characteristics and the production of lactic acid that aids in the increase of the shelf life of food products. Also, LAB can suppress growth of pathogens, control of serum cholesterol level, modulate immune system, and improve lactose digestion. Five standard (Lactobacillus paracasei, Lactobacillus helveticus, Lactobacillus fermentum, Bifidobacterium longum and Lactococcus lactis) lactic acid bacterial strains were screened for probiotic potential properties and their ability to antagonize the growth of some enteric pathogens isolated from patients suffering from acute gastroenteritis. The five strains of LAB were resistant to acidic pH and bile salts. Lactobacillus strains showed protein and starch digesting capability on agar plate while B. longum ATCC 15707 and L. lactis subsp. lactis ATCC 11454 showed only protein digestion. In addition, Lactobacillus strains showed antagonistic effects against all pathogenic strains tested. L. paracasei and L. helveticus [culture and cell-free culture supernatant (CFCS)] exhibited the highest antagonistic activity against the tested pathogens followed by L. fermentum. While B. longum and L. lactis subsp. lactis showed weak or no activity against the tested strains. L. paracasei, L. helveticus, and L. fermentum showed potential to be used as probiotic strains with considerable good antagonistic activity against the most important enteric pathogens.

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“…The molecular mass of the enzyme was estimated as a single peptide on 6% SDS-PAGE; its molecular weight was about 180 kDa (data not shown). The α-amylases of genus Bacillus have been well characterized and their molecular masses range from 28,000 to 59,000 (Krishnan and Chandra, 1983;Sajedi et al, 2005;Asoodeh et al, 2010;Hmidet et al, 2010;Kikani and Singh, 2011) . In the case of amylase in Lactobacillus manihotivorans, its molecular mass was 135,000 (Aguilar et al, 2000).…”

Section: Pediococcus Inopinatus (Aj271383)mentioning

confidence: 99%

Characterization of Novel Amylase from Amylolytic Lactic Acid Bacteria Pediococcus ethanolidurans Isolated from Japanese Pickles (Nuka-zuke)

Iuchi

Haruguchi

Mongkolthanaruk

et al. 2012

FSTR

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In this study, Pediococcus ethanolidurans A4-27 was isolated from Japanese pickles (nuka-zuke). The bacteria produce high molecular weight amylase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and zymogram activity staining showed a single band at around 150 kDa. The enzyme was purified by disc preparative native-polyacrylamide gel electrophoresis, and ion chromatograph analysis of reaction products of P. ethanolidurans amylase on starch showed that glucose and maltose are the main final products. The appearance of maltose and glucose as major hydrolysis products suggests that the amylase produced by this organism is of α-type. Optimal temperature and pH for the enzyme activity were 60℃ and pH 4.0 − 6.0, respectively. Enzyme activity was not affected by the presence of 10 mM calcium chloride (Ca 2+ ) or the presence of 1000 mM and 2000 mM NaCl. These results indicate that the amylase from P. ethanolidurans is a useful enzyme for fermentation of rice bran-bed (nuka-doko) containing more than 15% NaCl.

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A novel thermostable, acidophilic α-amylase from a new thermophilic “Bacillus sp. Ferdowsicous” isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization

Cited by 110 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

In vitro evaluation of probiotic potential of five lactic acid bacteria and their antimicrobial activity against some enteric and food-borne pathogens

Characterization of Novel Amylase from Amylolytic Lactic Acid Bacteria Pediococcus ethanolidurans Isolated from Japanese Pickles (Nuka-zuke)

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