2011
DOI: 10.3923/jm.2011.140.146
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Characterization of Alpha Amylase from Bacillus subtilis BS5 Isolated from Amitermes evuncifer Silvestri

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Cited by 25 publications
(18 citation statements)
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“…These results illustrated that gel filtration chromatography efficiently purified the amylase produced by B. subtilis in submerged fermentation. This purification fold was less than that from other strains of Bacillus which used DEAE-cellulose 27 and gel filtration chromatography 28 for purification, respectively. Bano et al 29 purified α-amylase from Bacillus subtilis having specific activity of 13011 U mg -1 with purification fold of 96.3.…”
Section: Purification Of Amylasementioning
confidence: 78%
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“…These results illustrated that gel filtration chromatography efficiently purified the amylase produced by B. subtilis in submerged fermentation. This purification fold was less than that from other strains of Bacillus which used DEAE-cellulose 27 and gel filtration chromatography 28 for purification, respectively. Bano et al 29 purified α-amylase from Bacillus subtilis having specific activity of 13011 U mg -1 with purification fold of 96.3.…”
Section: Purification Of Amylasementioning
confidence: 78%
“…MNJ23 produced low molecular weight α-amylase of 42.8 kDa, 42.0 kDa and 25kDa, respectively 27,31,32 . But some strains of Bacillus subtilis produced α-amylase having high molecular weight of 93, 68, 63 28,33,34 .…”
Section: Molecular Weight Determination Of the A-amylasementioning
confidence: 99%
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“…A similar trend with respect to concentration-dependence was observed in case of EDTA on amylase. Kiran and Chandra [22] and Femi-Ola and Olowe [23] reported that EDTA inhibited amylase activity; suggesting that EDTA acted by chelating Ca Dehydrogenase was also found to be sensitive to butanol and ethanol. A significant stimulation on the enzyme specific activity was observed with ethanol.…”
Section: Discussionmentioning
confidence: 99%
“…Так, величина K м у разі розщеплення роз-чинного крохмалю B. licheniformis [2] станови-ла 8,3 мг/мл. Величина K м α-амілази B. subtilis BS5 за розщеплення розчинного крохмалю становила 16,67 [68], α-амілази T. thalpophilus KSV 17 -5,2 [32], α-амілази Bacillus sp. GRE1 -4,98 [67], α-амілази B. subtilis KCX 006 -0,291 [79], α-амілази B. amyloliquefaciens -3,076 [23], α-амілази G. thermoleovorans -1,11 [65].…”
Section: фізико-хімічні властивості α-амілазunclassified