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Applied and Environmental Microbiology
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PHYSIOLOGY AND BIOTECHNOLOGY

Purification and Characterization of α-Amylase from Bacillus licheniformis CUMC305

T. Krishnan, A. K. Chandra
T. Krishnan
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A. K. Chandra
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ABSTRACT

α-Amylase produced by Bacillus licheniformis CUMC305 was purified 212-fold with a 42% yield through a series of four steps. The purified enzyme was homogeneous as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and discontinuous gel electrophoresis. The purified enzyme showed maximal activity at 90°C and pH 9.0, and 91% of this activity remained at 100°C. The enzyme retained 91, 79, and 71% maximal activity after 3 h of treatment at 60°C, 3 h at 70°C, and 90 min at 80°C, respectively, in the absence of substrate. On the contrary, in the presence of substrate (soluble starch), the α-amylase enzyme was fully stable after a 4-h incubation at 100°C. The enzyme showed 100% stability in the pH range 7 to 9; 95% stability at pH 10; and 84, 74, 68, and 50% stability at pH values of 6, 5, 4, and 3, respectively, after 18 h of treatment. The activation energy for this enzyme was calculated as 5.1 × 105 J/mol. The molecular weight was estimated to be 28,000 by sodium dodecyl sulfate-gel electrophoresis. The relative rates of hydrolysis of soluble starch, amylose, amylopectin, and glycogen were 1.27, 1.8, 1.94, and 2.28 mg/ml, respectively. Vmax values for hydrolysis of these substrates were calculated as 0.738, 1.08, 0.8, and 0.5 mg of maltose/ml per min, respectively. Of the cations, Na+, Ca2+, and Mg2+, showed stimulatory effect, whereas Hg2+, Cu2+, Ni2+, Zn2+, Ag+, Fe2+, Co2+, Cd2+, Al3+, and Mn2+ were inhibitory. Of the anions, azide, F−, SO32−, SO43−, S2O32−, MoO42−, and Wo42− showed an excitant effect. p-Chloromercuribenzoic acid and sodium iodoacetate were inhibitory, whereas cysteine, reduced glutathione, thiourea, β-mercaptoethanol, and sodium glycerophosphate afforded protection to enzyme activity. α-Amylase was fairly resistant to EDTA treatment at 30°C, but heating at 90°C in presence of EDTA resulted in the complete loss of enzyme activity, which could be recovered partially by the addition of Cu2+ and Fe2+ but not by the addition of Ca2+ or any other divalent ions.

  • Copyright © 1983, American Society for Microbiology
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Purification and Characterization of α-Amylase from Bacillus licheniformis CUMC305
T. Krishnan, A. K. Chandra
Applied and Environmental Microbiology Aug 1983, 46 (2) 430-437; DOI:

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Purification and Characterization of α-Amylase from Bacillus licheniformis CUMC305
T. Krishnan, A. K. Chandra
Applied and Environmental Microbiology Aug 1983, 46 (2) 430-437; DOI:
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