4.2 Article

Properties of an amylase from thermophilic Bacillus sp.

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BRAZILIAN JOURNAL OF MICROBIOLOGY
卷 39, 期 1, 页码 102-107

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SOC BRASILEIRA MICROBIOLOGIA
DOI: 10.1590/S1517-83822008000100023

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alpha-amylase; thermophilic bacterium; Bacillus sp

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alpha-Amylase production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing soluble starch as a carbon source and supplemented with 0.05% whey protein and 0.2% peptone reached a maximum activity at 32 h, with levels of 37 U/mL. Studies on the amylase characterization revealed that the optimum temperature of this enzyme was 90 degrees C. The enzyme was stable for 1 h at temperatures ranging from 4050 50 degrees C while at 90 degrees C, 66% of its maximum activity was lost. However, in the presence of 5 mM CaCl2, the enzyme was stable at 90 degrees C for 30 min and retained about 58% residual activity after 1 h. The optimum pH of the enzyme was found to be 8.5. After incubation of enzyme for 2 h at pH 9.5 and 11.0 was observed a decrease of about 6.3% and 16.5% of its original activity. At pH 6.0 the enzyme lost about 36% of its original activity. The enzyme was strongly inhibited by Co2+, Cu2+ and Ba2+, but less affected by Mg2+, Na+ and K+. In the presence of 2.0 M NaCl, 63% of amylase activity was retained after 2 h incubation at 45 degrees C. The amylase exhibited more than 70% activity when incubated for 1 h at 50 degrees C with sodium dodecyl sulphate. However, very little residual activity was obtained with sodium hypochlorite and with hydrogen peroxide the enzyme was completely inhibited. The compatibility of Bacillus sp SMIA-2 amylase with certain commercial detergents was shown to be good as the enzyme retained 86%, 85% and 75% of its activity after 20 min incubation at 50 degrees C in the presence of the detergent brands Omo (R), Campeiro (R) and Tide (R), respectively.

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