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  1. 1 Biotechnologia

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  1. 1 2000

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  1. 1 Rodziewicz A.

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Characteristics and purification of Bacillus polymyxa B-20 amylases

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Rodziewicz A.
Biotechnologia
|
2000
|
issue 1
49-55
EN
Bacillus polymyxa B-20 alpha- and beta-amylase were purified using a combination of acetone fractionations, ion-exchange chromatography and amonium sulfate precipitation. The a-amylase was purified 18-fold, to a specific activity of 1065 U/ mg. The enzyme had on optimal temperature at 70oC and was stable up to 50oC in presence of Ca++. A purified enzyme displayed maxima for activity of pH 6,8 and was inhibited by 1 mM EDTA. Maltose is predominantly produced from starch. The beta-amylase had pH optima at 5,6 (acetate buffer), temperature optima at 60oC, was stable pH range of 5,0 to 7,5 at temperature up to 45oC. Enzyme activity was inhibited by sulfhydryl reagents such as pCMB and Hg++. Both B.polymyxa B-20, alpha- and beta-amylase are maltogenic enzymes.
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