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KMID : 0379119890170030145
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Korean Journal of Mycology
1989 Volume.17 No. 3 p.145 ~ p.148
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Purification and Characterization of Acid - stable α-Amylase of Aspergillus niger K-25
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Abstract
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An acid-stable α-amylase produced by Aspergillus niger K-25 strain was purified by fractional precipitation with ammonium sulfate, ethacridine and acetone. The final preparation was homogeneous in cellulose acetate electrophoresis. The enzyme retained 91% of its original activity at pH 3.0, 8.7% at pH 2.4. The optimum pH of the enzyme was around pH 4. The purified-enzyme with optimum temperature of 40℃ was more heat-stable than the commercial product. The enzyme retained 80% of its original activity when heated to 60℃ for 30 minutes while the commercial amylase lost its activity completely within 30 minutes at 50℃.
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