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KMID : 0379119960240010008
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Korean Journal of Mycology
1996 Volume.24 No. 1 p.8 ~ p.16
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Characterization of Alternaria alternata α-Amylase
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Abstract
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The α-amylase of Alternaria alternate was purified through ammonium sulfate precipitation, dialysis and Sepbadex G-100 column chromatography. One single band was obtained in SDS-polyacrylamide gel electrophoresis. The optimum pH for enzyme activity was S.0 and the enzyme activity was maintained at 3.6∼7.0 pH range. The optimum temperature for α-amylase activity was 40℃ and 71 % of the activity was still maintained until 30 min after heating at 80℃. The α-amylase was slightly activated by Mn^(2+), Zn^(2+) and Sn^(2+), but inhibited by Ba^(2+), Pb^(2+), Co^(2+) and Ag^(3+). The Hg^(2+) and Ag^(2+) slightly inhibited the activity of the enzyme at concentrations of 10^(-3) and 10^(-4)M. The Michaelis constant (K_m) to soluble starch was 6.50×10^(-2) M and inhibition constant (K₁) by the 1 mM EDTA was 80×10^(-2) M. The inhibition of this enzyme by EDTA was competitive one.
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