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KMID : 0366119760040030091
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Korean Journal of Applied Microbiology & Bioengineering
1976 Volume.4 No. 3 p.91 ~ p.97
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Studies on the Production of Enzymes by Thermophilic Actinomycetes
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Yang, Han-Chul/양한철
Choi, Yong-Jin/Cho, Hong-Yeon/최용진/조홍연
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Abstract
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During the course of studies on the production and utilization of thermostable α-amylase from a ther mophilic actinomycete species isolated from soil, partial characterization of the α-amylase has been arried out. The optimum pH for the dextrinogenic activity of the enzyme was found to be 6.5 and the maximum reaction rate was achieved at a temperature range of 55° to 65℃. Calcium ion was recognized to have a slight effect in activating the enzyme, while heavy metal salts especially ferrous and cupric ions showed a remarkable inhibition effect. The enzyme was best protected from thermal denaturation at pH 8.0 with tris-HC1 buffer; inactivation was rapid at higher or lower pH values. Furthermore, its thermal stability was greatly increased by calcium ion, particulary at the final concentration of 1 X 10^(-²) mole in the reaction mixture. The Km value for the α-amylase was calculated to be 2.17 X 10^(-⁴)g per ml and the energy of activation for the dextrinogenic reaction to be 12, 000±580 cal per mole.
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