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KMID : 0896219910120010785
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Journal of Daegu Health College
1991 Volume.12 No. 1 p.785 ~ p.799
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Properties of Glucose Isomerase from Arthrobacter sp. KCTC 1877
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Kim Hyang-Ja
Lee Eun-Sook
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Abstract
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Enzymatic properties and characteristics of glucose isomerase from Aarthrobacter sp KCTC 1877 were investigated.
The optimum temperature and pH for the enzyme activity were 70℃ and 8.0, respectively. The enzyme activity was stimulated by Mg^(2+) at 30mM and inhibited strongly by Co^(2+), Cu^(2+), Fe^(2+), Mn^(2+) and Ca^(2+). The enzyme was very stable at high temperature. Pure enzyme was isolated by DEAE cellulose column chromatography with two-stage NaCl gradient elution and visualized as a single band in SDS-acrylamide gel electrophoresis. Km value and Vmax were 0.175(M) and 0.29(㎎/ml/min), respectively. Molecular weight was determined to be about 180,000 by gel filtration and 42,500 by SDS-acrylamide gel electrophoresis, suggesting that the enzyme to be four subunits.
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