Properties of a novel thermostable glucoamylase from the hyperthermophilic archaeon Sulfolobus solfataricus in relation to starch processing |
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Authors: | Kim Mi-Sun Park Jong-Tae Kim Young-Wan Lee Hee-Seob Nyawira Rose Shin Hyoun-Seung Park Cheon-Seok Yoo Sang-Ho Kim Yong-Ro Moon Tae-Wha Park Kwan-Hwa |
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Institution: | National Research Laboratory for Functional Food Carbohydrate and Center for Agricultural Biomaterials, Seoul National University, Sillim-dong, Kwanak-gu, Seoul 151-742, Korea. |
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Abstract: | A gene (ssg) encoding a putative glucoamylase in a hyperthermophilic archaeon, Sulfolobus solfataricus, was cloned and expressed in Escherichia coli, and the properties of the recombinant protein were examined in relation to the glucose production process. The recombinant glucoamylase was extremely thermostable, with an optimal temperature at 90 degrees C. The enzyme was most active in the pH range from 5.5 to 6.0. The enzyme liberated beta-d-glucose from the substrate maltotriose, and the substrate preference for maltotriose distinguished this enzyme from fungal glucoamylases. Gel permeation chromatography and sedimentation equilibrium analytical ultracentrifugation analysis revealed that the enzyme exists as a tetramer. The reverse reaction of the glucoamylase from S. solfataricus produced significantly less isomaltose than did that of industrial fungal glucoamylase. The glucoamylase from S. solfataricus has excellent potential for improving industrial starch processing by eliminating the need to adjust both pH and temperature. |
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