Organic solvent and pH induced alteration of product specificity of CGTase |
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Authors: | Kyo-Sun Park Hyun-Mi Oh Hui-Woog Choe Chung-Ung Park Kang-Min Lee |
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Affiliation: | (1) Department of Molecular Biology, Chonbuk National University, Chonju, Korea;(2) Department of Chemistry, Chonbuk National University, Chonju, Korea |
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Abstract: | Cyclodextrin glucanotransferase [CGTase, E.C.2.4.1.19] is an extracellular enzyme, which catalyzes the formation of α−, β−, γ− CDs from starch. Their proportions of formations depend on enzyme sources and reaction conditions. To understand what determines the product specificity of CGTases, we examined the alteration of product specificity of CGTase fromBacillus macerans by organic solvents and pH. At acidic pH range less than pH 6 where the enzyme was unstable, the ratio of α−/β-CD production was increased 4 times more than that at neutral pH range. As we increased the concentration of 2-butanol, α−/β-CD ratio was proportionally increased but/ratio remained constant. The α−/β-CD ratio of products was increased in the reaction media which yielded low products. |
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Keywords: | Cyclodextrin glucanotransferase Product specificity Organic solvents Cyclodextrin |
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