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• W2024793651 abstract "The cgt gene encoding α-cyclodextrin glycosyltransferase (α-CGTase) from Paenibacillus macerans strain JFB05-01 was expressed in Escherichia coli as a C-terminal His-tagged protein. After 90 h of induction, the activity of α-CGTase in the culture medium reached 22.5 U/mL, which was approximately 42-fold higher than that from the parent strain. The recombinant α-CGTase was purified to homogeneity through either nickel affinity chromatography or a combination of ion-exchange and hydrophobic interaction chromatography. Then, the purified enzyme was characterized in detail with respect to its cyclization activity. It is a monomer in solution. Its optimum reaction temperature is 45 °C, and half-lives are approximately 8 h at 40 °C, 1.25 h at 45 °C and 0.5 h at 50 °C. The recombinant α-CGTase has an optimum pH of 5.5 with broad pH stability between pH 6 and 9.5. It is activated by Ca2+, Ba2+, and Zn2+ in a concentration-dependent manner, while it is dramatically inhibited by Hg2+. The kinetics of the α-CGTase-catalyzed cyclization reaction could be fairly well described by the Hill equation." @default.
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• W2024793651 date "2010-05-01" @default.
• W2024793651 modified "2023-10-10" @default.
• W2024793651 title "Extracellular expression and biochemical characterization of α-cyclodextrin glycosyltransferase from Paenibacillus macerans" @default.
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• W2024793651 doi "https://doi.org/10.1016/j.carres.2010.02.002" @default.
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