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- W4252077030 abstract "Thermoanaerobacter cyclomaltodextrin glucanotransferase (CGTase) was immobilized using different supports and immobilization methods to study the effect on activity recovery. The enzyme covalently attached into glyoxyl-silica showed low activity recovery of 1.5%. The hydrophobic adsorption of the enzyme on Octadecyl-Sepabeads yielded also low activity recovery, 3.83%, and the enzyme could easily leak from the support at low ionic strength, although the immobilization yield was satisfactory, approximately 76%. The CGTase encapsulated in a sol-gel matrix gave an activity recovery of 6.94% and maximum cyclization activity at 60 °C, at pH 6.0. The half-time life at 60 °C, pH 6.0, in the presence of substrate was 100 min, which was lower than that of the free enzyme. The best activity recovery in this work (6.94%) is approximately five times smaller than that obtained previously using glyoxyl-agarose as support and covalent immobilization. Thus, the best support and method we tested so far for immobilization of CGTase is covalent attachment on glyoxyl-agarose." @default.
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- W4252077030 date "2007-01-01" @default.
- W4252077030 modified "2023-10-03" @default.
- W4252077030 title "Methods and Supports for Immobilization and Stabilization of Cyclomaltodextrin Glucanotransferase from Thermoanaerobacter" @default.
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- W4252077030 doi "https://doi.org/10.1007/978-1-60327-526-2_31" @default.
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