Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9616765 | Journal of Molecular Catalysis B: Enzymatic | 2005 | 5 Pages |
Abstract
Bacillus macerans cyclodextrin glycosyltransferase (CGTase) fused with 10 lysine residues at its C-terminus (CGTK10ase) was immobilized onto a cation exchanger by ionic interaction and used to produce α-cyclodextrin (CD) from soluble starch. Poly-lysine fused immobilization increased the Vm of the immobilized CGTase by 40% without a change in Km. The activation energies of thermal deactivation (Ea) were 41.4, 28.1, and 25.9 kcal molâ1, respectively, for soluble wild-type (WT) CGTase, soluble CGTK10ase, and immobilized CGTK10ase, suggesting destabilization of CGTase by poly-lysine fusion and immobilization onto a cation exchanger. Maximum α-CD productivity of 539.4 g lâ1 hâ1 was obtained with 2% soluble starch solution which was constantly fed at a flow rate of 4.0 ml minâ1 (D = 240 hâ1) in a continuous operation mode of a packed-bed reactor. The operational half-life of the packed-bed enzyme reactor was estimated 12 days at 25 °C and pH 6.0.
Related Topics
Physical Sciences and Engineering
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Catalysis
Authors
Chan-Su Rha, Dae-Hee Lee, Sung-Gun Kim, Won-Ki Min, Seong-Goo Byun, Dae-Hyuk Kweon, Nam Soo Han, Jin-Ho Seo,