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E. P. Segura-Ceniceros, K. R. Dabek, A. D. Ilyiná
Invertase immobilization on nylon-6 activated by hydrochloric acid in the
presence of glutaraldehyde as cross-linker
Abstract
The objective of this work was to immobilize
invertase on glutaraldehyde activated nylon-6 by covalent bonding. This method
of nylon-6 modification was chosen due to its chemical structure containing the
functional carboxyl (–COOH) and amine (–NH2)
groups. Amine groups bind with glutaraldehyde, which in turn binds with
invertase. Nylon-6 discs were produced by extrusion (the disk diameter (D) was
30 mm and the thickness (E) was 2 mm). The discs had nonporous but fairly rough
surfaces. The discs were treated with different concentrations of HCl and
activated with glutaraldehyde. On an average, 0.58 mg of invertase was
immobilized onto each gram of a disc. The percent yield of immobilization of
the invertase varied between 57 and 60%. Immediately after immobilization
51–64% activity was retained, 23–43% after 3 months and 18–31% after 6 months
of storage at 4°C. The immobilized invertase was used in 12 cycles of reaction
without a decrease in activity.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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