Abstract
β-Cyclodextrin (β-CD) was chosen as the matrix material for the affinity binding of α-amylase in this work. β-CD was cross-linked with epichlorohydrin to improve its rigidity. Iminodiacetic acid (IDA), as a ligand, was bond with the cross-linked β-CD to increase the binding affinity for α-amylase. The affinity adsorbent thus prepared was further chelated with Cu 2+ for the purpose of binding affinity and stability. The prepared affinity adsorbent was notated as β-CD cl-IDA- Cu 2+. Excellent binding as well as de-binding was achieved within an extremely short period of time. Consequently, β-CD cl-IDA-Cu 2+ successfully performed its ability on the affinity adsorption towards α-amylase. The adsorbent was also tested by its ability on repeated utilization. The result further confirmed that it could be repeatedly used and maintained the adsorption/desorption performance stably through many batches of operation. In addition, the bound α-amylase after many adsorption batches could be desorbed with a very high efficiency and hence rather high α-amylase activity could be collected.
Original language | English |
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Pages (from-to) | 17-24 |
Number of pages | 8 |
Journal | Biochemical Engineering Journal |
Volume | 23 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2005 Mar 1 |
All Science Journal Classification (ASJC) codes
- Biotechnology
- Environmental Engineering
- Bioengineering
- Biomedical Engineering