Article ID Journal Published Year Pages File Type
10160932 Biochemical Engineering Journal 2005 8 Pages PDF
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 Cu2+ for the purpose of binding affinity and stability. The prepared affinity adsorbent was notated as β-CDcl-IDA-Cu2+. Excellent binding as well as de-binding was achieved within an extremely short period of time. Consequently, β-CDcl-IDA-Cu2+ 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.
Related Topics
Physical Sciences and Engineering Chemical Engineering Bioengineering
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