Protein immobilization to alumina supports: I. Characterization of alumina‐organophosphate ligand interactions and use in the attachment of papain
- 20 December 1992
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 40 (11) , 1319-1327
- https://doi.org/10.1002/bit.260401105
Abstract
The chemical adsorption of organic phosphate compounds to alumina has been used to create surface linkers for protein immobilization. A number of particulate alumina supports were screened for their physical properties and ability to bind organic phosphate compounds. Two aluminas, termed C1 and CPC, were selected based on their suitability for subsequent testing as protein immobilization supports. Papain was successfully immobilized to these supports when derivatized with phosphate compounds containing free terminal carboxyl groups. Protein binding was enhanced when support carboxyl groups were activated with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. The level of papain immobilization was dependent upon the length of the linker used and the mass of protein exposed to the support. © 1992 John Wiley & Sons, Inc.Keywords
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