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- Publisher
- de Gruyter
- Copyright
- ©2018 IUPAC & De Gruyter. This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. For more information, please visit: http://creativecommons.org/licenses/by-nc-nd/4.0/
- ISSN
- 0033-4545
- eISSN
- 1365-3075
- DOI
- 10.1515/pac-2017-0710
- Publisher site
- See Article on Publisher Site
Abstract
AbstractCellulose monolith with a hierarchically porous morphology was utilized as a novel solid support for enzyme immobilization. After a series of modifications, succinimidyl carbonate (SC)-activated cellulose monolith (SCCL monolith) was obtained and it was employed to immobilize a model enzyme (horseradish peroxidase, HRP) through covalent bonding. The HRP immobilization capacity on SCCL monolith was calculated as 21.0 mg/g. The thermal stability measurement illustrated that the immobilized HRP exhibited a largely improved thermal resistance compared to its free counterpart. The reusability of the immobilized HRP was investigated, and it could be reused at least 10 cycles without significant activity loss. Therefore, cellulose monolith is found to be an ideal solid support for enzyme immobilization.
Journal
Pure and Applied Chemistry – de Gruyter
Published: Jun 27, 2018
Keywords: cellulose monolith; enzyme immobilization; hierarchical structure; POLYCHAR-25; thermally induced phase separation