Composite cryogel with immobilized concanavalin A for affinity chromatography of glycoproteins.
(2012) In Journal of Separation Science 35(21). p.2978-2985- Abstract
- Composite cryogels containing porous adsorbent particles were prepared under cryogelation conditions. The composites with immobilized concanavalin A (Con A) were used for capturing glycoproteins. Adsorbent particles were introduced into the structure in order to improve the capacity and to facilitate the handling of the particles. The monolithic composite cryogels were produced from suspensions of polyvinyl alcohol particles and porous adsorbent particles and cross-linked under acidic conditions at sub-zero temperature. The cryogels were epoxy activated and Con A was immobilized as an affinity ligand. Binding and elution of horseradish peroxidase (HRP) was studied in batch experiment and in a chromatographic setup. Increasing adsorbent... (More)
- Composite cryogels containing porous adsorbent particles were prepared under cryogelation conditions. The composites with immobilized concanavalin A (Con A) were used for capturing glycoproteins. Adsorbent particles were introduced into the structure in order to improve the capacity and to facilitate the handling of the particles. The monolithic composite cryogels were produced from suspensions of polyvinyl alcohol particles and porous adsorbent particles and cross-linked under acidic conditions at sub-zero temperature. The cryogels were epoxy activated and Con A was immobilized as an affinity ligand. Binding and elution of horseradish peroxidase (HRP) was studied in batch experiment and in a chromatographic setup. Increasing adsorbent concentration in composite cryogels will increase ligand density, which therefore enhances the amount of bound HRP from 0.98 till 2.9 (milligram enzyme per milliliter of gel) in the chromatographic system. The material was evaluated in 10 cycles for binding and elution of HRP. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3123693
- author
- Hajizadeh, Solmaz LU ; Kirsebom, Harald LU ; Leistner, Andre and Mattiasson, Bo LU
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Separation Science
- volume
- 35
- issue
- 21
- pages
- 2978 - 2985
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000310250300020
- pmid:23002026
- scopus:84867856871
- pmid:23002026
- ISSN
- 1615-9314
- DOI
- 10.1002/jssc.201200433
- language
- English
- LU publication?
- yes
- id
- 20a6875b-d464-4056-9ea6-3caf3a11c67a (old id 3123693)
- date added to LUP
- 2016-04-01 11:06:45
- date last changed
- 2022-04-20 17:06:07
@article{20a6875b-d464-4056-9ea6-3caf3a11c67a, abstract = {{Composite cryogels containing porous adsorbent particles were prepared under cryogelation conditions. The composites with immobilized concanavalin A (Con A) were used for capturing glycoproteins. Adsorbent particles were introduced into the structure in order to improve the capacity and to facilitate the handling of the particles. The monolithic composite cryogels were produced from suspensions of polyvinyl alcohol particles and porous adsorbent particles and cross-linked under acidic conditions at sub-zero temperature. The cryogels were epoxy activated and Con A was immobilized as an affinity ligand. Binding and elution of horseradish peroxidase (HRP) was studied in batch experiment and in a chromatographic setup. Increasing adsorbent concentration in composite cryogels will increase ligand density, which therefore enhances the amount of bound HRP from 0.98 till 2.9 (milligram enzyme per milliliter of gel) in the chromatographic system. The material was evaluated in 10 cycles for binding and elution of HRP.}}, author = {{Hajizadeh, Solmaz and Kirsebom, Harald and Leistner, Andre and Mattiasson, Bo}}, issn = {{1615-9314}}, language = {{eng}}, number = {{21}}, pages = {{2978--2985}}, publisher = {{John Wiley & Sons Inc.}}, series = {{Journal of Separation Science}}, title = {{Composite cryogel with immobilized concanavalin A for affinity chromatography of glycoproteins.}}, url = {{http://dx.doi.org/10.1002/jssc.201200433}}, doi = {{10.1002/jssc.201200433}}, volume = {{35}}, year = {{2012}}, }