Magnetically modified bacterial cellulose: A promising carrier for immobilization of affinity ligands, enzymes, and cells
Language English Country Netherlands Media print-electronic
Document type Journal Article
PubMed
27987701
DOI
10.1016/j.msec.2016.10.009
PII: S0928-4931(16)31654-X
Knihovny.cz E-resources
- Keywords
- Bacterial cellulose, Copper phthalocyanine, Crystal violet, Komagataeibacter sucrofermentans, Trypsin, Yeast cells,
- MeSH
- Acetobacteraceae chemistry MeSH
- Polysaccharides, Bacterial chemistry MeSH
- Cellulose chemistry MeSH
- Enzymes, Immobilized chemistry MeSH
- Gentian Violet chemistry MeSH
- Cells, Immobilized cytology MeSH
- Indoles chemistry MeSH
- Magnetics MeSH
- Drug Carriers chemistry MeSH
- Organometallic Compounds chemistry MeSH
- Saccharomyces cerevisiae cytology MeSH
- Cattle MeSH
- Trypsin chemistry MeSH
- Animals MeSH
- Check Tag
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Polysaccharides, Bacterial MeSH
- Cellulose MeSH
- copper phthalocyanine MeSH Browser
- Enzymes, Immobilized MeSH
- Gentian Violet MeSH
- Indoles MeSH
- Drug Carriers MeSH
- Organometallic Compounds MeSH
- Trypsin MeSH
Bacterial cellulose (BC) produced by Komagataeibacter sucrofermentans was magnetically modified using perchloric acid stabilized magnetic fluid. Magnetic bacterial cellulose (MBC) was used as a carrier for the immobilization of affinity ligands, enzymes and cells. MBC with immobilized reactive copper phthalocyanine dye was an efficient adsorbent for crystal violet removal; the maximum adsorption capacity was 388mg/g. Kinetic and thermodynamic parameters were also determined. Model biocatalysts, namely bovine pancreas trypsin and Saccharomyces cerevisiae cells were immobilized on MBC using several strategies including adsorption with subsequent cross-linking with glutaraldehyde and covalent binding on previously activated MBC using sodium periodate or 1,4-butanediol diglycidyl ether. Immobilized yeast cells retained approximately 90% of their initial activity after 6 repeated cycles of sucrose solution hydrolysis. Trypsin covalently bound after MBC periodate activation was very stable during operational stability testing; it could be repeatedly used for ten cycles of low molecular weight substrate hydrolysis without loss of its initial activity.
Department of Chemical Engineering University of Patras 26504 Patras Rio Greece
Global Change Research Institute CAS Na Sadkach 7 370 05 Ceske Budejovice Czech Republic
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