Magnetically modified bacterial cellulose: A promising carrier for immobilization of affinity ligands, enzymes, and cells

0474812 - BC 2018 RIV NL eng J - Článek v odborném periodiku
Baldíková, E. - Pospíšková, K. - Ladakis, D. - Kookos, I.K. - Koutinas, A.A. - Šafaříková, Miroslava - Šafařík, Ivo
Magnetically modified bacterial cellulose: A promising carrier for immobilization of affinity ligands, enzymes, and cells.
Materials Science & Engineering C-Materials for Biological Applications. Roč. 71, February (2017), s. 214-221. ISSN 0928-4931. E-ISSN 1873-0191
Institucionální podpora: RVO:60077344
Klíčová slova: bacterial cellulose * Komagataeibacter sucrofermentans * copper phthalocyanine * crystal violet * yeast cells * trypsin
Obor OECD: Bioproducts (products that are manufactured using biological material as feedstock) biomaterials, bioplastics, biofuels, bioderived bulk and fine chemicals, bio-derived novel materials
Impakt faktor: 5.080, rok: 2017

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 388 mg/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.
Trvalý link: http://hdl.handle.net/11104/0277690