Biocompatible magnetic cellulose–chitosan hybrid gel microspheres reconstituted from ionic liquids for enzyme immobilization

2012 ◽  
Vol 22 (30) ◽  
pp. 15085 ◽  
Author(s):  
Zhen Liu ◽  
Haisong Wang ◽  
Bin Li ◽  
Chao Liu ◽  
Yijun Jiang ◽  
...  
2019 ◽  
Vol 159 ◽  
pp. 133-138 ◽  
Author(s):  
Atsushi Kimura ◽  
Naotsugu Nagasawa ◽  
Mitsumasa Taguchi

SynOpen ◽  
2018 ◽  
Vol 02 (02) ◽  
pp. 0192-0199 ◽  
Author(s):  
A. Grollmisch ◽  
U. Kragl ◽  
J. Großeheilmann

Enzyme immobilization in polymerized ionic liquids (PILs) promises to be a versatile tool for simple recovery and reuse of catalysts. In this study, a raw extract of CalB was encapsulated in poly(VEImBr) and assessed with respect to solvent, temperature, amount of enzyme, leaching behavior, and reusability on the example of the kinetic resolution of rac-1-phenylethanol with vinyl acetate. This immobilization method increased the enzyme activity of the CalB raw extract in comparison to the non-immobilized enzyme. The desired product was synthesized with high enantiomeric excess (ee) and no leaching of active enzyme was observed in the experiments. The immobilization method was compared to Novozyme 435 and Lipozyme RM IM, as commercially available immobilisates. Nonpolar solvents, including n-heptane and n-dodecane, proved to be the best reaction solvents, showing nearly full conversion and high catalytic activities. The encapsulated ­lipase was easily recovered from the reaction mixture and reused for ten cycles.


INEOS OPEN ◽  
2020 ◽  
Author(s):  
N. A. Samoilova ◽  

The enzyme-containing magnetic composites are presented. The magnetic matrix for enzyme immobilization is obtained by sequential application of an amine-containing polysaccharide—chitosan and a synthetic polymer—poly(ethylene-alt-maleic acid) to the magnetite microparticles to form the interpolyelectrolyte complex shell. Then, the enzyme (trypsin) is immobilized by covalent or noncovalent binding. Thus, the suggested composites can be readily obtained in the environmentally friendly manner. The enzyme capacity of the resulting composites reaches 28.0–32.6 mg/g. The maximum hydrolysis rates of the H-Val-Leu-Lys-pNA substrate provided by these composites range within 0.60·10–7–0.77·10–7 M/min.


2011 ◽  
pp. 110923034559006
Author(s):  
Arnd Garsuch ◽  
D. Michael Badine ◽  
Klaus Leitner ◽  
Luiz H. S. Gasparotto ◽  
Natalia Borisenko ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document