Enzyme Immobilization on Ion Exchangers by Forming an Enzyme Coating with Transglutaminase as a Crosslinker

1992 ◽  
Vol 56 (8) ◽  
pp. 1323-1324 ◽  
Author(s):  
Yoshiro Kamata ◽  
Erika Ishikawa ◽  
Masao Motoki
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.


2020 ◽  
Author(s):  
Jia Shen Chew ◽  
Ken Chi Lik Lee ◽  
THI THANH NHA HO

<p>Lee and coworkers offers a kind of new concept to enzyme immobilization and explores its suitability in the context of miniaturisation and high-throughput screening. Here, polystyrene-immobilized ketoreductases are compared with its non-immobilized counterparts in terms of conversion and stereoselectivity (both determined by chiral HPLC), and the study indicates that the BioBeads perform similarly (sometimes slightly more selective) which may be useful whenever defined micro-scale amounts of biocatalysts were required in high-throughput experiment settings.</p>


2002 ◽  
Vol 1 (4) ◽  
pp. 577-588
Author(s):  
Eveline Popovici ◽  
Igor Cretescu ◽  
Elena Botezatu ◽  
Gabriela Soreanu ◽  
Alina Mihaela Hanu ◽  
...  

2013 ◽  
Vol 12 (1) ◽  
pp. 137-145 ◽  
Author(s):  
Iuliana Rogoveanu Radosavlevici ◽  
Dan Niculae Robescu
Keyword(s):  

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