Adsorption of trypsin onto magnetic ion‐exchange beads of poly(glycidylmethacrylate‐co‐ethyleneglycoldimethacrylate)

Abstract

Magnetic beads were prepared from glycidyl methacrylate (GMA), and ethyleneglycol dimethylmethacrylate (EGDMA) in the presence of Fe 3 O 4 nanopowder via suspension polymerization. The magnetic beads were characterized by surface area measurement, electron spin resonance (ESR), and scanning electron microscopy (SEM). ESR data revealed that the beads were highly super-paramagnetic. The effects of contact time, pH, ionic strength, and temperature on the adsorption process have been studied. Adsorption equilibrium was established in about 120 min. The maximum adsorption of trypsin on the magnetic beads was obtained as 84.96 mg g 21 at around pH 7.0. At increased ionic strength, the contribution of the electrostatic component to the overall binding decreased, and so the adsorption capacity. The experimen-tal equilibrium data obtained trypsin adsorption onto magnetic beads fitted well to the Langmuir isotherm model. The result of kinetic analyzed for trypsin adsorption onto magnetic ion-exchange beads showed that the second order rate equation was favorable. It was observed that after six adsorption-elution cycle, magnetic beads can be used without significant loss in trypsin adsorption capacity. Finally, the magnetic beads were used for separation of bovine serum albumin (BSA) and trypsin from binary solution in a batch system.

Functionalization of Regenerated Cellulose Membrane via Surface Initiated Atom Transfer Radical Polymerization for Boron Removal from Aqueous Solution

“…Following the polymerization, a new peak appears at 1726 cm −1 in the RC-PGMA (spectrum b), which is attributed to the ester CO stretching vibrations in −COO − . , The vibration at 1452 cm −1 corresponds to the −CH 2 scissoring band of PGMA . Three obvious characteristic bands of epoxide groups at 906, 848, and 759 cm −1 are also found in the spectrum. , Meanwhile, the intensity of hydroxyl characteristic peak at 3300−3400 cm −1 for RC membranes greatly decreases, which can be explained as follows.…”

“…Following the polymerization, a new peak appears at 1726 cm À1 in the RC-PGMA (spectrum b), which is attributed to the ester CdO stretching vibrations in ÀCOO À . 25,26 The vibration at 1452 cm À1 corresponds to the ÀCH 2 scissoring band of PGMA. 26 Three obvious characteristic bands of epoxide groups at 906, 848, and 759 cm À1 are also found in the spectrum.…”

“…25,26 The vibration at 1452 cm À1 corresponds to the ÀCH 2 scissoring band of PGMA. 26 Three obvious characteristic bands of epoxide groups at 906, 848, and 759 cm À1 are also found in the spectrum. 27,28 Meanwhile, the intensity of hydroxyl characteristic peak at 3300À3400 cm À1 for RC membranes greatly decreases, which can be explained as follows.…”

Enhanced adsorption of arsenate onto a natural polymer-based sorbent by surface atom transfer radical polymerization

“…6 shows the FTIR spectra of the CTS-MG before and after arsenic adsorption. For the pristine adsorbent, the peaks at 1642 and 1726 cm À1 represent the amide C@O stretching vibrations in -NHCO-and ester C@O stretching vibrations in carbonyl groups, respectively [38,39]. The peaks at 1084 and 881 cm À1 correspond to the C-N stretching vibration in the amine group and C-O stretching vibration in secondary alcohols [40].…”

pH-Sensitive Magnetic Ion Exchanger for Protein Separation

“…To solve these problems, magnetic separation technology has been introduced and widely investigated in the field of protein separation in recent years, − because it can be used to selectively recover desired proteins from liquors containing biological particulates in a rapid and easy way . By now, many investigations that focused on combining magnetic particles with ion-exchange support or synthesizing magnetic ion exchangers and have achieved success to some extent. − However, because the surface electric properties of most traditional ion-exchange supports were usually unalterable or unable to reverse through the changes of pH, the supports could not be controlled to selectively adsorb and release proteins through self-transformation.…”