Publication | Closed Access
Novel magnetic nanoparticles for the hydrolysis of starch with <i>Bacillus licheniformis</i> α‐amylase
39
Citations
33
References
2011
Year
NanoparticlesMagnetic PropertiesEngineeringPolymer-based MagnetBio-based NanomaterialsPolysaccharideChemistryEnzyme ImmobilizationMagnetic MaterialsFerrofluidNovel Magnetic NanoparticlesEnzyme ActivityHybrid MaterialsPolymer ChemistryNanoparticle CharacterizationBiocatalysisAdsorption AmountBiomolecular EngineeringNatural SciencesPolymer ScienceBiotechnologyImmobilized EnzymeNanomagnetism
Abstract Novel magnetic nanoparticles with an average size of 350–400 nm with N ‐methacryloyl‐( L )‐phenylalanine (MAPA) as a hydrophobic monomer were prepared by the surfactant‐free emulsion polymerization of 2‐hydroxyethyl methacrylate, MAPA, and magnetite in an aqueous dispersion medium. MAPA was synthesized from methacryloyl chloride and L ‐phenylalanine methyl ester. The specific surface area of the nonporous magnetic nanoparticles was found to be 580 m 2 /g. Magnetic poly[2‐hydroxyethyl methacrylate– N ‐methacryloyl‐( L )‐phenylalanine] nanoparticles were characterized by Fourier transform infrared spectroscopy, electron spin resonance, atomic force microscopy, and transmission electron microscopy. Elemental analysis of MAPA for nitrogen was estimated as 4.3 × 10 −3 mmol/g of nanoparticles. Then, magnetic nano‐poly[2‐hydroxyethyl methacrylate– N ‐methacryloyl‐( L )‐phenylalanine] nanoparticles were used in the adsorption of Bacillus licheniformis α‐amylase in a batch system. With an optimized adsorption protocol, a very high loading of 705 mg of enzyme/g nanoparticles was obtained. The adsorption phenomena appeared to follow a typical Langmuir isotherm. The inverse of enzyme affinity for free amylase (181.82 mg/mL) was higher than that for immobilized enzyme (81.97 mg/mL). Storage stability was found to increase with adsorption. It was observed that the enzyme could be repeatedly adsorbed and desorbed without a significant loss in the adsorption amount or enzyme activity. © 2011 Wiley Periodicals, Inc. J Appl Polym Sci, 2012
| Year | Citations | |
|---|---|---|
Page 1
Page 1