ArticleMolecules (Basel, Switzerland)2014
Surface-functionalized hyperbranched poly(amido acid) magnetic nanocarriers for covalent immobilization of a bacterial γ-glutamyltranspeptidase.
Article in Molecules (Basel, Switzerland), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- A Novel Platform Featuring Nanomagnetic Ligand Fishing Based on Fixed-Orientation Immobilized Magnetic Beads for Screening Potential Cyclooxygenase-2 Inhibitors fromMolecules (Basel, Switzerland) · 2024Article
- Immobilization of E. coli expressing γ-glutamyltranspeptidase on its surface for γ-glutamyl compound production.AMB Express · 2023Article
- Bacterial Gamma-Glutamyl Transpeptidase, an Emerging Biocatalyst: Insights Into Structure-Function Relationship and Its Biotechnological Applications.Frontiers in microbiology · 2021Review
- Affinity Immobilization of a Bacterial Prolidase onto Metal-Ion-Chelated Magnetic Nanoparticles for the Hydrolysis of Organophosphorus Compounds.International journal of molecular sciences · 2019Article
- Novel Application of Magnetic Protein: Convenient One-Step Purification and Immobilization of Proteins.Scientific reports · 2017Article
- Special Issue: Enzyme Immobilization 2016.Molecules (Basel, Switzerland) · 2017Article
- Biosafety of the Novel Vancomycin-loaded Bone-like Hydroxyapatite/Poly-amino Acid Bony Scaffold.Chinese medical journal · 2016Article
- Editorial: Special issue--Enzyme immobilization.Molecules (Basel, Switzerland) · 2014Article
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Authors and funding
6 authors.
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Abstract
In this study, we synthesized water-soluble hyperbranched poly(amido acid)s (HBPAAs) featuring multiple terminal CO2H units and internal tertiary amino and amido moieties and then used them in conjunction with an in situ Fe2+/Fe3+ co-precipitation process to prepare organic/magnetic nanocarriers comprising uniformly small magnetic iron oxide nanoparticles (NP) incorporated within the globular HBPAAs. Transmission electron microscopy revealed that the HBPAA-γ-Fe2O3 NPs had dimensions of 6-11 nm, significantly smaller than those of the pristine γ-Fe2O3 (20-30 nm). Subsequently, we covalently immobilized a bacterial γ-glutamyltranspeptidase (BlGGT) upon the HBPAA-γ-Fe2O3 nanocarriers through the formation of amide linkages in the presence of a coupling agent. Magnetization curves of the HBPAA-γ-Fe2O3/BlGGT composites measured at 300 K suggested superparamagnetic characteristics, with a saturation magnetization of 52 emu g⁻¹. The loading capacity of BlGGT on the HBPAA-γ-Fe2O3 nanocarriers was 16 mg g⁻¹ support; this sample provided a 48% recovery of the initial activity. The immobilized enzyme could be recycled 10 times with 32% retention of the initial activity; it had stability comparable with that of the free enzyme during a storage period of 63 days. The covalent immobilization and stability of the enzyme and the magnetization provided by the HBPAA-γ-Fe2O3 NPs suggests that this approach could be an economical means of depositing bioactive enzymes upon nanocarriers for BlGGT-mediated bio-catalysis.
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