Co-Immobilization of Enzymes and Magnetic Nanoparticles by Metal-Nucleotide Hydrogelnanofibers for Improving Stability and Recycling

Li, Chunfang; Jiang, Shuhui; Zhao, Xinshu; Liang, Hao

doi:10.3390/molecules22010179

Cited by 45 publications

(23 citation statements)

References 57 publications

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“…Storage stability is an important advantage of immobilized enzymes over their free counterparts since some previous investigations have already reported that free biocatalysts can usually lose their activities fairly quickly during storage [52,53,54,55]. In our case, the storage stability of free and immobilized His 6 - Ec PepQ was compared and the relevant research results are shown in Figure 6A.…”

Section: Resultsmentioning

confidence: 87%

Affinity Immobilization of a Bacterial Prolidase onto Metal-Ion-Chelated Magnetic Nanoparticles for the Hydrolysis of Organophosphorus Compounds

Wang

Chi

et al. 2019

IJMS

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In this study, silica-coated magnetic nanoparticles (SiMNPs) with isocyanatopropyltriethoxysilane as a metal-chelating ligand were prepared for the immobilization of His6-tagged Escherichia coli prolidase (His6-EcPepQ). Under one-hour coupling, the enzyme-loading capacity for the Ni2+-functionalized SiMNPs (NiNTASiMNPs) was 1.5 mg/mg support, corresponding to about 58.6% recovery of the initial activity. Native and enzyme-bound NiNTASiMNPs were subsequently characterized by transmission electron microscopy (TEM), superparamagnetic analysis, X-ray diffraction, and Fourier transform infrared (FTIR) spectroscopy. As compared to free enzyme, His6-EcPepQ@NiNTASiMNPs had significantly higher activity at 70 °C and pH ranges of 5.5 to 10, and exhibited a greater stability during a storage period of 60 days and could be recycled 20 times with approximately 80% retention of the initial activity. The immobilized enzyme was further applied in the hydrolysis of two different organophosphorus compounds, dimethyl p-nitrophenyl phosphate (methyl paraoxon) and diethyl p-nitrophenyl phosphate (ethyl paraoxon). The experimental results showed that methyl paraoxon was a preferred substrate for His6-EcPepQ and the kinetic behavior of free and immobilized enzymes towards this substance was obviously different. Taken together, the immobilization strategy surely provides an efficient means to deposit active enzymes onto NiNTASiMNPs for His6-EcPepQ-mediated biocatalysis.

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Section: Resultsmentioning

confidence: 87%

Affinity Immobilization of a Bacterial Prolidase onto Metal-Ion-Chelated Magnetic Nanoparticles for the Hydrolysis of Organophosphorus Compounds

Wang

Chi

et al. 2019

IJMS

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“…Further developing this co-immobilizationc oncept, Li and co-workersu sed Zn 2 + /AMP hydrogels to immobilize candida rugosa lipase (CRL) as well as Fe 3 O 4 nanoparticles. [107] CRLa nd citrate-capped Fe 3 O 4 nanoparticles (CA-Fe 3 O 4 )w ere encapsulated by incorporating them during the synthesis of the CP (Figure 9C). The main function of the CA-Fe 3 O 4 was to provide a high surface area for maximum enzyme loading.…”

Section: Enzyme Encapsulationmentioning

confidence: 99%

Self‐Assembly of Nucleobase, Nucleoside and Nucleotide Coordination Polymers: From Synthesis to Applications

Lopez

Liu

2017

ChemNanoMat

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With multiple metal binding sites, nucleobases, nucleosides, and nucleotides form various coordination polymers (CPs) with metal ions. These self-assembled materials are very interesting for their simplicity to prepare, highly tunable structure and properties, and excellent biocompatibility.P olymerization is achieved under ambient conditions without the need of free radical initiators or UV light. Different nucleobases have different metal-binding preferences, but in general most of their coordinations ites prefer borderline or soft metals, while the phosphate groups in the nucleotides prefer hard Lewis acids. In this Focus Review,r ecent developments in this fielda re summarized startingf rom the synthesis and characterization of these CPs. Various metal ions includingg old, silver,l anthanides, zinc, copper, and iron are individually reviewed, and each metal brings its own property into the CP materials.While mostoft hese materials are non-crystalline nanoparticles, under certainc onditions crystalline metal-organic frameworks (MOFs) andh ydrogels can also be prepared. The applicationso fs uch CPs are then described including enzyme entrapment,d rug loading and delivery, biosensor development, catalysis, coating of nanoparticles, and luminescence. Finally,f uture research opportunities of this field are discussed.

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“…Some researchers focused on the immobilization behavior of the enzyme, including chemical bonding, physical adsorption, and entrapment [ 13 , 14 , 15 ]. Others studied ways to immobilize as many enzyme molecules as possible through surface modification of the membrane [ 9 , 16 ]. However, the decrease in enzyme activity induced by aggregation of the enzyme molecules is often ignored [ 12 , 17 ].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Enzymes on a Phospholipid Bionically Modified Polysulfone Gradient-Pore Membrane for the Enhanced Performance of Enzymatic Membrane Bioreactors

et al. 2018

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Enzymatic membrane bioreactors (EMBRs), with synergistic catalysis-separation performance, have increasingly been used for practical applications. Generally, the membrane properties, particularly the pore structures and interface interactions, have a significant impact on the catalytic efficiency of the EMBR. Therefore, a biomimetic interface based on a phospholipid assembled onto a polysulfone hollow-fiber membrane with perfect radial gradient pores (RGM-PSF) has been prepared in this work to construct a highly efficient and stable EMBR. On account of the special pore structure of the RGM-PSF with the apertures decreasing gradually from the inner side to the outer side, the enzyme molecules could be evenly distributed on the three-dimensional skeleton of the membrane. In addition, the supported phospholipid layer in the membrane, prepared by physical adsorption, was used for the immobilization of the enzymes, which provides sufficient linkage to prevent the enzymes from leaching but also accommodates as many enzyme molecules as possible to retain high bioactivity. The properties of the EMBR were studied by using lipase from Candida rugosa for the hydrolysis of glycerol triacetate as a model. Energy-dispersive X-ray and circular dichroism spectroscopy were employed to observe the effect of lecithin on the membrane and structure changes in the enzyme, respectively. The operational conditions were investigated to optimize the performance of the EMBR by testing substrate concentrations from 0.05 to 0.25 M, membrane fluxes from 25.5 to 350.0 L·m−2·h−1, and temperatures from 15 to 55 °C. As a result, the obtained EMBR showed a desirable performance with 42% improved enzymatic activity and 78% improved catalytic efficiency relative to the unmodified membrane.

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Co-Immobilization of Enzymes and Magnetic Nanoparticles by Metal-Nucleotide Hydrogelnanofibers for Improving Stability and Recycling

Cited by 45 publications

References 57 publications

Affinity Immobilization of a Bacterial Prolidase onto Metal-Ion-Chelated Magnetic Nanoparticles for the Hydrolysis of Organophosphorus Compounds

Affinity Immobilization of a Bacterial Prolidase onto Metal-Ion-Chelated Magnetic Nanoparticles for the Hydrolysis of Organophosphorus Compounds

Self‐Assembly of Nucleobase, Nucleoside and Nucleotide Coordination Polymers: From Synthesis to Applications

Immobilization of Enzymes on a Phospholipid Bionically Modified Polysulfone Gradient-Pore Membrane for the Enhanced Performance of Enzymatic Membrane Bioreactors

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