In situ synthesized rGO–Fe3O4 nanocomposites as enzyme immobilization support for achieving high activity recovery and easy recycling

Yang, Dong; Wang, Xueyan; Shi, Jiafu; Wang, Xiaoli; Zhang, Shaohua; Han, Pingping; Jiang, Zhongyi

doi:10.1016/j.bej.2015.10.003

Cited by 55 publications

(27 citation statements)

References 49 publications

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“…Thus, magnetic nanoparticles, such as iron oxide and ferric oxide, have been successfully introduced into immobilizing composites. In these studies, functionalized magnetic nanoparticles have been used for immobilization [ 26 ], including graphene-Fe 3 O 4 [ 27 ], silica-Fe 3 O 4 [ 28 ], and polymer grafted-Fe 3 O 4 [ 29 , 30 ]. However, most of these methods are complicated to operate and easily lead to inactivation of the biocatalyst, so a proper immobilization support can improve enzyme operational stability (via multipoint or multisubunit attachment), activity, specificity, lifetimes, productivity, structural rigidity, and even provided reduction of inhibition [ 31 , 32 , 33 , 34 , 35 ].…”

Section: Introductionmentioning

confidence: 99%

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

Li¹,

Jiang

Zhao

et al. 2017

Molecules

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In this paper we report a facile method for preparing co-immobilized enzyme and magnetic nanoparticles (MNPs) using metal coordinated hydrogel nanofibers. Candida rugosa lipase (CRL) was selected as guest protein. For good aqueous dispersity, low price and other unique properties, citric acid-modified magnetic iron oxide nanoparticles (CA-Fe3O4 NPs) have been widely used for immobilizing enzymes. As a result, the relative activity of CA-Fe3O4@Zn/AMP nanofiber-immobilized CRL increased by 8-fold at pH 10.0 and nearly 1-fold in a 50 °C water bath after 30 min, compared to free CRL. Moreover, the immobilized CRL had excellent long-term storage stability (nearly 80% releative activity after storage for 13 days). This work indicated that metal-nucleotide nanofibers could efficiently co-immobilize enzymes and MNPs simultaneously, and improve the stability of biocatalysts.

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Section: Introductionmentioning

confidence: 99%

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

Li¹,

Jiang

Zhao

et al. 2017

Molecules

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“…The VSM magnetic characterization of Fe 3 O 4 /rGO was determined at room temperature, where the magnetization hysteresis loops appear S-like, and saturation magnetization is 59.4 emu as shown in Figure 5. This value is rather lower than the value of the pure nanomagnetic Fe 3 O 4 [30] but higher than those of Fe 3 O 4 /rGO in the reports [31,32]. This low saturation magnetization value of Fe 3 O 4 /rGO in comparison with pure magnetic Fe 3 O 4 may be attributed to the presence of reduced graphene oxide nanosheets and the relatively lower density of magnetic components in the nanocomposites.…”

Section: Journal Of Chemistrymentioning

confidence: 63%

Fe₃O₄/Reduced Graphene Oxide Nanocomposite: Synthesis and Its Application for Toxic Metal Ion Removal

Hoan

Thư

Duc

et al. 2016

Journal of Chemistry

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The synthesis of reduced graphene oxide modified by magnetic iron oxide (Fe3O4/rGO) and its application for heavy metals removal were demonstrated. The obtained samples were characterized by X-ray diffraction (XRD), nitrogen adsorption/desorption isotherms, X-ray photoelectron spectroscopy (XPS), Fourier transform infrared spectroscopy (FT-IR), and magnetic measurement. The results showed that the obtained graphene oxide (GO) contains a small part of initial graphite as well as reduced oxide graphene. GO exhibits very high surface area in comparison with initial graphite. The morphology of Fe3O4/rGO consists of very fine spherical iron nanooxide particles in nanoscale. The formal kinetics and adsorption isotherms of As(V), Ni(II), and Pb(II) over obtained Fe3O4/rGO have been investigated. Fe3O4/rGO exhibits excellent heavy metal ions adsorption indicating that it is a potential adsorbent for water sources contaminated by heavy metals.

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“…The K m values for all monolithic biocatalysts, i.e. HRP@BPEI/PSS cordierite‐H, HRP@LPEI/PSS cordierite‐H and HRP@LPEI/PSS cordierite‐H‐OSi, were in the range 0.157–0.354 mmol L −1 and higher than that of free HRP (0.019 mmol L −1 ), indicating a lower affinity between the reactant and the immobilized HRP . Interestingly, HRP@LPEI/PSS cordierite‐H (0.194 mmol L −1 min −1 ) even exhibited much higher V max when compared with free HRP (0.108 mmol L −1 min −1 ) (Fig.…”

Section: Resultsmentioning

confidence: 95%

Bioinspired synthesis of nanofibers on monolithic scaffolds for enzyme immobilization with enhanced loading capacity and activity recovery

Shi

Zhao

et al. 2019

J of Chemical Tech & Biotech

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BACKGROUND The enzymatic process in continuous flow reactors has become attractive owing to the merits of in‐line purification, improved mixing and mass transfer, etc. However, the construction of continuous flow reactors requires stable and surface‐active monolithic scaffolds for enzyme immobilization. RESULTS In this study, nanofibers of linear polyethyleneimine (LPEI) are formed on the surface of poly(sodium 4‐styrenesulfonate) (PSS)‐treated cordierite honeycomb (named LPEI/PSS cordierite‐H) as monolithic scaffold for enzyme immobilization. The controlled self‐assembly of LPEI ensures the formation of nanofibers (diameters of 20–80 nm) on the surface of cordierite‐H, which roughens the surface and offers many active sites for enzyme loading. The electrostatic interaction between negatively charged enzyme and positively charged LPEI helps the enzyme firmly attach on the surface. The loading capacity of LPEI/PSS cordierite‐H was 1.24 mg g−1. Horseradish peroxidase (HRP)‐loaded LPEI/PSS cordierite‐H (HRP@LPEI/PSS cordierite‐H) exhibited activity recovery of 55.33%, 2‐fold higher than that of HRP‐loaded branched polyethyleneimine (BPEI)/PSS cordierite‐H (HRP@BPEI/PSS cordierite‐H) (23.72%). Furthermore, a silica layer was formed on the surface of HRP@LPEI/PSS cordierite‐H through LPEI‐induced silicification, which could prevent the enzyme from deactivation under extreme conditions. CONCLUSION These monolithic biocatalysts have great potential for applications in wastewater treatment and even in other fields such as pharmaceutical synthesis. © 2019 Society of Chemical Industry

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In situ synthesized rGO–Fe3O4 nanocomposites as enzyme immobilization support for achieving high activity recovery and easy recycling

Cited by 55 publications

References 49 publications

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

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

Fe₃O₄/Reduced Graphene Oxide Nanocomposite: Synthesis and Its Application for Toxic Metal Ion Removal

Bioinspired synthesis of nanofibers on monolithic scaffolds for enzyme immobilization with enhanced loading capacity and activity recovery

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In situ synthesized rGO–Fe3O4 nanocomposites as enzyme immobilization support for achieving high activity recovery and easy recycling

Cited by 55 publications

References 49 publications

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

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

Fe3O4/Reduced Graphene Oxide Nanocomposite: Synthesis and Its Application for Toxic Metal Ion Removal

Bioinspired synthesis of nanofibers on monolithic scaffolds for enzyme immobilization with enhanced loading capacity and activity recovery

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Fe₃O₄/Reduced Graphene Oxide Nanocomposite: Synthesis and Its Application for Toxic Metal Ion Removal