High Activity Recovery Research Articles

Co-immobilization of amine dehydrogenase and glucose dehydrogenase for the biosynthesis of (S)-2-aminobutan-1-ol in continuous flow

Reductive amination by amine dehydrogenases is a green and sustainable process that produces only water as the by-product. In this study, a continuous flow process was designed utilizing a packed bed reactor filled with co-immobilized amine dehydrogenase wh84 and glucose dehydrogenase for the highly efficient biocatalytic synthesis of chiral amino alcohols. The immobilized amine dehydrogenase wh84 exhibited better thermo-, pH and solvent stability with high activity recovery. (S)-2-aminobutan-1-ol was produced in up to 99% conversion and 99% ee in the continuous flow processes, and the space-time yields were up to 124.5 g L-1 d-1. The continuous reactions were also extended to 48 h affording up to 91.8% average conversions. This study showcased the important potential to sustainable production of chiral amino alcohols in continuous flow processes.

Support Materials of Organic and Inorganic Origin as Platforms for Horseradish Peroxidase Immobilization: Comparison Study for High Stability and Activity Recovery.

In the presented study, a variety of hybrid and single nanomaterials of various origins were tested as novel platforms for horseradish peroxidase immobilization. A thorough characterization was performed to establish the suitability of the support materials for immobilization, as well as the activity and stability retention of the biocatalysts, which were analyzed and discussed. The physicochemical characterization of the obtained systems proved successful enzyme deposition on all the presented materials. The immobilization of horseradish peroxidase on all the tested supports occurred with an efficiency above 70%. However, for multi-walled carbon nanotubes and hybrids made of chitosan, magnetic nanoparticles, and selenium ions, it reached up to 90%. For these materials, the immobilization yield exceeded 80%, resulting in high amounts of immobilized enzymes. The produced system showed the same optimal pH and temperature conditions as free enzymes; however, over a wider range of conditions, the immobilized enzymes showed activity of over 50%. Finally, a reusability study and storage stability tests showed that horseradish peroxidase immobilized on a hybrid made of chitosan, magnetic nanoparticles, and selenium ions retained around 80% of its initial activity after 10 repeated catalytic cycles and after 20 days of storage. Of all the tested materials, the most favorable for immobilization was the above-mentioned chitosan-based hybrid material. The selenium additive present in the discussed material gives it supplementary properties that increase the immobilization yield of the enzyme and improve enzyme stability. The obtained results confirm the applicability of these nanomaterials as useful platforms for enzyme immobilization in the contemplation of the structural stability of an enzyme and the high catalytic activity of fabricated biocatalysts.

Authorizing of Immunogenicity of Concentrated and Purified Newcastle Disease Virus V4 Strain using Downstream Processing.

Newcastle disease virus (NVD) from the Paramyxoviridae family is a single-stranded negative-sense RNA virus. This infection can affect both domestic poultry and almost all other bird species. It has been considered a very severe difficulty for the poultry industry all over the world. Even though it remains a potential threat to poultry industries, this virus is a powerful oncolytic virus as well. In this study, a process was accomplished to achieve concentrated and highly purified NDV V4 strain particles. Downstream processing of Newcastle virus strain V4 was characterized by amplifying virus in embryonated chicken eggs. Through a sequence of steps, harvesting allantoic fluid, clarification by centrifuge, concentration by ultrafiltration, and size exclusion separation, the reduced volume and pure virus particles were considered for the amount of ovalbumin, hemagglutinin activity, transmission electron microscopy (TEM), electrophoresis, and additionally immunogenicity of prepared antigens. The results presented a high recovery of HA activity in concentrated and purified virus with the removal of ovalbumin and the typical morphology based on TEM. Sepharose CL-4B was determined as the best media among all used resins to purify the virus. Prepared formulations as vaccines demonstrated positive hemagglutinin inhibition for 6 months and stability for 2 years. Strong evidence from organized studies supports the effectiveness of this method in concentrating and purifying intact NDV, which could be valuable in vaccine research, antiserum preparation, or even as an alternative oncotic agent to traditional methods. Despite further studies being conducted, this method can be utilized particularly on a semi-industrial scale to produce various vaccine components.

Combined cross-linking of Rhizomucor miehei lipase and Candida antarctica lipase B for the effective enrichment of omega-3 fatty acids in fish oil

The incorporation of a non-specific lipase and a sn-1,3 specific one in a single immobilized system can be a promising approach for the exploitation of both lipases. A one-step immobilization platform mediated by an isocyanide-based multi-component reaction was applied to create co-cross-linked enzymes (co-CLEs) of lipases from Rhizomucor miehei (sn-1,3 specific) and Candida antarctica (non-specific). Glutaraldehyde was found to be effective cross-linker by producing specific activity of 16.9 U/mg and immobilization yield of 99 %. High activity recovery of up to 404 % was obtained for immobilized derivatives. Leaking experiment showed covalent nature of the cross-linking processes. BSA had considerable effect on the immobilization process, providing 87–100 % immobilization yields and up to 10 times improvement in the specific activity of the immobilized derivatives. Scanning electron microscopy images showed flower-like and rod-like structures for the CLEs prepared by glutaraldehyde and undecanedicarboxylic acid, respectively. The prepared co-CLEs were examined in non-selective enrichment of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) from fish oil, showing capability of releasing up to 100 % of both omega-3 fatty acids within 8 h of the reaction. The reusability of co-CLEs in five successive cycles presented retaining 63–72 % of their initial activities after the fifth reuse cycle in the hydrolysis reaction.

Preparation of cross-linked chitosan magnetic microspheres and immobilization of pectinase

Abstract In this paper, the kinetic model under the influence of each factor is given by investigating the effects of distribution effect, external diffusion effect and internal diffusion effect on the immobilized pectinase reaction system. The magnetic chitosan microspheres were prepared by the reversed-phase suspension cross-linking method, and the effects of the type and amount of cross-linking agent and the ratio of chitosan to magnetic core incorporation on the performance of the magnetic spheres were investigated. Then, the immobilized pectinase was prepared by using cross-linked chitosan magnetic microspheres as a carrier, and an orthogonal test was used to determine the conditions of immobilized enzyme preparation and to study the enzymatic properties and operational stability of immobilized pectinase. The results showed that the transmittance of the magnetic microspheres of this test increased from 32% to 90.79% in 10 min in a magnetic field, but in a gravity field, the transmittance increased from 32.12% to 46.44% in 50 min. The experimentally prepared microspheres exhibit good magnetic responsiveness. The optimum temperature of immobilized pectinase was 50°C, and the remaining enzyme activity was still 61.24% after 6 repetitions. The immobilized pectinase made by crosslinking glutaraldehyde with chitosan magnetic microspheres has a high recovery of enzyme activity and good operational stability, as indicated by this.

Enhanced Laccase Activity and Stability as Crosslinked Enzyme Aggregates on Magnetic Copper Ferrite Nanoparticles for Biotechnological Processes

AbstractHighly stable and reusable magnetic crosslinked enzyme aggregates (m‐CLEAS) of laccase are synthesized with simultaneous improved enzymatic activity. Magnetic copper ferrite nanoparticles (CFNPs) were synthesized by solvothermal procedure with an average size of ~8 nm. The nanometric m‐CLEAS were formed by co‐aggregation of enzyme with CFNPs and crosslinked using glutaraldehyde. Different mass ratios of CFNPs:Laccase were assayed (1 : 2, 1 : 3, and 1 : 6), where 1 : 6 resulted in the highest activity recovery (97 %). The m‐CLEAS showed an average size of ~239 nm, ~24 % enzyme immobilization efficiency, and loading as high as 1.75 g of protein per g of support. As expected, m‐CLEAS oxidized the substrate with a higher transformation rate (kcat) and catalytic efficiency (kcat/Km) than the free enzyme. m‐CLEAS showed superior storage and thermostability compared to free enzyme and non‐magnetic CLEAS. In particular, the m‐CLEAS showed ~150 % and ~100 % residual activity after 30 days of storage at 4 °C and room temperature, respectively. Furthermore, m‐CLEAS showed good recyclability, retaining ~78 % and ~54 % laccase activity after 5 and 10 cycles of reuse, respectively. This work highlights the facile and cost‐effective synthesis of nanometric m‐CLEAS with exceptional storage stability and simultaneously improved laccase activity, making them suitable for a range of green industrial processes.

Robust cross-linked cyclodextrin glucanotransferase from Bacillus lehensis G1 aggregates using an improved cross-linker and a new co-aggregant for the production of cyclodextrins

One of the potentials of carrier-free cross-linked enzyme aggregates (CLEA) immobilization is the ability to be separated and reuse. Yet, it might be impeded by the poor mechanical stability resulting low recyclability. CLEA of CGTase from Bacillus lehensis G1 (CGTase G1-CLEA) using chitosan (CS) as a cross-linker demonstrated high activity recovery however, displayed poor reusability. Therefore, the relationship between mechanical strength and reusability is studied by enhancing the CS mechanical properties and applying a new co-aggregation approach. Herein, CS was chemically cross-linked with glutaraldehyde (GA) and GA was introduced as a co-aggregant (coGA). CGTase G1-CLEA developed using an improved synthesized chitosan-glutaraldehyde (CSGA) cross-linker and a new coGA technique showed to increase its mechanical stability which retained 63.4% and 52.2%, respectively compared to using CS that remained 33.1% of their initial activity after stirred at 500 rpm. The addition of GA impacted the morphology and interaction consequently stabilizing the CLEAs durability in production of cyclodextrins. As a result, the reusability of CGTase G1-CLEA with CSGA and coGA increased by 56.6% and 42.8%, respectively compared to previous CLEA after 5 cycles for 2 h of reaction. This verifies that the mechanical strength of immobilized enzyme influences the improvement of its operational stability.

Removal of bisphenol A by integrated adsorption and biodegradation using immobilized laccase onto defective PCN-224

Environmentally widespread endocrine-disrupting chemicals, such as bisphenol A (BPA), have posed a risk to living things. Laccase, a kind of oxidoreductase, can effectively catalyze the degradation of phenolic compounds like BPA. Herein, a defective metal-organic framework (dPCN-224) with BPA adsorption capability was synthesized and used for laccase immobilization. The material was extensively characterized and successful immobilization of laccase via hydrophobic interaction was confirmed. The immobilization reached an enzyme loading density of 80 mg/g onto dPCN-224 and the laccase@dPCN-224 showed high activity recovery (90.0% vs. free laccase) and increased thermostability, pH tolerance, and organic co-solvent resistance over the free enzyme. Moreover, at various concentrations (0.5–20 mg/L), the BPA removal efficiencies of laccase@dPCN-224 were 3.3–5.0 times higher than those of free laccase due to the cooperative effect of adsorption and enzymatic degradation. The BPA bound on laccase@dPCN-224 could be almost completely biodegraded by adding 0.5 mM of electro-mediator (2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid)). In addition, after five consecutive batch cycles, the BPA removal efficiency of laccase@dPCN-224 kept as high as 98.1% at 5 mg/L BPA. Taken together, the results proved the potential of laccase@dPCN-224 for applications in addressing environmental BPA pollutions.

Biomimetic Laccase-Cu2O@MOF for synergetic degradation and colorimetric detection of phenolic compounds in wastewater

The successful combination of chemo- and enzyme catalysis technologies in wastewater treatment has presented great potentialities as well as challenges for decades. Herein, laccase (Lac) was immobilized on the Cu2[email protected] by covalent linkage to obtain a stable composite (Cu2[email protected]) with synergistic catalytic activity. The Cu2[email protected] with peroxidase-like activity was in situ synthesized by microwave-assisted assembly method. Cu2[email protected] exhibited high activity recovery, large immobilization capacity, remarkable tolerance to pH and high temperature conditions. Based on the prepared mimic multi-enzyme system, Cu2O[email protected] showed broad application prospects in degradation and detection of phenolic compounds. The synergetic catalytic degradation efficiency reached 82.5% in 2h and the limit of detection (LOD) was 0.29 μM in the range of 0-200 μM of 2,4-dichlorophenol (2,4-DCP). Further investigation found that chemo- and enzyme catalysis jointly accelerate the degradation of 2,4-DCP, and the hydroxyl radical (•OH) mediated radical pathway serve a predominant role. Therefore, the chem-enzyme integrated catalyst presented in this work provides a promising platform for organic pollutants degradation and detection by combining the enzymes and Cu2[email protected]

Boosting Chemoselective Hydrogenation of Nitroaromatic via Synergy of Hydrogen Spillover and Preferential Adsorption on Magnetically Recoverable Pt@Fe2 O3.

It is highly desired but challenging to design high performance catalyst for selective hydrogenation of nitro compounds into amino compounds. Herein, a boosting chemoselective hydrogenation strategy on Pt@Fe2 O3 is proposed with gradient oxygen vacancy by synergy of hydrogen spillover and preferential adsorption. Experimental and theoretical investigations reveal that the nitro is preferentially adsorbed onto oxygen vacancy of Pt@Fe2 O3 , meanwhile, the H2 dissociated on Pt nanoparticles and then spillover to approach the nitro for selective hydrogenation (>99% conversion of 4-nitrostyrene, > 99% selectivity of 4-aminostyrene, TOF of 2351h-1 ). Moreover, the iron oxide support endows the catalyst magnetic retrievability. This high activity, selectivity, and easy recovery strategy provide a promising avenue for selective hydrogenation catalysis of various nitroaromatic.

Green synthesis of silica-coated magnetic nanocarriers for simultaneous purification-immobilization of β-1,3-xylanase

Tailoring magnetic nanocarriers with tunable properties is of great significance for the development of multifunctional candidate materials in numerous fields. Herein, we report a one-pot biomimetic silicification-based method for the synthesis of silica-coated magnetic nanoparticles. The synthesis process was mild, low cost, and highly efficient, which took only about 21 min compared with 4.5–120 h in other literature. Then, the carriers had been characterized by VSM, SEM, TEM, XRD, FT-IR, and EDS to confirm their function. To evaluate the usefulness of the carriers, they were adopted to couple the purification and immobilization of β-1,3-xylanase from the cell lysate in a single step with high immobilization yield (92.8 %) and high activity recovery (82.4 %). The immobilized enzyme also retained 58.4 % of the initial activity after 10 cycles and displayed good storage properties, and improved thermal stability, which would be promising in algae biomass bioconversion as well as other diverse applications.

Triazine diphosphonium tetrachloroferrate ionic liquid immobilized on functionalized halloysite nanotubes as an efficient and reusable catalyst for the synthesis of mono-, bis- and tris-benzothiazoles.

Aminopropyl-1,3,5-triazine-2,4-diphosphonium tetrachloroferrate immobilized on halloysite nanotubes [(APTDP)(FeCl4)2@HNT] was prepared and fully characterized using different techniques such as FT-IR, thermogravimetric analysis (TGA), SEM/EDX, elemental mapping, TEM, ICP-OES, and elemental analysis (EA). This nanocatalyst was found to be highly effective for synthesis of various benzothiazole derivatives in excellent yields under solvent-free conditions. Furthermore, bis- and tris-benzothiazoles were smoothly synthesized from dinitrile and trinitrile in the presence of this catalytic system. High yields and purity, easy work up procedure, high catalytic activity (high TON and TOF) and easy recovery and reusability of the catalyst make this method a useful and important addition to the present methodologies for preparation of these vital heterocyclic compounds.

Effect of the Structure of Magnetic Nanocomposite Adsorbents on the Lysozyme Separation Efficiency.

In this study, we prepared various anionic magnetic adsorbents through the carboxyl functionalization of core/shell-structured Fe3O4/SiO2 (FS) particles by either succinic anhydride (FSC), low-molecular-weight (MW 1800) polyacrylic acid (PAA) (FSP1), or high-molecular-weight (MW 100,000) PAA (FSP2), and then, investigated the effect of the structure of adsorbents and operational parameters on their performance for the lysozyme separation. The type and size of functional molecules have significant effects on the surface concentration of functional carboxyl groups onto the adsorbent particles (increase in the order of FSP2 > FSP1 > FSC), and consequently on the adsorption efficiency (AE) (∼100, 98, and 62%, respectively) and adsorption capacity (AC) (∼1000, 980, and 621 mg·g-1, respectively) of the adsorbents. However, the loss of the antibacterial activity of separated lysozyme molecules due to the molecular conformational change increased in the order of FSP2 > FSP1 = FSC, as compared to the free lysozyme. The application of basic buffer solutions for the elution of adsorbed enzyme molecules resulted in more adverse effects on the enzyme activity. The obtained results recommend that FSP1 can be used as a suitable anionic adsorbent for the isolation of positively charged proteins, owing to its high adsorption capacity, excellent reusability, and structural stability, as well as the high purity, structural stability, and activity recovery of the isolated proteins.

Fabrication of Ag/TiO2 membrane on Ti substrate with integral structure for catalytic reduction of 4-nitrophenol

In this work, Ag/TiO2 monolithic membrane catalyst was successfully fabricated on alpha-titanium plate by using a facile two-step method. Firstly, a layer of anatase TiO2 film with nanosheet morphology was formed by the hydrothermal reaction in combination with calcination. After photo-deposition in AgNO3 solution under the ultraviolet irradiation, Ag nanoparticles in metallic state were then deposited on the surface of the as-prepared Ti-based TiO2 film. The catalytic performance of the Ag/TiO2 membrane in the presence of NaBH4 was evaluated by taking p-nitrophenol (4-NP) as a pollutant model. The results indicated that the Ag/TiO2 as a monolithic membrane catalyst exhibited excellent catalytic ability and high stability towards 4-NP degradation. During six consecutive recycling runs, the degradation rates of 4-NP were maintained above 73%, with slight difference. This study shows that the monolithic membrane catalyst Ag/TiO2 is a promising material for the degradation of 4-NP owe to its high activity and easy recovery.

The synergism of lytic polysaccharide monooxygenases with lichenase and their co-immobilization on silica nanospheres for green conversion of lichen biomass

Enzyme-assisted valorization of lichenan represents a green and sustainable alternative to the conventional chemical industry. The recently discovered lytic polysaccharide monooxygenases (LPMOs) are essential components of state-of-the-art enzyme cocktails for lichenin bioconversion. The LPMOs named SpyTag fused LPMOs (AST) from Chaetomium globosum was functionally expressed in E. coli and exhibited 1.25-fold synergism with lichenase, whereas AST alone produced no detectable reducing sugars. HPLC results further confirm that AST does not alter the endogenous hydrolysis mode of lichenase but rather enhances its hydrolysis efficiency by disrupting the long chain of lichenan and releasing more reducing ends. To the best of our knowledge, this was the first report on the synergistic effect of LPMOs and lichenase, which may have great synergistic potential in the conversion of lichen biomass. Furthermore, a novel strategy for the covalently immobilizing AST and lichenase on silica nanoparticles (SNPs) from the cell lysate in a single step was proposed, which exhibited high activity recovery (82.9%) and high immobilization yield (94.8%). After 12 independent runs, about 67.4 % of the initial activity of the immobilized enzymes was retained. The resulted biocatalyst systems exhibited the green and sustainable strategy in the bioconversion of lichen biomass as well as other diverse polysaccharides.

From Batch to Continuous Flow Bioprocessing: Use of an Immobilized γ-Glutamyl Transferase from B. subtilis for the Synthesis of Biologically Active Peptide Derivatives.

γ-Glutamyl-peptides are frequently endowed with biological activities. In this work, “kokumi peptides” such as γ-glutamyl-methionine (1) and γ-glutamyl-(S)-allyl-cysteine (2), as well as the neuroprotective γ-glutamyl-taurine (3) and the antioxidant ophthalmic acid (4), were synthesized through an enzymatic transpeptidation reaction catalyzed by the γ-glutamyl transferase from Bacillus subtilis (BsGGT) using glutamine as the γ-glutamyl donor. BsGGT was covalently immobilized on glyoxyl-agarose resulting in high protein immobilization yield and activity recovery (>95%). Compounds 1–4 were obtained in moderate yields (19–40%, 5–10 g/L) with a variable purity depending on the presence of the main byproduct (γ-glutamyl-glutamine, 0–16%). To achieve process intensification and better control of side reactions, the synthesis of 2 was moved from batch to continuous flow. The specific productivity was 1.5 times higher than that in batch synthesis (13.7 μmol/min*g), but it was not accompanied by a paralleled improvement of the impurity profile.

Engineering silica encapsulated composite of acyltransferase from Mycobacterium smegmatis and MIL-88A: A stability-and activity-improved biocatalyst for N-acylation reactions in water

Here the metal-organic framework material MIL-88A is used to purify and immobilize an acyltransferase from Mycobacterium smegmatis (MsAcT) simultaneously from the broken bacterial liquid. Regarding the possibility that the MsAcT@MIL-88A may display weak stability in its application, a silica layer is further introduced around it as a “shield” to protect the enzyme from degradation. The obtained MsAcT@MIL-88A@silica can exhibit high activity recovery, excellent thermal, pH, and storage stabilities compared with those of MsAcT@MIL-88A. The MsAcT@MIL-88A@silica can also be effectively recycled, and its initial activity of 84.0 % ± 1.2 % can be retained after the 5th cycle for N-acylation reaction in water. More importantly, the MsAcT@MIL-88A@silica can display much higher catalytic activity towards the reactions between ethyl or vinyl esters and aniline than those of free MsAcT and MsAcT@MIL-88A in aqueous media. This study provides a simple and inexpensive strategy to prepare MsAcT@MIL-88A@silica with high activity, stability, and excellent recyclability, and highlights its application potential as a biocatalyst.

Rapid Screening of Lipase Inhibitors in Scutellaria baicalensis by Using Porcine Pancreatic Lipase Immobilized on Magnetic Core–Shell Metal–Organic Frameworks

As for ligand fishing, the current immobilization approaches have some potential drawbacks such as the small protein loading capacity and difficult recycle process. The core–shell metal–organic frameworks composite (Fe3O4-COOH@UiO-66-NH2), which exhibited both magnetic characteristics and large specific surface area, was herein fabricated and used as magnetic support for the covalent immobilization of porcine pancreatic lipase (PPL). The resultant composite Fe3O4-COOH@UiO-66-NH2@PPL manifested a high loading capacity (247.8 mg/g) and relative activity recovery (101.5%). In addition, PPL exhibited enhanced tolerance to temperature and pH after immobilization. Then, the composite Fe3O4-COOH@UiO-66-NH2@PPL was incubated with the extract of Scutellaria baicalensis to fish out the ligands. Eight lipase inhibitors were obtained and identified by UPLC-Q-TOF-MS/MS. The feasibility of the method was further confirmed through an in vitro inhibitory assay and molecular docking. The proposed ligand fishing technique based on Fe3O4-COOH@UiO-66-NH2@PPL provided a feasible, selective, and effective platform for discovering enzyme inhibitors from natural products.

Preparation of cross-linked cell aggregates (CLCAs) of recombinant E. coli harboring glutamate dehydrogenase and glucose dehydrogenase for efficient asymmetric synthesis of l-phosphinothricin

The enzymatic asymmetric synthesis of L-phosphinothricin (L-PPT) from 2-carboxyl-4-(hydroxymethylphosporyl) butyric acid (PPO) is a green and efficient method. In our previous works, we constructed a glutamate dehydrogenase (GluDH) and glucose dehydrogenase (GDH) co-expression strain, Escherichia coli BL21 (DE3)/pETDuet-gludh-gdh, which can asymmetrically reduce PPO to L-PPT. To improve the stability and recyclability of the biocatalyst, we developed a novel method for whole-cell immobilization with cross-linked cell aggregates (CLCAs) and employed immobilized cells in L-PPT production. Montmorillonite was used as a carrier, and dextran polyaldehyde (DPA) was developed as a new cross-linker for cell immobilization. The highest activity recovery (79.2%) was obtained under the following conditions: 20 g/L cell concentration, 0.9% montmorillonite concentration, 1.2% polyethyleneimine (PEI) concentration, and 1.2% DPA concentration. The half-lives of CLCAs were 169.10 h (35 °C), 17.39 h (45 °C), and 10.65 h (55 °C), which were 1.87-, 3.70-, and 10.78-fold than that of free cells, respectively. The CLCAs showed good reusability, retaining over 85% of their initial activities after 10 cycles of utilization. The total yield of L-PPT reached 667 mmol/g cells, and the enantiomeric excess value was more than 99%. The immobilized whole-cell in the form of CLCAs is a valuable biocatalyst for industrial applications.

In‐situ synthesis of magnetic Ce‐BDC@Fe 3 O 4 metal–organic frameworks and their multiple enzyme‐mimicking catalysis

In this work, we used nano-magnetic fluid to magnetize Ce-BDC metal–organic framework (MOF) (BDC = 1,4-benzenedicarboxylic acid) by using Fe3O4-based nano-magnetic fluid grown in situ around a Ce-BDC core. The obtained Ce-BDC@Fe3O4 nanohybrid are mixed-valence MOFs, which could directly oxidize 3,3′,5,5′-tetramethylbenzidine (TMB) into oxTMB without the presence for H2O2. Significantly, the coupling of both Fe3O4 nano-magnetic fluid and Ce-BDC MOF exhibits 0.25-fold higher catalytic activity than Ce-BDC MOF under the same conditions, indicating that the synergistic enhancement occurred in the catalytic activity. This boost is benefited from the more superoxide radicals (O2•−) and then more hydroxyl radica (•OH) with the deposition of Fe3O4 nano-magnetic fluid, which was generated by Ce-BDC@Fe3O4 nanohybrid as both oxidase and peroxidase mimics. In view of high catalytic activity and easy recovery by applying an external magnet, a novel, simple and sensitive Vitamin C colorimetric detection could come true in the wide range (0–120 μM) with a correlation coefficient (R2) of 0.995.