Improving catalytic activity of laccase immobilized on the branched polymer chains of magnetic nanoparticles under alternating magnetic field

Xia, Tingting; Wan, Lin; Liu, Chun‐Zhao; Chen, Guo

doi:10.1002/jctb.5325

Cited by 12 publications

(13 citation statements)

References 30 publications

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“…The reaction rate of catechol oxidation catalyzed by immobilized laccase was determined according to the method described by Xia et al (2018) . To carry out this determination, the desired amount of immobilized laccase was added to 10 mM catechol dissolved in sodium acetate buffer (0.1 M, pH 5.0) under an alternating magnetic field at 25°C.…”

Section: Methodsmentioning

confidence: 99%

“…Among different supports, magnetic nanoparticles are good candidates for enzyme immobilization due to superparamagnetism, low toxicity, and the ease with which they separate ( Ou et al, 2019 ). With the assistance of an alternating magnetic field, magnetic supports can oscillate in the direction of a magnetic field and behave like microscopic stirrers, which can increase mass transfer in enzymatic reaction and result in higher catalytic efficiency for magnetic immobilized enzymes ( Liu et al, 2015 ; Xia et al, 2018 ). To carry out the continuous operation, a magnetically stabilized fluidized bed (MSFB) has been used in wastewater treatment and chiral compounds synthesis with enzymes immobilized on magnetic supports ( Wang et al, 2012 ; Ou et al, 2019 ).…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of Laccase on Magnetic Chelator Nanoparticles for Apple Juice Clarification in Magnetically Stabilized Fluidized Bed

Wang¹,

Owusu-Fordjour²,

Xu³

et al. 2020

Front. Bioeng. Biotechnol.

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The juice clarification, one of the key steps in juice processing, suffers from haze formation that results from residual phenolic compounds. In this study, laccase was immobilized on metal-chelated magnetic silica nanoparticles and used for continuous juice clarification in a magnetically stabilized fluidized bed (MSFB) assisted by alternating magnetic field. Furthermore, a new combination of laccase catalysis and microfiltration was developed for the juice clarification. Immobilized laccase provided high relative activity within broader ranges of pH and temperature compared to the free enzyme. Magnetic immobilized laccase exhibited the best reaction rate of 12.1 μmol g –1 min –1 for catechol oxidation under the alternating magnetic field of 400 Hz, 60 Gs. No activity loss occurred in immobilized laccase after 20 h continuous operation of juice treatment in MSFB under an alternating magnetic field. Combined with microfiltration after treatment with immobilized laccase, the color of apple juice was decreased by 33.7%, and the light transmittance was enhanced by 20.2%. Furthermore, only 16.3% of phenolic compounds and 15.1% of antioxidant activity was reduced for apple juice after the clarification. By this combination strategy, the apple juice possessed good freeze–thaw and thermal stability.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Immobilization of Laccase on Magnetic Chelator Nanoparticles for Apple Juice Clarification in Magnetically Stabilized Fluidized Bed

Wang¹,

Owusu-Fordjour²,

Xu³

et al. 2020

Front. Bioeng. Biotechnol.

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“…However, the relative conversion dropped below 50% after 8 cycles and 39.5 ± 0.7% at the tenth run. A study by Xia et al (2018) showed that laccase immobilized on polyethylenimine modified amine-functionalized Fe 3 O 4 nanoparticles retained 85% of its initial activity after six consecutive operation cycles. Laccase-immobilized dendritic nanofibrous membranes maintained a high bisphenol A conversion rate of up to 79% even after four filtration cycles (Koloti et al 2018).…”

Section: Laccase Recyclability During Dmelc Is Competitive With Immobmentioning

confidence: 99%

Dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization

Zhang

Wang

et al. 2020

AMB Expr

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Laccase is a versatile multicopper oxidase that holds great promise for many biotechnological applications. For such applications, it is essential to explore good biocatalytic systems for high activity and recyclability. The feasibility of membrane enclosed enzymatic catalysis (MEEC) for enzyme recycling with laccase was evaluated. The dialysis membrane enclosed laccase catalysis (DMELC) was tested for the conversion of the non-phenolic model substrate 2,2′-Azino-bis(3-ethylbenzthiazoline-6-sulfonate) (ABTS). Trametes versicolor laccase was found to be completely retained by the dialysis membrane during the process. The ABTS total conversion after DMELC reached the same values as the batch reaction of the enzyme in solution. The efficiency of DMELC conversion of ABTS under different process conditions including shaking speed, temperature, ABTS concentration and pH was investigated. The repetitive dialysis minimally affected the activity and the protein content of the enclosed laccase. DMELC retained 70.3 ± 0.8% of its initial conversion after 5 cycles. The usefulness of MEEC extends to other enzymes with the benefit of superior activity of an enzyme in solution and the recyclability which is normally only obtained with immobilized enzymes.

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“…The optimal stirring rate was 900 rpm and the optimal pH was 8 (Figure 4a-c). High stirring rate can promote mass transfer in biphasic enzymatic catalysis [47,48]. However, the further increase of stirring rate from 900 to 1000 rpm could result in fracture of the nanocomposite [36,49] and the dissociation of 2-Melm or PLA1, resulting in a significant reduction of catalytic activity.…”

Section: Enzymatic Activities Of 2-melm@pla1/msncmentioning

confidence: 99%

“…The optimal stirring rate was 900 rpm and the optimal pH was 8 (Figure 4a-c). High stirring rate can promote mass transfer in biphasic enzymatic catalysis [47,48].…”

Section: Enzymatic Activities Of 2-melm@pla 1 /Msncmentioning

confidence: 99%

Alkaline Modification of a Metal–Enzyme–Surfactant Nanocomposite to Enhance the Production of L-α-glycerylphosphorylcholine

Cao

et al. 2019

Catalysts

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Microenvironment modification within nanoconfinement can maximize the catalytic activity of enzymes. Phospholipase A1 (PLA1) has been used as the biocatalyst to produce high value L-α-glycerylphosphorylcholine (L-α-GPC) through hydrolysis of phosphatidylcholine (PC). We successfully developed a simple co-precipitation method to encapsulate PLA1 in a metal–surfactant nanocomposite (MSNC), then modified it using alkalescent 2-Methylimidazole (2-Melm) to promote catalytic efficiency in biphasic systems. The generated 2-Melm@PLA1/MSNC showed higher catalytic activity than PLA1/MSNC and free PLA1. Scanning electron microscopy and transmission electron microscopy showed a typical spherical structure of 2-Melm@PLA1/MSNC at about 50 nm, which was smaller than that of 2-Melm@MSNC. Energy disperse spectroscopy, N2 adsorption isotherms, Fourier transform infrared spectrum, and high-resolution X-ray photoelectron spectroscopy proved that 2-Melm successfully modified PLA1/MSNC. The generated 2-Melm@PLA1/MSNC showed a high catalytic rate per unit enzyme mass of 1.58 μmol mg-1 min-1 for the formation of L-α-GPC. The 2-Melm@PLA1/MSNC also showed high thermal stability, pH stability, and reusability in a water–hexane biphasic system. The integration of alkaline and amphiphilic properties of a nanocomposite encapsulating PLA1 resulted in highly efficient sequenced reactions of acyl migration and enzymatic hydrolysis at the interface of a biphasic system, which cannot be achieved by free enzyme.

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Improving catalytic activity of laccase immobilized on the branched polymer chains of magnetic nanoparticles under alternating magnetic field

Abstract: BACKGROUND: Immobilization of laccase may cause more or less mass transfer limitation in practical applications. In order to enhance the reaction rate, there is great interest in developing an effective way to increase the rate of diffusion in reactions catalyzed by immobilized laccase.

Cited by 12 publications

References 30 publications

Immobilization of Laccase on Magnetic Chelator Nanoparticles for Apple Juice Clarification in Magnetically Stabilized Fluidized Bed

Immobilization of Laccase on Magnetic Chelator Nanoparticles for Apple Juice Clarification in Magnetically Stabilized Fluidized Bed

Dialysis membrane enclosed laccase catalysis combines a controlled conversion rate and recyclability without enzyme immobilization

Alkaline Modification of a Metal–Enzyme–Surfactant Nanocomposite to Enhance the Production of L-α-glycerylphosphorylcholine

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