Dithiocarbamate to modify magnetic graphene oxide nanocomposite (Fe 3 O 4 -GO): A new strategy for covalent enzyme (lipase) immobilization to fabrication a new nanobiocatalyst for enzymatic hydrolysis of PNPD

Heidarizadeh, Mohammad; Doustkhah, Esmail; Rostamnia, Sadegh; Rezaei, Parisa Fathi; Darvishi, Farshad; Zeynizadeh, Behzad

doi:10.1016/j.ijbiomac.2017.03.152

Cited by 94 publications

(25 citation statements)

References 29 publications

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“…In a general procedure, silica nanoparticles powder was first functionalized by 3-aminopropyltriethysilane (APTES) and subsequently, the amino-functionalized silica nanoparticles (SiO 2 -NH 2 ) were reacted with sodium chloroacetate. Specifically, 1 g of silica nanoparticles were dispersed in toluene (15 mL) for 30 min at room temperature and then to the dispersion, APTES (10 mmol, 2.25 mL) was added to the reaction under same conditions and the temperature was raised to 90 °C and stir for 48 h. Finally, the product was collected by filtration on filter paper, washed with EtOH and dried in an oven at 80 °C for 2 h. Afterward, the as-obtained SiO 2 /PrNH 2 was dispersed by ultrasonic irradiation in ethanol (20 mL) containing sodium chloroacetate (30 mmol, 3.5 g), triethylamine (TEA, 10 mL) and EtOH (15 mL) and the reaction was kept at reflux conditions for 48 h. Then, the solid was centrifuged and washed with pure EtOH for several times and dried at 80 °C for 2 h [33]. Finally, the material was dispersed in water and its pH was adjusted to 6.5 by diluted HCl (10 −4 M) and collected by centrifugation and dried at 100 °C.…”

Section: Methodsmentioning

confidence: 99%

Noncovalent Immobilization of Yarrowia lipolytica Lipase on Dendritic-Like Amino Acid-Functionalized Silica Nanoparticles

et al. 2019

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Immobilization of enzymes is a promising approach for the cost-effective application of enzymes. Among others, noncovalent but unleachable approaches for immobilization are one of the most favorable and crucial approaches. Herein, silica nanoparticles are modified by (3-aminopropyl)triethoxysilane (APTES) to generate amino-functionalized silica nanoparticles. Then, the amine functionalities are converted to bifunctional amino acid via post-modification that has zwitterionic properties. This nanostructure with the new functional theme is employed to immobilize Yarrowia lipolytica lipase at room temperature with no further post-modification or cross-linking. This immobilization method is further compared with the metal chelate-based immobilization approach on the same support. The biocatalytic activity of the immobilized lipase is examined under various conditions. The encapsulation of lipase through amino acid-functionalized silica nanoparticles exhibited enhanced stability for the immobilized lipase at higher temperatures and unneutral pHs.

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Section: Methodsmentioning

confidence: 99%

Noncovalent Immobilization of Yarrowia lipolytica Lipase on Dendritic-Like Amino Acid-Functionalized Silica Nanoparticles

et al. 2019

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“…A number of scaffolds have been utilized in enzyme and TiO 2 immobilization, including cellulose nanofibers [20,21], ceramic membrane [22], graphene oxide membrane [23], silica nanoparticles [24], magnetic nanoparticles [25][26][27] and artificial polymers [28][29][30]. Among the carriers of Lac and TiO 2 , electrospun nanofibrous membranes have been proven to have great potential in wastewater treatment, especially with the addition of adsorbent material in the process of electrospinning [31].…”

Section: Introductionmentioning

confidence: 99%

TiO2 Sol-Gel Coated PAN/O-MMT Multi-Functional Composite Nanofibrous Membrane Used as the Support for Laccase Immobilization: Synergistic Effect between the Membrane Support and Enzyme for Dye Degradation

Wang

et al. 2020

Polymers

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Removal of a triphenylmethane dye (crystal violet, CV) by a simultaneous enzymatic-photocatalytic-adsorption treatment was investigated in this work. A desirable synergistic effect on dye treatment was achieved by decorating laccase (Lac) onto the surface of TiO2 sol-gel coated polyacrylonitrile/organically modified montmorillonite (PAN/O-MMT) nanofibers prepared by electrospinning. The assembly of Lac on the surface of PAN/O-MMT/TiO2 nanofibers was confirmed by confocal laser scanning microscope (CLSM). In comparison with free Lac, the immobilized Lac showed better pH, temperature and operational stabilities, reaching highest relative activity at an optimum pH of 3 and optimum temperature of 50 °C. Therefore, the immobilized Lac displayed a higher degradation efficiency of CV at an initial dye concentration of 100 mg/L, an optimum pH of 4.5 and temperature at 60 °C. Under UV illumination, the CV removal efficiency was further improved by ~20%. These results demonstrated that the Lac-immobilized PAN/O-MMT/TiO2 composite nanofibers with a combined effect between the immobilized enzyme and the polymeric support have potential for industrial dye degradation.

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“…The engineered BNPs are exciting prospects for drug targeting [5], bio-catalysis [6], biochemical separation [7] and bioremediation [8]. Compared with existing chemical immobilization technologies [9, 10], surface engineering of BNPs is highly advantageous. The functional BNPs usually assemble under mild physiological conditions in a single step, avoiding the requirement for additional external agents.…”

Section: Introductionmentioning

confidence: 99%

In vivo immobilization of an organophosphorus hydrolyzing enzyme on bacterial polyhydroxyalkanoate nano-granules

Yang

Xiao

et al. 2019

Microb Cell Fact

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Background Polyhydroxyalkanoate (PHA) are nano-granules naturally produced by bacteria. Two types of proteins, PHA synthase (PhaC) and phasins (PhaPs), are attached to the PHA surface by covalent and hydrophobic interactions. Utilizing these anchored proteins, functionalized PHA nano-granules displaying proteins of interest can be easily prepared by fermentation. Results In this study, a one-step fabrication method was developed for stable and efficient immobilization of an organophosphorus degrading enzyme on PHA nano-granules. The nano-biocatalysts were produced in recombinant Escherichia coli cells into which the polyhydroxyalkanoate synthesis pathway from Cupriavidus necator had been introduced. Two different strategies, covalent attachment and hydrophobic binding, were investigated by fusing bacterial organophosphorus anhydride hydrolase (OPAA4301) with PhaC and PhaP, respectively. Using both methods, the tetrameric enzyme successfully self-assembled and was displayed on the PHA surface. The display density of the target fused enzyme was enhanced to 6.8% of total protein on decorated PHA by combination of covalent and non-covalent binding modes. Immobilization of the enzyme on PHA granules resulted in higher catalytic efficiency, increased stability and excellent reusability. The kcat values of the immobilized enzymes increased by threefold compared to that of the free enzyme. The pH stability under acidic conditions was significantly enhanced, and the immobilized enzyme was stable at pH 3.0–11.0. Furthermore, more than 80% of the initial enzyme activity retained after recycling ten times. Conclusions This study provides a promising approach for cost-efficient in vivo immobilization of a tetrameric organophosphorus degrading enzyme. The immobilization process expands the utility of the enzyme, and may inspire further commercial developments of PHA nano-biocatalysts. As revealed by our results, combination of covalent and non-covalent binding is recommended for display of enzymes on PHA granules.

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Dithiocarbamate to modify magnetic graphene oxide nanocomposite (Fe 3 O 4 -GO): A new strategy for covalent enzyme (lipase) immobilization to fabrication a new nanobiocatalyst for enzymatic hydrolysis of PNPD

Cited by 94 publications

References 29 publications

Noncovalent Immobilization of Yarrowia lipolytica Lipase on Dendritic-Like Amino Acid-Functionalized Silica Nanoparticles

Noncovalent Immobilization of Yarrowia lipolytica Lipase on Dendritic-Like Amino Acid-Functionalized Silica Nanoparticles

TiO2 Sol-Gel Coated PAN/O-MMT Multi-Functional Composite Nanofibrous Membrane Used as the Support for Laccase Immobilization: Synergistic Effect between the Membrane Support and Enzyme for Dye Degradation

In vivo immobilization of an organophosphorus hydrolyzing enzyme on bacterial polyhydroxyalkanoate nano-granules

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