Reversible immobilization of BSA on Cu-chelated PAMAM dendrimer modified iron oxide nanoparticles

Demir, Mine; Şenel, Mehmet; Baykal, A.

doi:10.1016/j.apsusc.2014.07.082

Cited by 12 publications

(3 citation statements)

References 28 publications

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“…19,20 Thus, the concentration of spacers needs to be controlled in relation to the activity of immobilized enzymes. 21 To determine the introduction time, the BSA concentration was maintained at 1.5% (w/v) at reaction times of 2-24 h (Figure 4(b)). The relative activity rapidly increased and reached a maximum within 3 h, with gradual reduction thereafter.…”

Section: Resultsmentioning

confidence: 99%

Development of an enzyme-immobilized support using a polyester woven fabric

Shim

Lee

Song

et al. 2016

Textile Research Journal

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In this study, we aimed to develop an enzyme-immobilized support using polyester woven fabrics and to optimize the development process. We obtained information about the storage stability and reusability of the enzyme and showed the applicability of the polyester woven fabric as an enzyme-immobilized support. In particular, the samples hydrolyzed by hydrogen chloride were treated with N,N'-dicyclohexylcarbodiimide and N-hydroxysuccinimide to activate the surfaces. We evaluated the relative activity of the enzyme immobilization processes, the introduction of spacers, crosslinking and enzyme immobilization and optimized these parameters. The introduction process was controlled to a bovine serum albumin concentration of 1.5% (w/v) and treatment time of 3 h. The crosslinking process was optimized to pH 10.0, a glutaraldehyde concentration of 3% (v/v) and a crosslinking time of 90 min. The immobilization conditions were maintained at pH 8.5, a temperature of 25 C, a time of 45 min and a trypsin concentration of 6% (o.w.f.).Enzyme-immobilized supports have been used in various medical applications, food production processes, ion batteries and filters for waste-water purification. 1,2 Numerous methods for enzyme immobilization on different supports have been described in the literature. Ideal support properties include mechanical stability, hydrophilicity, resistance to microbial attack, porosity and availability at low cost. 2,3 The application of fabrics as immobilization supports could offer several advantages in terms of price and structure compared with other materials such as gels, beads, membranes and films. 2-4 Fabrics are commercially available and relatively cheaper than these or inorganic materials. The fiber-based structures have a high porosity and a large average pore size, so that more enzymes are immobilized, and the immobilized enzymes are protected from the environment. [2][3][4] There are various fabric supports available for enzyme immobilization, which can be classified into natural and synthetic fibers. Natural fibers such as cellulose and chitosan, which have excellent biocompatibility and hydrophilicity, are non-toxic and biodegradable. However, the weak mechanical stability of these natural fibers has greatly limited their application. 3,5 Synthetic fibers such as polylactic acid, polystyrene, polyamide and polyester (polyethylene terephthalate, PET) can be used for enzyme supports due to their good mechanical stability. However, their hydrophobicity is the major disadvantage. It is well known that the hydrophobic interaction between the enzyme and the support is one of the main reasons for protein denaturation. 3,5 One method to address these problems is to introduce spacers between the enzymes and the support. 6 This is a common method to reduce undesirable interactions between the functional groups of support surfaces and the enzyme molecule, and to lower steric hindrance. 7 In particular, the introduction of spacers increases the distance between the enzyme and the hydrophobic surfaces of sy...

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Section: Resultsmentioning

confidence: 99%

Development of an enzyme-immobilized support using a polyester woven fabric

Shim

Lee

Song

et al. 2016

Textile Research Journal

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“…1(a). It indicated the presence of both Fe3O4 ((220), ( 311), ( 400), ( 422), ( 511), ( 440)) [39] and Ag ((111) and ( 200)) [40]. All the diffraction peaks matched well with Ag (JCPDS 87-0720) NPs and Fe3O4 NPs (JCPDS 75-0033).…”

Section: Characterizationsmentioning

confidence: 88%

A Fe3O4@Nico@Ag nanocatalyst for the hydrogenation of nitroaromatics

Kurtan

Amir

Baykal

2015

Chinese Journal of Catalysis

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“…From now on, in order to realize immobilized enzyme regeneration, some approaches had been put forward, such as metal ion chelation, DNA single strand complementation, and direct crosslinking on the inactive enzyme by glutaraldehyde. [40][41][42] There were still some limits in application. For example the enzyme which could not chelate with the metal ion was not suitable in metal ion chelation, DNA complementation would be broken in high temperature situation and magnetic properties could be critically inuenced when excessive inactive enzymes were immobilized on supports.…”

Section: Magnetic Recovery and Regeneration Of Immobilised Trypsinmentioning

confidence: 99%

Thermo-stable hollow magnetic microspheres: preparation, characterization and recyclable catalytic applications

Zeng

et al. 2015

J. Mater. Chem. A

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Thermo-stable hollow magnetic microspheres are prepared by layer-by-layer (LbL) assembly on a uniform melamineformaldehyde resin microsphere template coated by silica and calcination for burning off organic resin. Trypsin is immobilised by their coated polydopamine layer, and nanogolds are assembled onto microspheres by LbL method for catalytic applications. The morphologies and hollow structures are observed by scanning electron microscope and transmission electron microscope. The characteristics are investigated by Fourier transfer infrared spectra, thermogravimetric analysis and vibrating sample magnetometer. Meanwhile, the catalytic characteristics of nanogolds and trypsin are evaluated by ultraviolet-visible spectra. The prepared hollow thermo-stable magnetic microspheres are narrowdispersed with relatively low coefficient of variation, and their size ranging from 0.5 μm to 5.0 μm and saturation magnetization (4-30 emu·g -1 ) can be regulated by different conditions. Combined with magnetic separation and calcination activation or regeneration, these microspheres can also be reused for over 20 times for nanogold catalyst and over 32 times for trypsin catalyst reconjugation without any significant loss in catalytic activity, indicating their considerable potential for recyclable catalytic applications. in our previous research, and importantly, MF organic template could simply be removed by calcination. Recently, MF microspheres with various diameters in the range of 0.5-5.0 μm were synthesised in our research. 23 The size could easily be changed by altering the

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Reversible immobilization of BSA on Cu-chelated PAMAM dendrimer modified iron oxide nanoparticles

Cited by 12 publications

References 28 publications

Development of an enzyme-immobilized support using a polyester woven fabric

Development of an enzyme-immobilized support using a polyester woven fabric

A Fe3O4@Nico@Ag nanocatalyst for the hydrogenation of nitroaromatics

Thermo-stable hollow magnetic microspheres: preparation, characterization and recyclable catalytic applications

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