2016
DOI: 10.1177/0263617416661563
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Application of an industrial waste magnetic iron dust as a solid phase support for immobilizing enzyme of industrial applications

Abstract: Magnetic iron dust, a byproduct by many chemical industries that performs the reduction of nitro compounds to amine, was used for laccase immobilization. The characterization of magnetic iron dust was done by X-ray diffraction, Fourier-transform infrared, and dynamic light scattering. Biodegradable polymer, chitosan, was coated on to the magnetic iron dust by reverse phase suspension method, which was confirmed by Fourier-transform infrared analysis. Immobilization of the laccase enzyme was done onto the chito… Show more

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Cited by 3 publications
(2 citation statements)
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“…Metal nanoparticles (NPs) are advantageous support for enzyme immobilization: they are easy to synthesize without using any toxic reagents; their surface is mostly nonporous which facilitates enzyme attachment and there are no internal diffusion limitations; they have extremely high mechanical strength and a high surface-to-volume ratio which makes particle diffusion faster; surface modification is simple which helps the immobilization of a relatively large number of molecules without altering the enzyme orientation during the enzymatic reaction, and finally, this offers the option of easy enzyme recovery. However, enzymes immobilized onto the external surface of adjacent particles may interact with each other and lead to NP agglomeration. This limitation can be overcome by adding polymer coating which helps avoiding enzyme interactions in stirred systems. , Many laccase immobilization studies focused on assessing the nature of enzyme attachment to the NP surface. ,,, Conversely, the role of the NP surface on the enzyme kinetic and thermodynamic parameters was not investigated. Moreover, strategies used for the immobilization of laccase and other enzymes often require modification of the NP surface using ligands (often denoted as stabilizers), which is not ideal as they remain adsorbed after immobilization and therefore influence immobilization efficiency and catalyst performance by decreasing the accessibility of substrates to the enzyme. , …”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…Metal nanoparticles (NPs) are advantageous support for enzyme immobilization: they are easy to synthesize without using any toxic reagents; their surface is mostly nonporous which facilitates enzyme attachment and there are no internal diffusion limitations; they have extremely high mechanical strength and a high surface-to-volume ratio which makes particle diffusion faster; surface modification is simple which helps the immobilization of a relatively large number of molecules without altering the enzyme orientation during the enzymatic reaction, and finally, this offers the option of easy enzyme recovery. However, enzymes immobilized onto the external surface of adjacent particles may interact with each other and lead to NP agglomeration. This limitation can be overcome by adding polymer coating which helps avoiding enzyme interactions in stirred systems. , Many laccase immobilization studies focused on assessing the nature of enzyme attachment to the NP surface. ,,, Conversely, the role of the NP surface on the enzyme kinetic and thermodynamic parameters was not investigated. Moreover, strategies used for the immobilization of laccase and other enzymes often require modification of the NP surface using ligands (often denoted as stabilizers), which is not ideal as they remain adsorbed after immobilization and therefore influence immobilization efficiency and catalyst performance by decreasing the accessibility of substrates to the enzyme. , …”
Section: Introductionmentioning
confidence: 99%
“…16,22 Many laccase immobilization studies focused on assessing the nature of enzyme attachment to the NP surface. 7,9,23,24 Conversely, the role of the NP surface on the enzyme kinetic and thermodynamic parameters was not investigated. Moreover, strategies used for the immobilization of laccase and other enzymes often require modification of the NP surface using ligands (often denoted as stabilizers), which is not ideal as they remain adsorbed after immobilization and therefore influence immobilization efficiency and catalyst performance by decreasing the accessibility of substrates to the enzyme.…”
Section: ■ Introductionmentioning
confidence: 99%