Immobilization of Glucose Oxidase on Fe3O4 Magnetic Nanoparticles and its Application in the Removal of Acid Yellow 12

Aber, Soheil; Mahmoudikia, Ehsan; Karimi, Afzal; Mahdizadeh, Fatemeh

doi:10.1007/s11270-016-2754-x

Cited by 28 publications

(14 citation statements)

References 12 publications

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“…As a general rule, Q increased as a function of t f , C HRP , and T. Table 3 shows that a 5‐time increase of C HRP (from 0.1 to 0.5 mg/ml) produced about a 2‐fold increase in Q values. Similar behavior was reported by Aber et al, 40 who immobilized glucose oxidase onto Fe 3 O 4 . With regard to the functionalization time (t f ), Table 3 shows that a noticeable enhancement of Q from 0.20 ± 0.03 to 0.30 ± 0.03 mgHRP/cm 2 was obtained when t f increased from 35 to 95 min.…”

Section: Resultssupporting

confidence: 88%

Immobilization of horseradish peroxidase onto electrospun polyurethane nanofiber matrices

Urrea

Caracciolo

Haure

et al. 2021

Polymers for Advanced Techs

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In this work, horseradish peroxidase (HRP) was immobilized onto polyurethane nanofiber membranes. The following variables were optimized to maximize the surface density of grafted HRP (Q): NaClO functionalization time (tf), immobilization time (ti), HRP concentration of the immobilization solution (CHRP), and immobilization temperature (T). Catalytic activity was evaluated using the decolorization reaction of Orange II (OII). A statistical analysis of SEM images demonstrates that fiber diameters (d) of native (M), AGE‐modified (MA), and HRP immobilized (MAH) electrospun membranes obeyed a log‐normal distribution and that the effects of the NaClO activation procedure, and the use of MAH membranes in OII oxidation during 4 h on the fiber size were negligible. Although obtained membranes at 40°C (MAH9540) presented the highest Q, matrices obtained at 20°C (MAH9520) exhibited the highest catalytic activity, indicating that HRP was partially inactivated during the immobilization at 40°C. Reusability tests demonstrated that membranes retained between 11% and 33% of their initial enzyme activity after a total reaction time between 4 and 8 h.

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Section: Resultssupporting

confidence: 88%

Immobilization of horseradish peroxidase onto electrospun polyurethane nanofiber matrices

Urrea

Caracciolo

Haure

et al. 2021

Polymers for Advanced Techs

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show abstract

“…In another study, Aber et al immobilized glucose oxidase by adsorption on unmodified MNPs and used the resulting system for decolourization of Acid Yellow 12. After 15 catalytic cycles the immobilized glucose oxidase retained more than 90% of its initial properties [84]. Atacan et al used magnetic nanoparticles, pre-treated with gallic acid, for the covalent immobilization of trypsin.…”

Section: Magnetic Particlesmentioning

confidence: 99%

A General Overview of Support Materials for Enzyme Immobilization: Characteristics, Properties, Practical Utility

et al. 2018

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In recent years, enzyme immobilization has been presented as a powerful tool for the improvement of enzyme properties such as stability and reusability. However, the type of support material used plays a crucial role in the immobilization process due to the strong effect of these materials on the properties of the produced catalytic system. A large variety of inorganic and organic as well as hybrid and composite materials may be used as stable and efficient supports for biocatalysts. This review provides a general overview of the characteristics and properties of the materials applied for enzyme immobilization. For the purposes of this literature study, support materials are divided into two main groups, called Classic and New materials. The review will be useful in selection of appropriate support materials with tailored properties for the production of highly effective biocatalytic systems for use in various processes.

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“…Candida antarctica lipase immobilized on modified magnetic nanoparticles showed a high level of reusability when used for production of biodiesel from waste cooking oil (Mehrasbi, Mohammadi, Peyda, & Mohammadi 2017). High reusability was also observed when the immobilized glucose oxidase was used for the decolorization of acid yellow 12 (Aber, Mahmoudikia, Karimi, & Mahdizadeh 2016). The immobilization of trypsin on modified Fe 3 O 4 magnetic nanoparticles for hydrolysis of bovine serum albumin was also reported in literature (Atacan, Çakıroğlu, & Özacar 2016).…”

Section: Magnetic Materialsmentioning

confidence: 66%

The Enzyme Immobilization: Carriers and Immobilization methods

Spasojević¹,

Prodanović²,

Pantić³

et al. 2020

JEPM

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Strategies based on the enzyme application are increasingly replacing the conventionalchemical procedures because of their efficiency, quicker performance and environmentalprotection. However, natural enzymes can rarely be used in industrysince their beneficial features cannot endure the industrial conditions. Additionaldrawbacks of natural enzymes are their inhibition by reaction products and difficultyto be removed from the reaction mixture. The most promising techniqueto substantially improve the enzyme properties, such as activity, pH, thermal andorganic-solvent stability, reusability and storage stability, in non-natural environmentsis by the enzyme immobilization. In this review different techniques usedto immobilize enzymes to inert carriers were summarized. Different materials ofboth the organic and inorganic origin were used as carriers for the enzyme immobilization.A class of new materials where the enzyme performance was enhancedby combining different classical materials and shaping in specific forms was alsosummarized.

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Immobilization of Glucose Oxidase on Fe3O4 Magnetic Nanoparticles and its Application in the Removal of Acid Yellow 12

Cited by 28 publications

References 12 publications

Immobilization of horseradish peroxidase onto electrospun polyurethane nanofiber matrices

Immobilization of horseradish peroxidase onto electrospun polyurethane nanofiber matrices

A General Overview of Support Materials for Enzyme Immobilization: Characteristics, Properties, Practical Utility

The Enzyme Immobilization: Carriers and Immobilization methods

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