Preparation of nanoparticles which contains histidine for immobilization of Trametes versicolor laccase

Çorman, M. Emin; Öztürk, Nevra; Bereli, Nilay; Akgöl, Sinan; Deni̇zli̇, Adil

doi:10.1016/j.molcatb.2009.12.017

Cited by 33 publications

(13 citation statements)

References 25 publications

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“…These characteristics together with the broad substrate specificity make laccase from T. versicolor a promising enzyme for industrial applications [11]. During the last decades, new and attractive methodologies involving its oxidation capacity have been used in different areas such as: textile industries [12][13][14], pulp and paper industry [15,16], soil bioremediation [17], nanobiotechnology and biosensors [18][19][20], synthetic chemistry [21], and cosmetics [22].…”

Section: Introductionmentioning

confidence: 99%

Laccase recovery with aqueous two-phase systems: Enzyme partitioning and stability

Silvério

Rodrı́guez

Tavares

et al. 2013

Journal of Molecular Catalysis B: Enzymatic

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a b s t r a c tIn this work, the potential of several aqueous two-phase systems (ATPS) for laccase recovery was evaluated. For this purpose, different types of ATPS were prepared and the partition coefficient of pure commercial laccase was determined in each one, at 23 • C. A total of 21 ATPS were investigated: 12 composed by a polymer and a salt and 9 composed by two different polymers. For polymer-salt ATPS, different compositions of the same biphasic system were also studied. Laccase partition coefficients (K) obtained were used to conclude about ATPS effectiveness for this enzyme recovery. According to the results, it was found that UCON-phosphate salts (K ≤ 0.604), PEG-Li 2 SO 4 (K = 2.081) and PES-dextran (K = 1.911) ATPS can be interesting options for laccase extraction, with laccase partitioning toward opposite directions. However, the most effective ATPS for laccase extraction was UCON-K 2 HPO 4 , presenting K values from 0.272 up to 0.306. UCON is a thermo-separating polymer which facilitates its recovery and reutilization. Additionally, for the first time, laccase stability in different ATPS was investigated by incubating the enzyme in each equilibrium phase during a week, at room temperature. The results obtained showed that UCON-sulfate salts, UCON-NaH 2 PO 4 and UCON-KH 2 PO 4 ATPS are not recommended for laccase recovery since a high loss of activity was observed: approximately 88% for sulphates and 80% for both dihydrogen phosphates. The best stability results were obtained with PEG-sulfate salts. For these ATPS, laccase stability remained similar or improved over time.

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Section: Introductionmentioning

confidence: 99%

Laccase recovery with aqueous two-phase systems: Enzyme partitioning and stability

Silvério

Rodrı́guez

Tavares

et al. 2013

Journal of Molecular Catalysis B: Enzymatic

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“…Lentinula edodes laccase immobilized onto chitosan (pH 4.0) [20], Pycnoporus sanguineus laccase immobilized onto magnetic chitosan microspheres (pH 3.0) [21] but lower than that of Trametes versicolor laccase immobilized onto platinum nanoparticles (pH 6.5) [22]. The optimum temperature of biosensor was 35 • C, which is lower than that immobilized on magnetic chitosan microspheres (55 • C) [21] but higher than that on carbon paste modified graphite electrode [23] and nanoparticles (25 • C) [24]. Polyaniline being a good thermal insulator for enzymes might have provided the microenvironment to protect the enzyme from environmental and thermal variations, which favours the repeated use of MnO 2 NPs/cMWCNT/PANI electrode [12].…”

Section: Optimization Of Experimental Conditions Of Biosensormentioning

confidence: 94%

An amperometric biosensor based on laccase immobilized onto MnO2NPs/cMWCNT/PANI modified Au electrode

Rawal

Chawla

Malik

et al. 2012

International Journal of Biological Macromolecules

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“…Immobilization techniques are using for several enzymes even biomedical or not (Esquisabel et al, 2006). Synthetic polymers can be formed as composites for enzyme immobilization experiments especially medical enzymes such as lysozyme (Akgöl et al, 2010), catalase (Akgöl et al, 2009; Çorman, Öztürk, Tüzmen, et al, 2010; Öztürk et al, 2008), laccase (Çorman, Öztürk, Bereli, et al, 2010), and l ‐asparaginase (Andrade et al, 2014; Cruz et al, 1993; Manuela Gaspar et al, 1998) and so on.…”

Section: Usability Of Composite Nanomaterials In Biomedical Engineeringmentioning

confidence: 99%

The usage of composite nanomaterials in biomedical engineering applications

Akgöl

Ulucan‐Karnak

Kuru

et al. 2021

Biotech & Bioengineering

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Nanotechnology is still developing over the decades and it is commonly used in biomedical applications with the design of nanomaterials due to the several purposes. With the investigation of materials on the molecular level has increased the develop composite nanomaterials with exceptional properties using in different applications and industries. The application of these composite nanomaterials is widely used in the fields of textile, chemical, energy, defense industry, electronics, and biomedical engineering which is growing and developing on human health. Development of biosensors for the diagnosis of diseases, drug targeting and controlled release applications, medical implants and imaging techniques are the research topics of nanobiotechnology. In this review, overview of the development of nanotechnology and applications which is use of composite nanomaterials in biomedical engineering is provided.

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Preparation of nanoparticles which contains histidine for immobilization of Trametes versicolor laccase

Cited by 33 publications

References 25 publications

Laccase recovery with aqueous two-phase systems: Enzyme partitioning and stability

Laccase recovery with aqueous two-phase systems: Enzyme partitioning and stability

An amperometric biosensor based on laccase immobilized onto MnO2NPs/cMWCNT/PANI modified Au electrode

The usage of composite nanomaterials in biomedical engineering applications

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