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            <subfield code="a">10.1016/j.jcis.2018.11.058</subfield>
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            <subfield code="2">sideral</subfield>
            <subfield code="a">109106</subfield>
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            <subfield code="a">ART-2019-109106</subfield>
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            <subfield code="a">eng</subfield>
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        <datafield tag="100" ind1=" " ind2=" ">
            <subfield code="a">Armenia, I.</subfield>
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        <datafield tag="245" ind1=" " ind2=" ">
            <subfield code="a">Enzyme activation by alternating magnetic field: Importance of the bioconjugation methodology</subfield>
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        <datafield tag="260" ind1=" " ind2=" ">
            <subfield code="c">2019</subfield>
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            <subfield code="a">Iron oxide nanoparticles (NPs) are attractive materials for enzyme immobilization and, thanks to their superparamagnetism, can be accessed by remote stimuli. This can be exploited to activate molecules that are not remotely actuable. Here, we demonstrate that thermophilic enzymes chemically linked to NPs can be activated in a “wireless” fashion by an external alternate magnetic field (AMF). To this aim, we have conjugated, with different binding strategies, the thermophilic enzymes a-amylase and L-aspartate oxidase to iron oxide NPs obtaining NP-enzyme systems with activities depending on the different orientations and stretching of the enzymes. Since enzyme activation occurs without a significant rise of the “overall” temperature of the systems, we have speculated a local NP-enzyme heating that does not immediately interest the rest of the solution that remains at relatively low temperature, low enough to allow non-thermophilic enzymes to work together with the NP-conjugated thermophilic enzymes. Nanoactuation of thermophilic enzymes by AMF has potential applications in different fields. Indeed, multi-enzymatic processes with enzymes with different temperature optima could be carried out in the same reaction pot and thermolabile products could be efficiently produced by thermophilic enzymes without suffering for the high temperatures. Moreover, our findings represent a proof of concept of the possibility to achieve a fine-tuning of the enzyme-NP system with the aim to intervene in cell metabolism.</subfield>
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            <subfield code="9">info:eu-repo/grantAgreement/ES/DGA/FSE</subfield>
            <subfield code="9">info:eu-repo/grantAgreement/ES/MINECO/BIO2017-84246-C2-1-R</subfield>
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            <subfield code="u">http://creativecommons.org/licenses/by-nc-nd/3.0/es/</subfield>
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            <subfield code="a">CHEMISTRY, PHYSICAL</subfield>
            <subfield code="b">31 / 158 = 0.196</subfield>
            <subfield code="c">2019</subfield>
            <subfield code="d">Q1</subfield>
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            <subfield code="a">1.45</subfield>
            <subfield code="b">2019</subfield>
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        <datafield tag="593" ind1=" " ind2=" ">
            <subfield code="a">Biomaterials</subfield>
            <subfield code="c">2019</subfield>
            <subfield code="d">Q1</subfield>
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        <datafield tag="593" ind1=" " ind2=" ">
            <subfield code="a">Surfaces, Coatings and Films</subfield>
            <subfield code="c">2019</subfield>
            <subfield code="d">Q1</subfield>
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            <subfield code="a">Electronic, Optical and Magnetic Materials</subfield>
            <subfield code="c">2019</subfield>
            <subfield code="d">Q1</subfield>
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        <datafield tag="593" ind1=" " ind2=" ">
            <subfield code="a">Colloid and Surface Chemistry</subfield>
            <subfield code="c">2019</subfield>
            <subfield code="d">Q1</subfield>
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            <subfield code="a">info:eu-repo/semantics/article</subfield>
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        <datafield tag="700" ind1=" " ind2=" ">
            <subfield code="0">(orcid)0000-0001-6170-4237</subfield>
            <subfield code="a">Grazú Bonavia, M.V.</subfield>
            <subfield code="u">Universidad de Zaragoza</subfield>
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        <datafield tag="700" ind1=" " ind2=" ">
            <subfield code="0">(orcid)0000-0001-6995-4302</subfield>
            <subfield code="a">De Matteis, L.</subfield>
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        <datafield tag="700" ind1=" " ind2=" ">
            <subfield code="a">Ivanchenko, P.</subfield>
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        <datafield tag="700" ind1=" " ind2=" ">
            <subfield code="a">Martra, G.</subfield>
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        <datafield tag="700" ind1=" " ind2=" ">
            <subfield code="a">Gornati, R.</subfield>
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        <datafield tag="700" ind1=" " ind2=" ">
            <subfield code="0">(orcid)0000-0003-1081-8482</subfield>
            <subfield code="a">de la Fuente, J.M.</subfield>
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        <datafield tag="700" ind1=" " ind2=" ">
            <subfield code="a">Bernardini, G.</subfield>
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        <datafield tag="710" ind1="2" ind2=" ">
            <subfield code="1">2013</subfield>
            <subfield code="2">765</subfield>
            <subfield code="a">Universidad de Zaragoza</subfield>
            <subfield code="b">Dpto. Química Orgánica</subfield>
            <subfield code="c">Área Química Orgánica</subfield>
        </datafield>
        <datafield tag="773" ind1=" " ind2=" ">
            <subfield code="g">537 (2019), 615-628</subfield>
            <subfield code="p">J. colloid interface sci.</subfield>
            <subfield code="t">Journal of Colloid and Interface Science</subfield>
            <subfield code="x">0021-9797</subfield>
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            <subfield code="s">453861</subfield>
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            <subfield code="a">2020-07-16-09:18:53</subfield>
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