<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>0121-7488</journal-id>
<journal-title><![CDATA[Ciencia en Desarrollo]]></journal-title>
<abbrev-journal-title><![CDATA[Ciencia en Desarrollo]]></abbrev-journal-title>
<issn>0121-7488</issn>
<publisher>
<publisher-name><![CDATA[Universidad Pedagógica y Tecnológica de Colombia]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S0121-74882021000100069</article-id>
<article-id pub-id-type="doi">10.19053/01217488.v12.n1.2021.12818</article-id>
<title-group>
<article-title xml:lang="en"><![CDATA[Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization]]></article-title>
<article-title xml:lang="es"><![CDATA[Nanopartículas magnéticas funcionalizadas y modificadas con entrecruzamiento para mejorar la inmovilización de la invertasa]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Vargas]]></surname>
<given-names><![CDATA[Annie Y.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Romanelli]]></surname>
<given-names><![CDATA[Gustavo P.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Martinez]]></surname>
<given-names><![CDATA[José J.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Pedagógica y Tecnológica de Colombia. Facultad de Ciencias. Grupo de Catálisis (GC-UPTC). Escuela de Ciencias Químicas.]]></institution>
<addr-line><![CDATA[Avenida Central del Norte, Tunja, Boyacá]]></addr-line>
<country>Colombia</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,UNLP-CCT-CONICET Departamento de Química, Facultad de Ciencias Exactas Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. J. J. Ronco" (CINDECA)]]></institution>
<addr-line><![CDATA[ ]]></addr-line>
<country>Colombia</country>
</aff>
<aff id="Af3">
<institution><![CDATA[,Universidad Pedagógica y Tecnológica de Colombia. Facultad de Ciencias. Grupo de Catálisis (GC-UPTC) Escuela de Ciencias Químicas]]></institution>
<addr-line><![CDATA[Avenida Central del Norte, Tunja, Boyacá]]></addr-line>
<country>Colombia</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>06</month>
<year>2021</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>06</month>
<year>2021</year>
</pub-date>
<volume>12</volume>
<numero>1</numero>
<fpage>69</fpage>
<lpage>77</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_arttext&amp;pid=S0121-74882021000100069&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_abstract&amp;pid=S0121-74882021000100069&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_pdf&amp;pid=S0121-74882021000100069&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract Procedures of immobilization invertase have been developed using different supports. However, disadvantages such as use of small particles for invertase immobilizations in packed-bed reactors are being solved using magnetic particles. In this study, composites containing Fe3O4 were prepared by incorporation of a polysiloxane layer required for the physical adsorption of the invertase. Besides, the functionalized magnetite was activated with glutaraldehyde and polyethylenimine (PEI) with the aim of performing a covalent immobilization. The effect of different conditions such as enzyme: support ratio, pH, and temperature were analyzed in the preservation of invertase. The results demonstrated that the optimum enzyme:support ratio is higher for covalent bonding than for physical adsorption. The ideal pH for the immobilized enzyme is 5.0, and the enzymatic activity is retained until 70 °C. The values of km are similar in both immobilization methods. The analysis of the effect of pH and thermostability showed that the catalytic activity of invertase is not affected in comparison with the free enzyme. The covalent immobilization displays higher efficiency in the immobilization process (F£), less inhibition and twice as much stability. The enzymes immobilized by physical and covalent methods can be reused for up to four cycles and can be removed from the reaction medium by applying an external magnetic field.]]></p></abstract>
<abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen Se han desarrollado procedimientos de inmovilización con invertasa utilizando diferentes soportes. Sin embargo, las desventajas como el uso de partículas pequeñas para inmovilizaciones de invertasa en reactores de lecho compacto se están resolviendo utilizando partículas magnéticas. En este estudio, los compuestos que contienen Fe3O4 se prepararon mediante la incorporación de una capa de polisiloxano necesaria para la adsorción física de la invertasa. Además, la magnetita funcionalizada se activó con glutaraldehído y polietilenimina (PEI) con el objetivo de realizar una inmovilización covalente. Se analizó el efecto de diferentes condiciones como la relación enzima: soporte, pH y temperatura en la conservación de la invertasa. Los resultados demostraron que la relación enzima: soporte óptima es mayor para la unión covalente que para la adsorción física. El pH ideal para la enzima inmovilizada es 5,0 y la actividad enzimática se mantiene hasta 70 °C. Los valores de km son similares en ambos métodos de inmovilización. El análisis del efecto del pH y la termoestabilidad mostró que la actividad catalítica de la invertasa no se ve afectada en comparación con la enzima libre. La inmovilización covalente muestra una mayor eficacia en el proceso de inmovilización (Fe), menos inhibición y el doble de estabilidad. Las enzimas inmovilizadas por métodos físicos y covalentes se pueden reutilizar hasta por cuatro ciclos y se pueden eliminar del medio de reacción aplicando un campo magnético externo.]]></p></abstract>
<kwd-group>
<kwd lng="en"><![CDATA[invertase]]></kwd>
<kwd lng="en"><![CDATA[Fe3O4]]></kwd>
<kwd lng="en"><![CDATA[immobilization]]></kwd>
<kwd lng="en"><![CDATA[composites]]></kwd>
<kwd lng="es"><![CDATA[invertasa]]></kwd>
<kwd lng="es"><![CDATA[Fe3O4]]></kwd>
<kwd lng="es"><![CDATA[inmovilización]]></kwd>
<kwd lng="es"><![CDATA[compuestos]]></kwd>
</kwd-group>
</article-meta>
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