<?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>0120-100X</journal-id>
<journal-title><![CDATA[Revista ION]]></journal-title>
<abbrev-journal-title><![CDATA[Rev. ion]]></abbrev-journal-title>
<issn>0120-100X</issn>
<publisher>
<publisher-name><![CDATA[Universidad Industrial de Santander]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S0120-100X2019000200007</article-id>
<article-id pub-id-type="doi">10.18273/revion.v32n2-2019001</article-id>
<title-group>
<article-title xml:lang="en"><![CDATA[Immobilization of lipase in biochar obtained from Manihot esculenta Crantz]]></article-title>
<article-title xml:lang="es"><![CDATA[Inmobilización de lipasa en biochar obtenida de Manihot Esculenta Crantz]]></article-title>
<article-title xml:lang="pt"><![CDATA[Imobilização da lipase em biochar obtido de Manihot Esculenta Crantz]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Oliveira-Ribeiro]]></surname>
<given-names><![CDATA[Livia Maria]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Meili]]></surname>
<given-names><![CDATA[Lucas]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Silva-Belo-Gois]]></surname>
<given-names><![CDATA[Georgia Nayane]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Rosas-Garcia-Almeida]]></surname>
<given-names><![CDATA[Renata Maria]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Silva-Duarte]]></surname>
<given-names><![CDATA[José Leandro da]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
<xref ref-type="aff" rid="Aaf"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidade Federal de Alagoas  ]]></institution>
<addr-line><![CDATA[ ]]></addr-line>
<country>Brazil</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,Universidade Federal de Alagoas  ]]></institution>
<addr-line><![CDATA[ ]]></addr-line>
<country>Brazil</country>
</aff>
<aff id="Af3">
<institution><![CDATA[,Universidade Federal de Alagoas  ]]></institution>
<addr-line><![CDATA[ ]]></addr-line>
<country>Brazil</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>12</month>
<year>2019</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>12</month>
<year>2019</year>
</pub-date>
<volume>32</volume>
<numero>2</numero>
<fpage>7</fpage>
<lpage>13</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_arttext&amp;pid=S0120-100X2019000200007&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_abstract&amp;pid=S0120-100X2019000200007&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_pdf&amp;pid=S0120-100X2019000200007&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract The immobilized enzymes are catalysts of great industrial interest, as it unites the advantages of heterogeneous catalysis with the high selectivity and mild operation conditions of the enzymes. Biochar is a porous carbonaceous material, which have characteristic that it makes a strong candidate to incorporate enzymes in its structure. Another relevant fact is the possibility of changes and adaptations by synthesis condition in the biochar structure due to the application needs. In this context, the objective of this work was the study of immobilization of lipase (type II, code l3126, Sigma Aldrich) in a biochar produced by pyrolysis (600oC) from an agricultural residue called cassava stump. It was evaluated different enzymatic concentrations (0.1, 0.25 and 0.5 g/L) in order to determine the affinity between the enzyme and biochar. The obtained results showed that the enzyme studied could be easily immobilized in the biochar, obtaining as immobilization yield 61.2% when using the highest concentration of enzyme.]]></p></abstract>
<abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen Las enzimas inmovilizadas son catalizadores de gran interés industrial, ya que unen las ventajas de la catálisis heterogénea con la alta selectividad y las condiciones de operación suaves de las enzimas. El biochar es un material carbonoso poroso, que tiene la característica de que es un fuerte candidato para incorporar enzimas en su estructura. Otro hecho relevante es la posibilidad de cambios y adaptaciones por condición de síntesis en la estructura de Biochar debido a las necesidades de la aplicación. En este contexto, el objetivo de este trabajo fue el estudio de la inmovilización de lipasa en un biochar producido por pirólisis (600 ° C) de un residuo agrícola llamado tocón de yuca. Se evaluaron diferentes concentraciones enzimáticas (0.1, 0.25 y 0.5 g / L) para determinar la afinidad entre la enzima y el biochar. Los resultados obtenidos mostraron que la enzima estudiada se podía inmovilizar fácilmente en el biochar, obteniendo como rendimiento de inmovilización 61.2% cuando se usa la mayor concentración de enzima.]]></p></abstract>
<abstract abstract-type="short" xml:lang="pt"><p><![CDATA[Resumo As enzimas imobilizadas são catalisadoras de grande interesse industrial, pois unem as vantagens da catálise heterogênea com a alta seletividade e condições de operação moderada das enzimas. Biochar é um material carbonoso poroso, que possui característica que faz forte candidato a incorporar enzimas em sua estrutura. Outro fato relevante é a possibilidade de mudanças e adaptações por condição de síntese na estrutura do Biochar devido às necessidades de aplicação. Neste contexto, o objetivo deste trabalho foi o estudo da imobilização da lipase em um biochar produzido por pirólise (600o C) a partir de um resíduo agrícola denominado cepa de mandioca. Foram avaliadas diferentes concentrações enzimáticas (0,1; 0,25 e 0,5 g / L) para determinar a afinidade entre a enzima e o biocarvão. Os resultados obtidos mostraram que a enzima estudada pode ser facilmente imobilizada no biocarvão, obtendo como imobilização rendimento de 61,2% quando se utiliza a maior concentração de enzimas.]]></p></abstract>
<kwd-group>
<kwd lng="en"><![CDATA[Enzyme]]></kwd>
<kwd lng="en"><![CDATA[Adsorption]]></kwd>
<kwd lng="en"><![CDATA[Porous Material.]]></kwd>
<kwd lng="es"><![CDATA[Enzima]]></kwd>
<kwd lng="es"><![CDATA[Adsorción]]></kwd>
<kwd lng="es"><![CDATA[Material Poroso.]]></kwd>
<kwd lng="pt"><![CDATA[Biochar]]></kwd>
<kwd lng="pt"><![CDATA[Enzima]]></kwd>
<kwd lng="pt"><![CDATA[Adsorção]]></kwd>
<kwd lng="pt"><![CDATA[Material Poroso.]]></kwd>
</kwd-group>
</article-meta>
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