<?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>0120-2804</journal-id>
<journal-title><![CDATA[Revista Colombiana de Química]]></journal-title>
<abbrev-journal-title><![CDATA[Rev.Colomb.Quim.]]></abbrev-journal-title>
<issn>0120-2804</issn>
<publisher>
<publisher-name><![CDATA[Departamento de Química,  Universidad Nacional de Colombia.]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S0120-28042020000100003</article-id>
<article-id pub-id-type="doi">10.15446/rev.colomb.quim.v1n49.69474</article-id>
<title-group>
<article-title xml:lang="en"><![CDATA[Immobilization of bromelain on cobalt-iron magnetic nanoparticles (CoFe2O4) for casein hydrolysis]]></article-title>
<article-title xml:lang="es"><![CDATA[Inmovilización de bromelina sobre nanopartículas magnéticas de cobalto-hierro (CoFe2O4) para la hidrólisis de caseína]]></article-title>
<article-title xml:lang="pt"><![CDATA[Inmovilización de bromelina sobre nanopartículas magnéticas de cobalto-hierro (CoFe2O4) para a hidrólise de caseína]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[García-Colmenares]]></surname>
<given-names><![CDATA[José Mauricio]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Reyes-Cuellar]]></surname>
<given-names><![CDATA[Julia Constanza]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Pedagógica y Tecnológica de Colombia  ]]></institution>
<addr-line><![CDATA[Tunja ]]></addr-line>
<country>Colombia</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>04</month>
<year>2020</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>04</month>
<year>2020</year>
</pub-date>
<volume>49</volume>
<numero>1</numero>
<fpage>3</fpage>
<lpage>10</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_arttext&amp;pid=S0120-28042020000100003&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_abstract&amp;pid=S0120-28042020000100003&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.co/scielo.php?script=sci_pdf&amp;pid=S0120-28042020000100003&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract By means of recycling an enzyme, bromelain was used in casein hydrolysis facilitated by a nanobiocatalyst consisting of bromelain, CoFe2O4 magnetic nanoparticles, chitosan, and glutaraldehyde. Bromelain was immobilized on the chitosan cobalt-magnetite nanoparticle surface via covalent bonds to form the nanobiocatalyst. Immobilized bromelain showed 77% immobilization binding, retaining 85 ± 2% of the initial catalytic activity. Nanoparticles and immobilized bromelain were characterized using UV-Vis and IR spectroscopies, X-ray, square wave voltammetry (SWV), cyclic voltammetry (CV), vibrating-sample magnetization (VSM), and transmission electron microscope (TEM). The Michaelis-Menten constant (KM) and VMAX of the free and immobilized enzyme were calculated: KM = 2.1 ± 0.18 mM and 1.8 mM, respectively and VMAX = 6.08 x 10-2 ± 2.1 x 10-2 U/min and 6.46 ± 0.91 U/min, respectively. The thermal stability of the free enzyme was higher than the immobilized enzyme: 95-98% and 83-87%, respectively. An optimum pH of 6 and a temperature of 20 °C were determined in both cases. Immobilized bromelain maintained 50% of the initial catalytic activity after the fifth use. The immobilized bromelain proved to be effective and reusable for casein hydrolysis. As novel contribution the characterization by VOC and CV was carried out.]]></p></abstract>
<abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen Se investigó la reutilización de la bromelina inmovilizada sobre nanopartículas magnéticas de CoFe2O4 para la hidrólisis de caseína. La inmovilización se efectuó covalentemente en un catalizador de nanopartículas de hierro y cobalto recubiertas con quitosano, glutaraldehído y bromelina. La bromelina alcanzó un máximo de inmovilización del 77%, conservando el 85 ± 2% de su actividad catalítica inicial a los 30 min. La caracterización del catalizador se realizó por espectrofotometría IR y UV-Vis, microscopía electrónica de transmisión (TEM), difracción de rayos X, voltametría de onda cuadrada (VOC), voltametría cíclica (VC) y magnetización de muestra vibrante (VSM). Los parámetros cinéticos KM y VMAX de la enzima libre e inmovilizada fueron: KM = 2,1 ± 0,18 mM y 1,8 ± 0,16 mM, respectivamente y VMAX = 6,08 x 10-2 ± 2,1 x 10-2 U/min y 6,46 ± 0,91 U/min, respectivamente. La estabilidad térmica de la enzima libre fue mayor que la de enzima inmovilizada: 95-98% y 83-87%, respectivamente. Se determinó un pH óptimo de 6 y temperatura de 20 °C en ambos casos. La bromelina inmovilizada mantuvo el 50% de su actividad catalítica hasta el quinto uso. Como aporte novedoso se realizó, en este estudio se realizó la caracterización por VOC y VC.]]></p></abstract>
<abstract abstract-type="short" xml:lang="pt"><p><![CDATA[Resumo Foi estudado o reuso da enzima bromelina imobilizada sobre nano partículas magnéticas de CoFe2O4, para a hidrólise de caseína. A imobilização efetuou-se covalentemente em um catalisador de nano partículas de cobalto e ferro recobertas com quitosano, glutaraldehido e bromelina. A bromelina atingiu seu máximo de imobilização do 77% aos 30 minutos, conservando o 85 ± 2% da sua atividade catalítica inicial. A caraterização foi feita mediante espectrofotometria IV e UV-Vis, microscopia eletrônica de transmissão (TEM), difração de raios X, voltametria de onda quadrada (VOQ), voltametria cíclica (VC) e por magnetização de amostra vibrante (VSM). Os parâmetros cinéticos KM e VMAX da enzima livre e imobilizada foram KM = 2,1 ± 0,18 mM e 1,8 8 ± 0,16mM, respeitivamente; VMAX = 6,08 x 10-2 ± 2,1 x 10-2 U/min e 6,46 ± 0,91 U/min, respectivamente. A estabilidade térmica da enzima livre (95-98%) foi maior do que a estabilidade da enzima imobilizada (83-87%), determinou-se um pH óptimo de 6 e temperatura de 20 °C em ambos os casos. A bromelina imobilizada manteve o 50% de sua atividade catalítica até o quinto uso. Como aporte inovador neste estudo apresenta-se a caraterização por VOQ e VC.]]></p></abstract>
<kwd-group>
<kwd lng="en"><![CDATA[immobilization]]></kwd>
<kwd lng="en"><![CDATA[enzyme]]></kwd>
<kwd lng="en"><![CDATA[casein]]></kwd>
<kwd lng="en"><![CDATA[recycling]]></kwd>
<kwd lng="en"><![CDATA[hydrolysis]]></kwd>
<kwd lng="en"><![CDATA[voltammetry]]></kwd>
<kwd lng="es"><![CDATA[inmovilización]]></kwd>
<kwd lng="es"><![CDATA[enzima]]></kwd>
<kwd lng="es"><![CDATA[caseína]]></kwd>
<kwd lng="es"><![CDATA[reutilización]]></kwd>
<kwd lng="es"><![CDATA[hidrólisis]]></kwd>
<kwd lng="es"><![CDATA[voltametría]]></kwd>
<kwd lng="pt"><![CDATA[enzima imobilizada]]></kwd>
<kwd lng="pt"><![CDATA[caseína]]></kwd>
<kwd lng="pt"><![CDATA[reutilização]]></kwd>
<kwd lng="pt"><![CDATA[hidrolises]]></kwd>
<kwd lng="pt"><![CDATA[voltametria]]></kwd>
</kwd-group>
</article-meta>
</front><back>
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