<?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>1665-2738</journal-id>
<journal-title><![CDATA[Revista mexicana de ingeniería química]]></journal-title>
<abbrev-journal-title><![CDATA[Rev. Mex. Ing. Quím]]></abbrev-journal-title>
<issn>1665-2738</issn>
<publisher>
<publisher-name><![CDATA[Universidad Autónoma Metropolitana, División de Ciencias Básicas e Ingeniería]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S1665-27382014000100011</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Utilización de materiales a base de quitina y quitosano en la inmovilización de proteasas: efectos en su estabilización y aplicaciones]]></article-title>
<article-title xml:lang="en"><![CDATA[Utilization of chitin and chitosan based materials for protease immobilization: stabilization effects and applications]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Salazar-Leyva]]></surname>
<given-names><![CDATA[J.A.]]></given-names>
</name>
<xref ref-type="aff" rid="A01"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Lizardi-Mendoza]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<xref ref-type="aff" rid="A01"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Ramírez-Suarez]]></surname>
<given-names><![CDATA[J.C.]]></given-names>
</name>
<xref ref-type="aff" rid="A01"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[García-Sánchez]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<xref ref-type="aff" rid="A01"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Ezquerra-Brauer]]></surname>
<given-names><![CDATA[J.M.]]></given-names>
</name>
<xref ref-type="aff" rid="A02"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Valenzuela-Soto]]></surname>
<given-names><![CDATA[E.M.]]></given-names>
</name>
<xref ref-type="aff" rid="A01"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Carvallo-Ruiz]]></surname>
<given-names><![CDATA[M.G.]]></given-names>
</name>
<xref ref-type="aff" rid="A01"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Lugo-Sánchez]]></surname>
<given-names><![CDATA[M.E.]]></given-names>
</name>
<xref ref-type="aff" rid="A01"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Pacheco-Aguilar]]></surname>
<given-names><![CDATA[R.]]></given-names>
</name>
<xref ref-type="aff" rid="A01"/>
</contrib>
</contrib-group>
<aff id="A01">
<institution><![CDATA[,Centro de Investigación en Alimentación y Desarrollo A.C.  ]]></institution>
<addr-line><![CDATA[Hermosillo Sonora]]></addr-line>
<country>México</country>
</aff>
<aff id="A02">
<institution><![CDATA[,Universidad de Sonora Departamento de Investigación y Posgrado en Alimentos ]]></institution>
<addr-line><![CDATA[Hermosillo Sonora]]></addr-line>
<country>México</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>00</month>
<year>2014</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>00</month>
<year>2014</year>
</pub-date>
<volume>13</volume>
<numero>1</numero>
<fpage>129</fpage>
<lpage>150</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S1665-27382014000100011&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S1665-27382014000100011&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S1665-27382014000100011&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Las enzimas proteolíticas poseen un amplio campo de aplicación en diversas áreas de la industria, por lo que la búsqueda de estrategias para optimizar su desempeño catalítico es de gran importancia. La inmovilización de enzimas en soportes sólidos es una tecnología que induce cambios a nivel estructural en los sistemas catalíticos inmovilizados, ocasionando que las características de reacción de estos se vea mejorada notablemente, permitiendo, además, la posibilidad de utilizar repetidamente a las enzimas inmovilizadas en un mismo proceso. La quitina y su derivado el quitosano, son compuestos que poseen propiedades funcionales que los convierten en excelentes materiales para ser utilizados como soportes en la inmovilización de enzimas. Este artículo de revisión discute los efectos que causa el proceso de inmovilización en materiales a base de quitina y quitosano sobre la estabilidad bioquímica y operacional de enzimas proteolíticas; de igual forma, se presentan algunas aplicaciones de los sistemas catalíticos inmovilizados.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Proteolytic enzymes have a wide range of applications in different industrial fields therefore the development of strategies focused in the optimization of their catalytic performance is a topic of great interest. Enzyme immobilization onto solid supports induces changes at structural level in the immobilized systems, and consequently some reaction characteristics can be enhanced; furthermore, immobilized enzymes can be reused in the same process. Due to the unique physicochemical and functional properties that chitin and its derivate chitosan possess, these biopolymers are an excellent option as support for enzyme immobilization. This review discusses the effects on the biochemical and operational performance of proteases immobilized in chitin and chitosan based materials. Some aspects related with the industrial applications of the immobilization systems are also mentioned.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[inmovilización]]></kwd>
<kwd lng="es"><![CDATA[proteasas]]></kwd>
<kwd lng="es"><![CDATA[quitina]]></kwd>
<kwd lng="es"><![CDATA[quitosano]]></kwd>
<kwd lng="es"><![CDATA[estabilidad]]></kwd>
<kwd lng="en"><![CDATA[immobilization]]></kwd>
<kwd lng="en"><![CDATA[proteases]]></kwd>
<kwd lng="en"><![CDATA[chitin]]></kwd>
<kwd lng="en"><![CDATA[chitosan]]></kwd>
<kwd lng="en"><![CDATA[stability]]></kwd>
</kwd-group>
</article-meta>
</front><body><![CDATA[  	    <p align="justify"><font face="verdana" size="4">Art&iacute;culos de investigaci&oacute;n </font></p>     <p align="justify">&nbsp;</p>      <p align="center"><font face="verdana" size="4"><b>Utilizaci&oacute;n de materiales a base de quitina y quitosano en la inmovilizaci&oacute;n de proteasas: efectos en su estabilizaci&oacute;n y aplicaciones</b></font></p>     <p align="center">&nbsp;</p>  	    <p align="center"><b><font face="verdana" size="3">Utilization of chitin and chitosan based materials for protease immobilization: stabilization effects and applications</font></b></p>     <p align="center">&nbsp;</p>  	    <p align="center"><b><font face="verdana" size="2">J.A. Salazar&#45;Leyva<sup>1</sup>, J. Lizardi&#45;Mendoza<sup>1</sup>, J.C. Ram&iacute;rez&#45;Suarez<sup>1</sup>, G. Garc&iacute;a&#45;S&aacute;nchez<sup>1</sup>, J.M. Ezquerra&#45;Brauer<sup>2</sup>, E.M. Valenzuela&#45;Soto<sup>1</sup>, M.G. Carvallo&#45;Ruiz<sup>1</sup>, M.E. Lugo&#45;S&aacute;nchez<sup>1</sup> y R. Pacheco&#45;Aguilar<sup>1</sup>*</font></b><font face="verdana" size="2"></font></p> 	    <p align="justify">&nbsp;</p>      <p align="justify"><font face="verdana" size="2"><i><sup>1</sup> Centro de Investigaci&oacute;n en Alimentaci&oacute;n y Desarrollo A.C. Carretera a la Victoria, C.P. 83304. Hermosillo, Sonora, M&eacute;xico. </i>*<i>Autor para la correspondencia. E&#45;mail</i>: <a href="mailto:rpacheco@ciad.mx">rpacheco@ciad.mx</a> <i>Tel</i>/<i>Fax. 662&#45;280&#45;04&#45;21 Ext. 525.</i></font></p>     ]]></body>
<body><![CDATA[<p align="justify"><font face="verdana" size="2"><i><sup>2</sup> Departamento de Investigaci&oacute;n y Posgrado en Alimentos, Universidad de Sonora. Rosales y Ni&ntilde;os H&eacute;roes SN. Hermosillo, Sonora, M&eacute;xico.</i></font></p>     <p align="justify">&nbsp;</p>      <p align="justify"><font face="verdana" size="2">Received September 17, 2013.    <br> </font><font face="verdana" size="2">Accepted November 20, 2013.</font></p>     <p align="justify">&nbsp;</p>     <p align="justify"><font face="verdana" size="2"><b>Resumen</b></font></p>  	    <p align="justify"><font face="verdana" size="2">Las enzimas proteol&iacute;ticas poseen un amplio campo de aplicaci&oacute;n en diversas &aacute;reas de la industria, por lo que la b&uacute;squeda de estrategias para optimizar su desempe&ntilde;o catal&iacute;tico es de gran importancia. La inmovilizaci&oacute;n de enzimas en soportes s&oacute;lidos es una tecnolog&iacute;a que induce cambios a nivel estructural en los sistemas catal&iacute;ticos inmovilizados, ocasionando que las caracter&iacute;sticas de reacci&oacute;n de estos se vea mejorada notablemente, permitiendo, adem&aacute;s, la posibilidad de utilizar repetidamente a las enzimas inmovilizadas en un mismo proceso. La quitina y su derivado el quitosano, son compuestos que poseen propiedades funcionales que los convierten en excelentes materiales para ser utilizados como soportes en la inmovilizaci&oacute;n de enzimas. Este art&iacute;culo de revisi&oacute;n discute los efectos que causa el proceso de inmovilizaci&oacute;n en materiales a base de quitina y quitosano sobre la estabilidad bioqu&iacute;mica y operacional de enzimas proteol&iacute;ticas; de igual forma, se presentan algunas aplicaciones de los sistemas catal&iacute;ticos inmovilizados.</font></p>  	    <p align="justify"><font face="verdana" size="2"><b>Palabras clave:</b> inmovilizaci&oacute;n, proteasas, quitina, quitosano, estabilidad.</font></p>     <p align="justify">&nbsp;</p>      <p align="justify"><font face="verdana" size="2"><b>Abstract</b></font></p>  	    ]]></body>
<body><![CDATA[<p align="justify"><font face="verdana" size="2">Proteolytic enzymes have a wide range of applications in different industrial fields therefore the development of strategies focused in the optimization of their catalytic performance is a topic of great interest. Enzyme immobilization onto solid supports induces changes at structural level in the immobilized systems, and consequently some reaction characteristics can be enhanced; furthermore, immobilized enzymes can be reused in the same process. Due to the unique physicochemical and functional properties that chitin and its derivate chitosan possess, these biopolymers are an excellent option as support for enzyme immobilization. This review discusses the effects on the biochemical and operational performance of proteases immobilized in chitin and chitosan based materials. Some aspects related with the industrial applications of the immobilization systems are also mentioned.</font></p>  	    <p align="justify"><font face="verdana" size="2"><b>Keywords:</b> immobilization, proteases, chitin, chitosan, stability.</font></p> 	    <p align="justify">&nbsp;</p> 	    <p align="justify"><font size="2" face="verdana"><a href="/pdf/rmiq/v13n1/v13n1a11.pdf" target="_blank">DESCARGAR ART&Iacute;CULO EN FORMATO PDF</a></font></p>     <p align="justify">&nbsp;</p>     <p align="justify"><font face="verdana" size="2"><b>Referencias</b></font></p>  	    <!-- ref --><p align="justify"><font face="verdana" size="2">Agull&oacute;, E., Rodriguez, M.S., Ramos, V. y Albertengo, L. (2003). Present and future role of chitin and chitosan in food. <i>Macromolecular Bioscience 3</i>, 521&#45;530.    &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;[&#160;<a href="javascript:void(0);" onclick="javascript: window.open('/scielo.php?script=sci_nlinks&ref=8571525&pid=S1665-2738201400010001100001&lng=','','width=640,height=500,resizable=yes,scrollbars=1,menubar=yes,');">Links</a>&#160;]<!-- end-ref --></font></p>      <!-- ref --><p align="justify"><font face="verdana" size="2">Ahmed, S. A., Saleh, S. A. y Abdel&#45;Fattah, A. F. (2007). Stabilization of Bacillus licheniformis ATCC 21415 alkaline protease by immobilization and modification. <i>Australian Journal of Basic and Applied Sciences 1</i>, 313&#45;322.    &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;[&#160;<a href="javascript:void(0);" onclick="javascript: window.open('/scielo.php?script=sci_nlinks&ref=8571527&pid=S1665-2738201400010001100002&lng=','','width=640,height=500,resizable=yes,scrollbars=1,menubar=yes,');">Links</a>&#160;]<!-- end-ref --></font></p>  	    ]]></body>
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