<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:dcterms="http://purl.org/dc/terms/">
<rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/6858">
    <dcterms:title><![CDATA[<strong>Purification and characterization of &alpha;-fucosidase from Dichostereum sordulentum 1488</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[GLICOSIDASAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[CARBOHIDRATOS]]></dcterms:subject>
    <dcterms:subject><![CDATA[A-L-FUCOSA]]></dcterms:subject>
    <dcterms:subject><![CDATA[A-FUCOSIDASA]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2024]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Biological glycans mediate several physiological processes, thus altered glycosylation patterns can lead to different diseases such as autoimmune, infectious, chronic anti-inflammatory diseases, or even cancer. In fact, alterations in fucosylation in either N- or O-glycans are among the most frequent changes in glycosylation patterns associated with cancer. Therefore, elucidation of the role of glycoconjugate glycans is essential for understanding the development of pathologies where they are involved. In this sense glycosidases are excellent tools, since they catalyse the selective removal of sugar residues, allowing the evaluation of changes in their biological role due to glycan removal. This work describes the purification and characterization of a &alpha;-fucosidase from the fungus Dichostereum sordulentum 1488. It is a homodimer with a molecular weight of 214 kDa and optimum pH and temperature of 4.0 and 70 ◦C respectively. It has a KM of 0.27 mM and VMax of 3.3 &mu;moles PNP/ min per mg for the substrate p-nitrophenyl-&alpha;-L-fucopyranoside, showing a substrate inhibition profile. It showed high specificity for the hydrolysis of fucose linked by &alpha;-(1,2) bonds. The identification, purification, and characterization of this new &alpha;-fucosidase is highly relevant for enlarging the availability of glycosidases for use as tools for glycan elucidation.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<a href="https://export.cvuy.uy/cv/?89f4f95ef44a6b6cf3cc08494680b267"><strong>Herrera, Lorena</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a href="https://export.cvuy.uy/cv/?441488c6d1acc8438d8713846d7f670b"><strong>Cedr&eacute;s, Mar&iacute;a Eugenia</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a href="https://export.cvuy.uy/cv/?a7dc62e1b1bbd449b3ac8472794ba2e52c18f2d4c52e9debc1b69bc3869e0f2eee9e4150d80c79f75a9876faa56a6b16a3a194119f3a19e8ff051ce749292a53"><strong>Rodr&iacute;guez Bonnecarr&eacute;re, Paula</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a href="https://export.cvuy.uy/cv/?8c80c1ae8b95cb6b8bc4b6ce3a8d3a39b297d1bd27a3804c09be97adcbe35a3741bd28180c0446feac51238afbedb3cf67010e8ed6fa462a13806c083463ea87"><strong>Giacomini, Cecilia</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[Carbohydrate Research, v. 545, n&ordm; 1, 2024. -- e109278]]></dcterms:source>
    <dcterms:publisher><![CDATA[Elsevier]]></dcterms:publisher>
    <dcterms:date><![CDATA[2024]]></dcterms:date>
    <dcterms:rights><![CDATA[<div class="element-text">
<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong>&nbsp;de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong>&nbsp;La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>
</div>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:extent><![CDATA[8 p.]]></dcterms:extent>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[10.1016/j.carres.2024.109278]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/6784">
    <dcterms:title><![CDATA[<strong>The adsorption/desorption behaviour of horseradish peroxidase heroxidase and porcine Thyroglobulin on concanavalin a-sepharose with different ligand densities</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[LECTINA]]></dcterms:subject>
    <dcterms:subject><![CDATA[PEROXIDASAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2000]]></dcterms:subject>
    <dcterms:abstract><![CDATA[A series of Concanavalin A-Sepharose gels containing between 5 and 480 mg lectin/g of dry gel was prepared by varying the amount of Concanavalin A used in the coupling reaction after activation with 1-cyano-4-(dimethyl-amino)-pyridinium tetrafluoroborate (CDAP) in a modified procedure. The influence of the ligand content on the adsorption / desorption of two different glycoproteins horseradish peroxidase (HRP Mw 40 KDa) and porcine thyroglogulin (Mw 670 KDa) was studied. The adsorption of HRP was found to be dependent on the ligand density and the largest amount adsorbed was obtained when the molar ratio between immobilized Con A and applied HRP was 9/1. The results indicate that highly effective lectin affinity adsorbents can be rationally designed based on the amounts of immobilized lectin]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Franco Fraguas, Laura</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Batista Viera, Francisco.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Carlsson, J.</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[International Journal of Bio/Chromatographyv. 5, no. 4, 2000. -- pp. 255-265]]></dcterms:source>
    <dcterms:publisher><![CDATA[Overseas]]></dcterms:publisher>
    <dcterms:date><![CDATA[2000]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong>&nbsp;de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong>&nbsp;La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:extent><![CDATA[11 p.]]></dcterms:extent>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/6554">
    <dcterms:title><![CDATA[<strong>Highlighting the roles of transition metals and speciation in chemical biology</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[METALES]]></dcterms:subject>
    <dcterms:subject><![CDATA[COFACTORES]]></dcterms:subject>
    <dcterms:subject><![CDATA[REACTIVIDAD]]></dcterms:subject>
    <dcterms:subject><![CDATA[METALES DE TRANSICION]]></dcterms:subject>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2022]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Transition metal ions play key structural and functional roles, affecting structures of biomolecules and enzyme function. The importance of transition metal ions in chemical biology is, thus, undisputed. However, the aqueous chemistry of metal ions is complicated because they form species in several protonation and redox states. In the presence of metabolites, metal ions can also form coordination complexes. The existence of several species is relevant because enzymes and membrane receptors can distinguish between species even when they are rapidly equilibrating. Thus, metal ions, enzyme cofactors, and therapeutic agents are sensitive to the metal ion speciation chemistry because it affects their interaction with enzymes and other biomolecules. Speciation is also crucial for metal containing bioorthogonal reactions, since water and metabo lites stabilize active catalysts, affect chemoselectivity and re action yields.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Kostenkova, Kateryna</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a href="https://export.cvuy.uy/cv/?30f70e9dfd00c43ffab403face2bbb4fd0f8853410743d6fa48798782e4078d5bf0735c77ca026b5828f7194ff3401bbfd4bd422c0ea61fda7a3ceb0a5af09f8" target="_blank"><strong>Scalese, Gonzalo</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a href="https://export.cvuy.uy/cv/?6bb5dcce3e2559101357796ca4a2b2d4c9ba6b3a978a0bd4c5dab0107081b73e1ff46dcf49a7de2b571ff7980c4a01789f09f1d7eac1b879a8553641f940b9a5" target="_blank"><strong>Gambino, Dinorah</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Crans, Debbie C.</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[Current Opinion in Chemical Biology v. 69, 2022. -- e102155]]></dcterms:source>
    <dcterms:publisher><![CDATA[Elsevier]]></dcterms:publisher>
    <dcterms:date><![CDATA[2022]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong>&nbsp;de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong>&nbsp;La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:extent><![CDATA[11 p.]]></dcterms:extent>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[10.1016/j.cbpa.2022.102155]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/6316">
    <dcterms:title><![CDATA[<strong>Redox biocatalysis :&nbsp;fundamentals and applications</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[BIOCATALISIS]]></dcterms:subject>
    <dcterms:subject><![CDATA[OXIDACION]]></dcterms:subject>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[QUIMICA ORGANICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2012]]></dcterms:subject>
    <dcterms:creator><![CDATA[<a href="https://exportcvuy.anii.org.uy/cv/?8c505850402fa99348b3dddca227f30fb5ab9d97971fb6ad5af3e09e8062fc92ab83038800b795f8297d263e2e90d1e57819f948dcda71408e3b5de86f57b62f" target="_blank"><strong>Gamenara, Daniela</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a href="https://exportcvuy.anii.org.uy/cv/?cbfccfdb54596e6cb04c5c403027fe4eababcb01435d93575e63367c06474cc7c5897f2b080448c7cf73d21a359e87a044d9cc552bdb2f20cedca29dba1930fd" target="_blank"><strong>Seoane, Gustavo A.</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=664abf8d2959acb20a57fad7a94769fcd6bcd6cb9185d87136fd434e7fddcd763e08b59175070ea1f148f412f58e75bc27b7717516f5d6c76fd53747356f34d4&amp;formato=pdf&amp;convocatoria=21" target="_blank"><strong>Saenz M&eacute;ndez, Patricia</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Dom&iacute;nguez de Ma&iacute;a, Pablo</strong>]]></dcterms:creator>
    <dcterms:publisher><![CDATA[Wiley]]></dcterms:publisher>
    <dcterms:date><![CDATA[2012]]></dcterms:date>
    <dcterms:rights><![CDATA[<span><span><span><strong><em>Informaci&oacute;n sobre Derechos de Autor</em></strong></span></span></span>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong><em>La legislaci&oacute;n uruguaya&nbsp;</em></strong>protege el derecho de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA</strong>&nbsp;- La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[Papel]]></dcterms:format>
    <dcterms:extent><![CDATA[512 p.]]></dcterms:extent>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Libro]]></dcterms:type>
    <dcterms:identifier><![CDATA[ISBN: 9780470874202]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/6225">
    <dcterms:title><![CDATA[<strong>Identification of a Potential Zika Virus Inhibitor Targeting NS5 Methyltransferase Using Virtual Screening and Molecular Dynamics Simulations</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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    <dcterms:subject><![CDATA[ANTIVIRALES
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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    <dcterms:subject><![CDATA[METILTRANSFERASA
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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    <dcterms:subject><![CDATA[ZIKA-VIRUS
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>]]></dcterms:subject>
    <dcterms:subject><![CDATA[2020
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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    <dcterms:abstract><![CDATA[attractive molecular target for antivirals discovery against the Zika virus (ZIKV). Here, we report structure-based virtual screening of 42 390 structures from the Development Therapeutics Program (DTP) AIDS Antiviral Screen Database. Among the docked compounds, ZINC1652386 stood out due to its high affinity for MTase in comparison to the cocrystallized ligand MS2042, which interacts with the Asp146 residue in the MTase binding site by hydrogen bonding. Subsequent molecular dynamics simulations predicted that this compound forms a stable complex with MTase within 50 ns. Thus, ZINC1652386 may represent a promising ZIKV methyltransferase inhibitor.
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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    <dcterms:creator><![CDATA[<strong>Santos, Felipe R. S.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Lima, William G.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Maia, Eduardo H. B.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Assis, Let&iacute;cia C.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Davyt, Danilo</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Guterres Taranto, Alex</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Ferreira, Jaqueline M. S.</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[Journal of Chemical Information and Modeling v. 60, 2020.-- p. 562-568
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>]]></dcterms:source>
    <dcterms:publisher><![CDATA[American Chemical Society
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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    <dcterms:date><![CDATA[2020
<div id="sconnect-is-installed" style="display: none;">2.11.0.0</div>
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    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong> (Por favor lea este aviso antes de abrir los documentos u objetos)<strong> La legislaci&oacute;n uruguaya protege el derecho de autor </strong>sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006) ADVERTENCIA - La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>
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    <dcterms:format><![CDATA[Pdf
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    <dcterms:language><![CDATA[Ingl&eacute;s
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    <dcterms:type><![CDATA[Art&iacute;culo
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    <dcterms:identifier><![CDATA[https://dx.doi.org/10.1021/acs.jcim.9b00809
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</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/6220">
    <dcterms:title><![CDATA[In Vitro Bioaccessibility of Extractable Compounds from Tannat Grape Skin Possessing Health Promoting Properties with Potential to Reduce the Risk of Diabetes]]></dcterms:title>
    <dcterms:subject><![CDATA[ANTIINFLAMATORIOS
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    <dcterms:subject><![CDATA[ANTIOXIDANTES
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    <dcterms:subject><![CDATA[AMILASA
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    <dcterms:subject><![CDATA[DIABETES
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    <dcterms:subject><![CDATA[GLUCOSIDASA
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    <dcterms:subject><![CDATA[ENZIMAS
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    <dcterms:subject><![CDATA[UVA TANNAT
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    <dcterms:subject><![CDATA[TRANSPORTADORES DE GLUCOSA
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    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA
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    <dcterms:subject><![CDATA[2020
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    <dcterms:abstract><![CDATA[Diabetes pathogenesis encompasses oxidative stress, inflammation, insulin malfunctioning and partial or total insulin secretion impairment, which leads to a constant hyperglycemia. Polyphenols are known to possess bioactive properties, being Tannat grape skin a natural and sustainable source of these compounds. The present study aimed to find out the bioaccessibility of health-promoting molecules composing a multifunctional extract from Tannat grape skin obtained under hydro-alcoholic-acid conditions. The identification of phenolic compounds in the samples was performed by ultra-high performance liquid chromatography tandem mass spectrometry (UHPLC-MS/MS). Subsequently, the samples were in vitro digested mimicking the human oral gastrointestinal conditions and the bioactivity of the digest (antioxidant, anti-inflammatory and modulation of glucose metabolism) was assessed. Eect on glucose metabolism was estimated by measuring carbohydrases activity and the functionality of glucose transporters of small intestine cells in presence and absence of the digested extract. Flavonoids, phenolic acids and phenolic alcohols were the major phenol compounds detected in the extract. The bioaccessible compounds protected the intestinal cells and macrophages against the induced formation of reactive oxygen species (ROS) and nitric oxide (NO). In addition, glucose transporters were inhibited by the digested extract. In conclusion, the bioaccessible compounds of the extract, including phenols, modulated key biochemical events involved in the pathogenesis of diabetes such as oxidative stress, inflammation and glucose absorption. The extract was eective under prevention with co-administration conditions supporting its potential for either reducing the risk or treating this disease.
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    <dcterms:creator><![CDATA[<strong>Fern&aacute;ndez Fern&aacute;ndez, Adriana Maite</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Iriondo DeHond, Amaia</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Nardin, Tiziana</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Larcher, Roberto</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Dellacassa, Eduardo</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Medrano Fern&aacute;ndez, Alejandra</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Del Castillo, Mar&iacute;a Dolores</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[Foods v. 9, 2020. -- p. 1-14.--e1575
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    <dcterms:publisher><![CDATA[MDPI
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    <dcterms:date><![CDATA[2020
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    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong> (Por favor lea este aviso antes de abrir los documentos u objetos)<strong> La legislaci&oacute;n uruguaya protege el derecho de autor </strong>sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006) ADVERTENCIA - La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>
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    <dcterms:format><![CDATA[Pdf
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    <dcterms:language><![CDATA[Ingl&eacute;s
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    <dcterms:type><![CDATA[Art&iacute;culo
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    <dcterms:identifier><![CDATA[doi:10.3390/foods9111575
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</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/6074">
    <dcterms:title><![CDATA[<strong>C&mdash;H Amination via Nitrene Transfer Catalyzed by Mononuclear Non-Heme Iron-Dependent Enzymes</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIOCATALISIS]]></dcterms:subject>
    <dcterms:subject><![CDATA[HIERRO]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2020]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Expanding the reaction scope of natural metalloenzymes can provide new opportunities for biocatalysis. Mononuclear non‐heme iron‐dependent enzymes represent a large class of biological catalysts involved in the biosynthesis of natural products and catabolism of xenobiotics, among other processes. Here, we report that several members of this enzyme family, including Rieske dioxygenases as well as &alpha;‐ketoglutarate‐dependent dioxygenases and halogenases, are able to catalyze the intramolecular C&minus;H amination of a sulfonyl azide substrate, thereby exhibiting a promiscuous nitrene transfer reactivity. One of these enzymes, naphthalene dioxygenase (NDO), was further engineered resulting in several active site variants that function as C&minus;H aminases. Furthermore, this enzyme could be applied to execute this non‐native transformation on a gram scale in a bioreactor, thus demonstrating its potential for synthetic applications. These studies highlight the functional versatility of non‐heme iron‐dependent enzymes and pave the way to their further investigation and development as promising biocatalysts for non‐native metal‐catalyzed transformations.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Vila, Mar&iacute;a Agustina</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Steck, Viktoria</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Rodr&iacute;guez Giordano, Sonia</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Carrera, Ignacio</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Fasan, Rudi</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[ChemBioChem 2020. --p. 1-9]]></dcterms:source>
    <dcterms:publisher><![CDATA[Wiley]]></dcterms:publisher>
    <dcterms:date><![CDATA[2020]]></dcterms:date>
    <dcterms:rights><![CDATA[<strong>Informaci&oacute;n sobre Derechos de Autor</strong> (Por favor lea este aviso antes de abrir los documentos u objetos) <strong>La legislaci&oacute;n uruguaya protege el derecho de autor sobre toda creaci&oacute;n</strong> literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006) ADVERTENCIA - La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.]]></dcterms:rights>
    <dcterms:format><![CDATA[Pdf]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.1002/cbic.201900783]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/6058">
    <dcterms:title><![CDATA[<strong>Identification of Zika Virus NS2B-NS3 Protease Inhibitors by Structure-Based Virtual Screening and Drug Repurposing Approaches</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[VIRUS ZIKA]]></dcterms:subject>
    <dcterms:subject><![CDATA[TECNOLOGIA VIRTUAL]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2020]]></dcterms:subject>
    <dcterms:abstract><![CDATA[The NS2B-NS3 protease has been identified as an attractive target for drug development against Zika virus (ZIKV) and combined drug repurposing and structure-based virtual screening has improved the development of antiviral drugs. In this study, we performed a structure-based virtual screening of 1861 Food and Administration (FDA) approved drugs available in DrugBank by the selection and docking validation of crystal structure of ZIKV NS2B-NS3 protease (PDB ID 5H4I) using Glide and DOCK 6 software. The antihistaminic chlorcyclizine (Grid score &minus;24.8 kcal/mol) exhibited the most promising interaction with NS2B-NS3 protease in comparison to crystallography ligand (Grid score &minus;15.6 kcal/mol) by interaction to Tyr161 by hydrophobic interactions in the binding site of NS2B-NS3 which is recognized as an important amino acid in substrate molecular recognition. Cytotoxicity and global antiviral activity assay in Vero cells by MTT method showed that chlorcyclizine reduced the ZIKV induced cytopathic effect (EC50 of 69.0 &plusmn; 7.3 &mu;M and SI = 1.9), and explicit molecular dynamics simulations implemented on a NAMD program indicated great stability of chlorcyclizine in protease binding site, suggesting the repurposing of chlorcyclizine as a promising finding in anti-ZIKV drug development.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Santos, Felipe</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Nunes, Damiana Ant&ocirc;nia de F&aacute;tima</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Lima, William Gustavo</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Davyt, Danilo</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Lara Santos, Luciana</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Gutteres Taranto, Alex</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Siqueira Ferreira Jaqueline Maria</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[Journal of Chemical Information and Modeling. v. 60, 2020. -- p.731-737]]></dcterms:source>
    <dcterms:publisher><![CDATA[American Chemical Society]]></dcterms:publisher>
    <dcterms:date><![CDATA[2020]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong> (Por favor lea este aviso antes de abrir los documentos u objetos)<strong> La legislaci&oacute;n uruguaya protege el derecho de autor </strong>sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006) ADVERTENCIA - La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[https://doi.org/10.1021/acs.jcim.9b00933]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/6017">
    <dcterms:title><![CDATA[<strong>Survey of B-galactosidase properties : Applications of to transglycosylation process</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[GALACTOSIDASAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2019]]></dcterms:subject>
    <dcterms:subject><![CDATA[LIBROS-ANALITICA]]></dcterms:subject>
    <dcterms:abstract><![CDATA[&beta;-galactosidase is an enzyme responsible for catalyzing the hydrolysis of the lactose &beta;-1,4 linkage into &alpha;-D-glucose and &beta;-D-galactose. &beta;-galactosidase is found in plants, animals and microorganisms. In Beta-Galactosidase: Properties, Structure and Functions, the authors discuss the main microorganisms that produce &beta;-galactosidase, the characteristics of the culture media, bioprocessing parameters, the most relevant downstream steps used in the recovery of microbial &beta;-galactosidase, as well as the main immobilization techniques. Next, this compilation examines &beta;-galactosidases classification, mechanisms, characterization and applications. Recent advances in galacto-oligosaccharides production and purification are also covered, and different challenges and future perspectives are discussed. In the closing study, strains with &beta;-Galactosidase activity were isolated from 25 Yak Yoghourt samples collected from the Gannan pasturing area of Gansu Province. An efficient &beta;-galactosidase producing strain SYA2 screened out from 21 strains was identified as Enterobacter sp. by means of morphological feature observation, physiological and biochemical characteristics measurement, and 16S rDNA sequence analysis. (Imprint: Nova)]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Porci&uacute;ncula Gonz&aacute;lez, Cecilia</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=8c80c1ae8b95cb6b8bc4b6ce3a8d3a39b297d1bd27a3804c09be97adcbe35a3741bd28180c0446feac51238afbedb3cf67010e8ed6fa462a13806c083463ea87&amp;formato=pdf&amp;convocatoria=21" target="_self"><strong>Giacomini, Cecilia.</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=474f369ea3b1fc932eae2ef74a840fde72a287c4022b8c7ae177620a9a9a36a03940b9c9865791e747006099aafe21d37740477c7cf44f84809f96116321782b&amp;formato=pdf&amp;convocatoria=21" target="_self"><strong>Irazoqui, Gabriela</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[Beta-Galactosidase, properties, structure and functions / Eloy Kras.New York: Nova Science Publishers, 2019 p. 65-115]]></dcterms:source>
    <dcterms:publisher><![CDATA[Nova Science Publishers]]></dcterms:publisher>
    <dcterms:date><![CDATA[2019]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong> La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong> ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Capitulo de Libro]]></dcterms:type>
    <dcterms:identifier><![CDATA[ISBN: 978-1-53615-605-8]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5967">
    <dcterms:title><![CDATA[<strong>New ACE-inhibitory peptides derived from &alpha;-lactalbumin produced by hydrolysis with Bromelia antiacantha peptidases</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[PEPTIDOS BIOACTIVOS]]></dcterms:subject>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BROMELIA ANTIACANTHA]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2019]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Angiotensin converting enzyme (ACE) plays a key role in regulating blood pressure and ACE inhibitors are first-line drugs for treating hypertension. Food protein-derived peptides with ACE inhibitory activity are natural and safe alternatives for both prevention and treatment of hypertension. The second most abundant whey protein, &alpha;-lactalbumin (ALA) was hydrolysed with proteases from Bromelia antiacantha Bertol., a native plant. Two new peptides with potent ACE-inhibitory activity: TTFHTSGY (IC50 = 142 &mu;M) and GYDTQAIVQ (IC50 = 1.0 mM) were purified by affinity chromatography and sequences were determined by mass spectrometry. In silico analysis indicated that neither of these peptides was toxic (ToxinPred). Inhibition kinetic analysis showed that TTFHTSGY was a fully functional ACE competitive inhibitor, whereas GYDTQAIVQ caused only partial ACE inhibition. Our results indicate that cysteine peptidases from B. antiacantha hydrolyse ALA to produce novel ACE inhibitory peptides that could be useful even as functional food ingredients.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Villad&oacute;niga, Carolina.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="https://www.google.com/url?sa=t&amp;rct=j&amp;q=&amp;esrc=s&amp;source=web&amp;cd=1&amp;cad=rja&amp;uact=8&amp;ved=2ahUKEwjB76T92L_mAhXALLkGHfUrBZ0QFjAAegQIARAH&amp;url=https%3A%2F%2Fexportcvuy.anii.org.uy%2Fpdf%2F%3Fbd8b7c287e1bdb475b38786d96574bc21c644cc92a497042503b97d738ee7bf7585334f57b6510e7209a7afc9025553d0d1dc743d6968b0ed4c3c847f1701193&amp;usg=AOvVaw3V0pd9Xf__23TQqqL35ob3" target="_self"><strong>Cantera, Ana Mar&iacute;a</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[Biocatalysis and Agricultural Biotechnology v.20, 2019. -- p. 1-7.--e1012158]]></dcterms:source>
    <dcterms:publisher><![CDATA[Elsevier]]></dcterms:publisher>
    <dcterms:date><![CDATA[2019]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong> La legislaci&oacute;n uruguaya</strong> protege el derecho de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006 LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong> ADVERTENCIA</strong> - La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[Pdf]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.1016/j.bcab.2019.101258]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5908">
    <dcterms:title><![CDATA[<strong>Enzymatic synthesis of non-natural trisaccharides and galactosides; Insights of their interaction with galectins as a function of their structure</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[SINTESIS ENZIMATICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[OLISACARIDOS]]></dcterms:subject>
    <dcterms:subject><![CDATA[GALECTINAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[GALACTOSIDASAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2019]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Galectins are a family of carbohydrate-recognizing proteins that by interacting with specific glycoepitopes can mediate important biological processes, including immune cell homeostasis and activation of tolerogenic circuits. Among the different members of this family, Galectin 1 and 3 have shown pro-tumorigenic effects, being overexpressed in numerous neoplasic diseases, proving to be relevant in tumor immune escape, tumor progression and resistance to drug-induced apoptosis. Thus, generation of specific glycosides that could inhibit their pro-tumorigenic ability by blocking their carbohydrate recognition domain is one of the current major challenges in the field. Considering that galectin-ligand binding strength is closely related to the ligand structure, analysis of this relationship provides valuable information for rational design of high-affinity ligands that could work as effective galectin inhibitors. Taking profit of the ability of glycosidases to catalyze transglycosylation reactions we achieved the enzymatic synthesis of &beta;-d-Galp-(1 &rarr; 6)-&beta;-d-Galp-(1 &rarr; 4)-d-Glcp (2), a mixture of &beta;-d-Galp-(1 &rarr; 6)-&beta;-d-Glcp-(1 &rarr; 4)-d-Glcp (5) and &beta;-d-Galp-(1 &rarr; 3)-&beta;-d-Glcp-(1 &rarr; 4)-d-Glcp (6), and finally benzyl &beta;-d-galactopyranoside (9), with reaction yields between 16 and 27%. All the galactosides were purified, and characterized using 1H and 13C nuclear magnetic resonance spectroscopy. Docking results performed between the synthesized compounds and human Galectin 1 (hGal-1) and human Galectin 3 (hGal-3) showed that the replacement of a glucose moiety linked to the terminal galactose with a galactose moiety, decreases the affinity for these galectins. Moreover, regarding the interglycosidic bond the most favorable &beta;-Gal linkage seems to be &beta;(1 &rarr; 4) followed by &beta;(1 &rarr; 3) and &beta;(1 &rarr; 6) for hGal-1, and &beta;(1 &rarr; 4) followed by &beta;(1 &rarr; 6) and &beta;(1 &rarr; 3) for hGal-3. These results were in accordance with the IC50 values obtained with in vitro solid phase inhibition assays. Therefore, docking results obtained in this work proved to be a very good approximation for predicting binding affinity of novel galactosides.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Porci&uacute;ncula Gonz&aacute;lez, Cecilia</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Cagnoni, Alejandro</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Mari&ntilde;o, Karina v.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Fontana, Carolina</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="c" href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=664abf8d2959acb20a57fad7a94769fcd6bcd6cb9185d87136fd434e7fddcd763e08b59175070ea1f148f412f58e75bc27b7717516f5d6c76fd53747356f34d4&amp;formato=pdf&amp;convocatoria=21" target="_self"><strong>Saenz-M&eacute;ndez, Patricia</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=474f369ea3b1fc932eae2ef74a840fde72a287c4022b8c7ae177620a9a9a36a03940b9c9865791e747006099aafe21d37740477c7cf44f84809f96116321782b&amp;formato=pdf&amp;convocatoria=21" target="_self"><strong>Irazoqui, Gabriela</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=8c80c1ae8b95cb6b8bc4b6ce3a8d3a39b297d1bd27a3804c09be97adcbe35a3741bd28180c0446feac51238afbedb3cf67010e8ed6fa462a13806c083463ea87&amp;formato=pdf&amp;convocatoria=21" target="_self"><strong>Giacomini, Cecilia.</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[Carbohydrate Research v. 472, 2019. -- p. 1-15]]></dcterms:source>
    <dcterms:publisher><![CDATA[Elsevier]]></dcterms:publisher>
    <dcterms:date><![CDATA[2019]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong> La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.1016/j.carres.2018.10.011]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5851">
    <dcterms:title><![CDATA[<strong>Yeasts from Tierra Del Fuego Province (Argentina) : Biodiversity, Characterization and Bioprospection of Hydrolytic Enzymes</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[ LEVADURAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[ ARGENTINA]]></dcterms:subject>
    <dcterms:subject><![CDATA[ ENZIMAS HIDROLITICAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIODIVERSIDAD]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2019]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Antarctic and sub-Antarctic regions are &ndash; with Polar Regions, mountains and the deep sea &ndash; the most extreme environments on Earth because of its low temperatures, dryness, high incidence of solar radiation and low nutrient availability. Nevertheless, microorganisms have successfully colonized these regions. In this study, culturable yeasts from soil samples collected from two different locations, a human-impacted area (Encerrada Bay) and a largely pristine and naturally vegetated area near Lago Escondido city (54&deg;39&prime;0&Prime;S, 67&deg;46&prime;48&Prime;W) from Tierra del Fuego province, Argentina were identified and characterized at different levels. They were characterized and classified as psychrotolerant and were considered as moderately halotolerant because of their ability to grow in the presence of 1.5 M of NaCl. Yeasts from phylum Ascomycota were affiliated to five genera: Candida, Yarrowia, Debaryomyces, Nadsonia, and Wickerhamiella, whereas from phylum Basidiomycota yeasts were affiliated to six genera: Naganishia, Rhodotorula, Leucosporidum, Tausonia, Cystofilobasidium, and Apiotrichum. Most of the yeasts demonstrated at least one extracellular enzymatic activity (mainly &beta;-glucosidase, esterase, and protease activities). One isolate identified as Tausonia pullulans showed significant activity across the eight enzyme types tested. In light of these findings, Tierra del Fuego province could be considered as a cold environment with a potential source of cold-adapted yeasts producing industrially relevant cold-active enzymes.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Cavello, Ivana Alejandra</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Bezus, Brenda</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Mart&iacute;nez, Adalgisa</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=1abff03565910db14be63e86513a20cbe627ac482e68a4d87cfd73350dc31d1eb17260fc580c9ceb9a08945c38c4a9800c63804476aac1e7069d68e0f8a8b7fe&amp;formato=pdf&amp;convocatoria=21" target="_self"><strong>Garmendia, Gabriela.</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=513cd40ab0f7a3ae4d114f4a4e9dc877c410ad8f0bff71b7001257cfe95eca4576e784b3d7ba4a4ef9b56967d3205b0cb2adc6266bf6792221c2f2f8b5f7200e&amp;formato=pdf&amp;convocatoria=21" target="_self"><strong>Vero, Silvana.</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Cavalitto, Sebasti&aacute;n</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[Geomicrobiology Journal v.36, no. 9, 2019. -- p. 847-857]]></dcterms:source>
    <dcterms:publisher><![CDATA[Taylor and Francis]]></dcterms:publisher>
    <dcterms:date><![CDATA[2019]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.1080/01490451.2019.1641769]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5826">
    <dcterms:title><![CDATA[<strong>Celulasas sicr&oacute;filas, una innovaci&oacute;n en la industria del bioetanol</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[BIOQU&Iacute;MICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIOTECNOLOGIA]]></dcterms:subject>
    <dcterms:subject><![CDATA[CELULASA]]></dcterms:subject>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIOETANOL]]></dcterms:subject>
    <dcterms:subject><![CDATA[SICI&Oacute;FILOS]]></dcterms:subject>
    <dcterms:abstract><![CDATA[En este trabajo de tesis se han explorado dos metodolog&iacute;as en la b&uacute;squeda de la obtenci&oacute;n de nanopart&iacute;culas de boratos de zinc. Estas metodolog&iacute;as fueron planteadas para lograr sintetizar fases de boratos de zinc en distintos rangos de temperaturas, lo que brinda grandes posibilidades en el desarrollo de aplicaciones tecnol&oacute;gicas. Empleando la s&iacute;ntesis por combusti&oacute;n de gel asistida se pretendi&oacute; sintetizar boratos de zinc a temperatura mayores a 250 &deg;C, para los cuales se esperaba obtener nanopart&iacute;culas que fueran importantes en el desarrollo de nuevos aditivos de materiales que se preparan a altas temperaturas, por ejemplo, pl&aacute;sticos. A partir de las s&iacute;ntesis asistidas por micelas reversas, se pretendi&oacute; obtener boratos de zinc a baja temperatura, por ejemplo, los aminoboratos de zinc [Zn(NH3)3B4O5(OH)4]&middot;H2O (ZB1) y Zn3(H2B3O7)2&middot;2NH3&middot;4H2O (ZB2), reportados previamente durante mi trabajo de Licenciatura en Qu&iacute;mica. Mediante la metodolog&iacute;a de combusti&oacute;n de gel asistida se logr&oacute; sintetizar la fase ZnB4O7. Los resultados presentados para estas s&iacute;ntesis son contundentes respecto a los procesos qu&iacute;micos que tienen lugar en el sistema estudiado. El medio reductor ofrecido por la alta concentraci&oacute;n de amonio da lugar a la formaci&oacute;n de carbono amorfo que permanece como principal impureza en las muestras obtenidas, no siendo posible la obtenci&oacute;n de nanopart&iacute;culas de boratos de zinc. La obtenci&oacute;n de ZB2 por m&eacute;todos de baja temperatura fue posible a partir de un sistema coloidal mantenido por agitaci&oacute;n formado por agua, CTAB, hexano y diferentes alcoholes como cosurfactantes. Para estos sistemas se obtuvo la fase cristalina ZB2 con tama&ntilde;os entre 100 y 1000 nm, report&aacute;ndose tama&ntilde;os menores a 150 nm cuando se emple&oacute; isopropanol como cosurfactante. Tambi&eacute;n se sintetiz&oacute; la fase ZB2 en un medio de micelas reversas. Este &uacute;ltimo es uno de los logros m&aacute;s importantes de este trabajo, ya que se consigui&oacute; estabilizar un sistema de micelas reversas y obtener un producto con un tama&ntilde;o de part&iacute;cula menor a 150 nm. Este trabajo es un aporte importante en la qu&iacute;mica b&aacute;sica de estos sistemas, abriendo puertas a futuros estudios de s&iacute;ntesis en sistemas de micelas reversas. La metodolog&iacute;a utilizada para determinar las condiciones de formaci&oacute;n de micelas reversas es extrapolable a cualquier sistema de obtenci&oacute;n de compuestos qu&iacute;micos a partir de una soluci&oacute;n acuosa con par&aacute;metros de concentraci&oacute;n y fuera i&oacute;nica adecuados. Los estudios microbiol&oacute;gicos realizados sobre la fase ZB2 permitieron confirmar la actividad antif&uacute;ngica y antibacteriana presentada por este compuesto y su dependencia con el tama&ntilde;o de part&iacute;cula]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Herrera, Lorena.</strong>]]></dcterms:creator>
    <dcterms:publisher><![CDATA[Montevideo: Udelar-Facultad de Química]]></dcterms:publisher>
    <dcterms:date><![CDATA[2019]]></dcterms:date>
    <dcterms:contributor><![CDATA[<strong><a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=729d3d9bb07d7be0ba5e4dc762c01e29" target="_self">Franco Fraguas, Laura</a></strong>]]></dcterms:contributor>
    <dcterms:contributor><![CDATA[<strong>Castro, Susana</strong>]]></dcterms:contributor>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[Papel]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Tesis]]></dcterms:type>
    <dcterms:identifier><![CDATA[577.1 HER]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5822">
    <dcterms:title><![CDATA[<strong>Production of D-tagatose and D-fructose from whey by co-immobilized enzymatic system</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[SUERO]]></dcterms:subject>
    <dcterms:subject><![CDATA[FRUCTUOSA]]></dcterms:subject>
    <dcterms:subject><![CDATA[INMOVILIZACION DE ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2019]]></dcterms:subject>
    <dcterms:abstract><![CDATA[&beta;-Galactosidase from Bacillus circulans, l-arabinose (d-galactose) isomerase from Enterococcus faecium and d-xylose (d-glucose) isomerase from Streptomyces rubiginosus, immobilized individually and co-immobilized onto Eupergit C and Eupergit C 250&thinsp;L, were used batchwise in mono- and multi-bioreactor systems for lactolysis/isomerization processes in Mozzarella cheese whey. The degrees of lactolysis achieved with the multienzymatic systems were significantly higher than those obtained by using mono-enzymatic processes with immobilized &beta;-galactosidase. This effect was observed when at least one of the isomerases was present in the reactor, suggesting a reduction in product inhibition of lactolysis as a result of decrease in d-galactose and/or d-glucose levels during reaction. Temperature was the main factor that affected d-tagatose/d-galactose and d-fructose/d-glucose ratios. Degree of lactolysis achieved at 50&thinsp;&deg;C was between 88% and 100%. Mono-reactor processes with co-immobilized stabilized tri-enzymatic systems exhibited the best performances regarding conversion degrees (producing complete lactolysis, 45% d-tagatose and 39% d-fructose against 93% lactolysis, 40% d-tagatose and 29% d-fructose for mono-reactor processes with individually immobilized enzymes). Stabilized co-immobilized enzymes were able to improve further to 53% the yield in d-fructose when demineralized Mozzarella cheese whey was employed as substrate. The productivities were moderate, ranging 9.5&ndash;10&thinsp;g/Lh in terms of d-tagatose. Stabilized derivatives could be reused for at least 12 cycles in batch bio-reactors.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Torres, Pedro</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="https://www.google.com/url?sa=t&amp;rct=j&amp;q=&amp;esrc=s&amp;source=web&amp;cd=1&amp;ved=2ahUKEwjMpqqk17_mAhURA9QKHdpCDWoQFjAAegQIAhAH&amp;url=https%3A%2F%2Fexportcvuy.anii.org.uy%2FCvEstatico%2F%3FurlId%3Dbdd067f4b1b8fa059782e3e95521aaa16343c974cf882a9fb942c2f9a70e3e2d28d24a267afde55919add09cb3bff5a88dda976b68929de358c4acefe988f545%26formato%3Dpdf%26convocatoria%3D21&amp;usg=AOvVaw3lmlSV2CODwKIRjXTVF_3B" target="_self"><strong>Batista Viera, Francisco.</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[Molecular Catalysis&nbsp; v. 463, 2019. -- p. 99-109]]></dcterms:source>
    <dcterms:publisher><![CDATA[Elsevier]]></dcterms:publisher>
    <dcterms:date><![CDATA[2019]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Artículo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.1016/j.mcat.2018.11.017]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5697">
    <dcterms:title><![CDATA[<strong>Elucidation of the O-antigen structure of Escherichia coli O63</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[ESCHERICHIA COLI]]></dcterms:subject>
    <dcterms:subject><![CDATA[ANTIGENOS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2018]]></dcterms:subject>
    <dcterms:abstract><![CDATA[The structure of the O-antigen polysaccharide (PS) from the Shiga-toxin producing Escherichia coli O63 has been elucidated using a combination of bioinformatics, component analyses and NMR spectroscopy. The O-antigen is comprised of tetrasaccharide repeating units with the following structure: &rarr;2)-&beta;-d-Quip3N(d-allo-ThrAc)-(1&rarr;2)-&beta;-d-Ribf-(1&rarr;4)-&beta;-d-Galp-(1&rarr;3)-&alpha;-d-GlcpNAc-(1&rarr; in which the N-acetylated d-allo-threonine is amide-linked to position 3 of the 3-amino-3-deoxy-d-Quip sugar residue. The presence of a predicted flippase and polymerase encoded in the O63 gene cluster is consistent with the Wzx/Wzy biosynthetic pathway and consequently the biological repeating unit has likely an N-acetyl-d-glucosamine residue at its reducing end. A bioinformatics approach based on predictive glycosyltransferase function present in ECODAB (E. coli O-antigen database) suggested the structural element &beta;-d-Galp-(1&rarr;3)-d-GlcpNAc in the O-antigen. Notably, multiple gene sequence alignment of fdtA and qdtA from E. coli to that in E. coli O63 resulted in discrimination between the two, confirmation of the latter in E. coli O63, and consequently, together with qdtB, biosynthesis of dTDP-d-Quip3N. The E. coli O63 O-antigen polysaccharide differs in two aspects from that of E. coli O114 where the latter carries instead an l-serine residue, and the glycosidic linkage positions to and from the Quip3N residue are both changed. The structural characterization of the O63 antigen repeat supports the predicted functional assignment of the O-antigen cluster genes.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>St&aring;hle, J.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Fontana, C.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Weintraub, A.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Widmalm, G.</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[Glycobiology v.29, no.2, 2018. --p. 179-187]]></dcterms:source>
    <dcterms:publisher><![CDATA[Oxford University Press]]></dcterms:publisher>
    <dcterms:date><![CDATA[2018]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Artículo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI:10.1093/glycob/cwy098]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5687">
    <dcterms:title><![CDATA[<strong>The use of magnetic nanoparticles for immobilization and recycling of enzymes</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[NANOTECNOLOGIA]]></dcterms:subject>
    <dcterms:subject><![CDATA[INMOVILIZACION DE ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[NANOPARTICULAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:abstract><![CDATA[The use of nanostructured materials for enzyme immobilization is an active field of research due to its large surface area and the new emergent properties derived from its size. The present work is focused on the synthesis of magnetic nanoparticles for the adsorption of cysteine-proteolytic enzymes extracted from Bromelia antiacantha Bertol (Bromeliaceae) fruit. The results show that enzyme adsorption is highly dependent on the temperature and pH. The biocatalyst activity increased up to 40 %, once immobilized onto the magnetic nanoparticles. In addition, they can be recovered using a magnet allowing them to be reused up to 5 cycles with a marginal loss (5 %) of the initial activity.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Furtado, Shirley</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Brandes, Mariana</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Alam&oacute;n, Catalina</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Botasini, Santiago</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="https://www.google.com/url?sa=t&amp;rct=j&amp;q=&amp;esrc=s&amp;source=web&amp;cd=1&amp;cad=rja&amp;uact=8&amp;ved=2ahUKEwjB76T92L_mAhXALLkGHfUrBZ0QFjAAegQIARAH&amp;url=https%3A%2F%2Fexportcvuy.anii.org.uy%2Fpdf%2F%3Fbd8b7c287e1bdb475b38786d96574bc21c644cc92a497042503b97d738ee7bf7585334f57b6510e7209a7afc9025553d0d1dc743d6968b0ed4c3c847f1701193&amp;usg=AOvVaw3V0pd9Xf__23TQqqL35ob3" target="_self"><strong>Cantera, Ana Mar&iacute;a</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[MRS Advances&nbsp; v. 3, no 61, 2018. -- p. 3581-3587]]></dcterms:source>
    <dcterms:publisher><![CDATA[Cambridge]]></dcterms:publisher>
    <dcterms:date><![CDATA[2018]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.1557/adv.2018.559]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5594">
    <dcterms:title><![CDATA[<strong>A computer model-built structure of the T. Congolense Trypathione reductase in complex with NADP</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[TRIPATIONA REDUCTASA]]></dcterms:subject>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[1992]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[COMPLEJOS]]></dcterms:subject>
    <dcterms:abstract><![CDATA[A three-dimensional structure is engineered for the Trypanosoma congolense trypanothione reductase (TpR) using the sequence homology with glutathione reductase (GR) and lipoamide dehydrogenase, molecular graphics, energy optimization and molecular dynamics techniques. The model was extended to include the complex with the coenzyme nicotinamide adenine dinucleotide phosphate (NADP). The TpR-NADP structure is compared with X-ray data from the glutathione reductase complex with the reduced NADP (NADPH). A model of TpR-NADP including the trypanothione substrate is presented, and an electron-transfer mechanism is proposed.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Horjales, Eduardo</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Oliva, B.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Stamato, F.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="https://exportcvuy.anii.org.uy/CvEstatico/?urlId=8e4377ca77382678fd5af0d455590aa18a44e65bac89340cfafbbd41152343acd96dc3153f75f2fdf08a92578f213300543d33a6754527876021976e495c507b&amp;formato=pdf&amp;convocatoria=21" target="_self"><strong>Paulino, Margot.</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Nilsson, O.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Tapia, Orlando.</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[Molecular Engineering&nbsp; v. 1, , 1992. -- p. 357]]></dcterms:source>
    <dcterms:publisher><![CDATA[Springer]]></dcterms:publisher>
    <dcterms:date><![CDATA[1992]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.1007/BF00176807]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5394">
    <dcterms:title><![CDATA[<strong>Characterization of catalytic and non-catalytic activities of EgGST2-3, a heterodimeric glutathione transferase from Echinococcus granulosus</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[GLUTATION TRANSFERASA]]></dcterms:subject>
    <dcterms:subject><![CDATA[ECHINOCOCCUS GRANULOSUS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2018]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Glutathione transferases (GSTs) perform several catalytic and non-catalytic roles in the defense against toxicities of electrophile compounds and oxidative stress, and therefore are involved in stress-response and cell detoxification. Previously, we have provided evidence indicating that EgGST2 and EgGST3, two phylogenetically distant Echinococcus granulosus GSTs, can naturally form a heterodimeric structure (EgGST2-3). In the present work, the recombinant heterodimer GST (rEgGST2-3) is characterized. Hence, rEgGST2-3 was able to conjugate GSH to three substrates: 1-chloro-2,4-dinitrobenzene (CDNB, general substrate for GSTs), 1,2-dichloro-4-nitrobenzene (specific substrate for mammalian Mu class) and trans,trans-deca-2,4-dienal (reactive carbonyl). The canonical activity was considerably reduced by all the conventional inhibitors (cybacron blue, triphenylthin chloride and bromosulfophthalein) and by other inhibitors (ellagic acid, alizarin and chenodeoxycholic acid). Besides this, rEgGST2-3 activity was inhibited by a number of anthelmintic drugs, where the halogenated phenolic drugs (mainly bithionol and hexachlorophene) acted as stronger inhibitors, suggesting they may bind to the EgGST2-3. Moreover, rEgGST2-3 exhibited glutathione-peroxidase activity, and its specific constant (kcat/KM) was calculated. Finally, rEgGST2-3 displayed the ability to bind non-substrate molecules, particularly anthelmintic drugs, suggesting that ligandin activity may have potential to act as a passive protection parasite mechanism. Overall, the rEgGST2-3 behavior was shown to be both complementary and redundant to that reported for rEgGST1, another characterized GST from E. granulosus. It would be appropriate that different enzymes in the same organism do not have exactly the same functional properties to develop a better adaptation to life in the host.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>L&oacute;pez, Ver&oacute;nica.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>La Rocca, S.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Arbildi Torres, Paula.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=df0341a1f28a6244d86ad94a750c3ec2" target="_self"><strong>Fern&aacute;ndez, Ver&oacute;nica.</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[Acta Tropica&nbsp; v. 180, 2018. -- p. 69-75]]></dcterms:source>
    <dcterms:publisher><![CDATA[Elsevier]]></dcterms:publisher>
    <dcterms:date><![CDATA[2018]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong> ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.1016/j.actatropica.2018.01.007]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5347">
    <dcterms:title><![CDATA[<strong>Production and characterization of a b-glucosidase from Issatchenkia terricola and its use for hydrolysis of aromatic precursors in Cabernet Sauvignon wine</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[GLUCOSIDASA]]></dcterms:subject>
    <dcterms:subject><![CDATA[VINO]]></dcterms:subject>
    <dcterms:subject><![CDATA[VINO CABERNET SAUVIGNON]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2018]]></dcterms:subject>
    <dcterms:abstract><![CDATA[New enzymes isolated from the biodiversity of native wine ecosystems could contribute to increase the varietal character of regional wines. This study reports on the production and characterization of Issatchenkia terricola, beta-glucosidase and its potential to release red-wine aromatic compounds. The enzyme, a monomer of 48 kDa with an isoelectric point of 3.5 is tolerant to glucose and ethanol, properties compatible with enological use. Although fed-batch is usually the most suitable system for enzyme production in submerged culture, in this case the yield was practically the same as in batch culture. Enzyme productivity was increased 2-fold in synthetic medium with glucose with respect to the YPG and 3&ndash;8-fold with respect to other media assayed. After enzymatic treatment, GC-MS analysis of the released aglycones demonstrated significant increases in the concentration of phenols (83%) and norisoprenoids (65%). According to the judges of the sensory panel, the treatment resulted in a wine with dried fruits and raisins notes, as compared to the control, which was found more sweet and fruity. This, together with the lack of activity on anthocyanin glycosides, highlights the potential of this enzyme in enology, since its high selectivity allowed the development of aroma without compromising wine color.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>de Ovalle, Stefani</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Cavello, Ivana</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=586cda0b970a37c5463af91ae8481fed" target="_self"><strong>Brena, Beatriz M.</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Cavalitto, Sebasti&aacute;n</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Gonz&aacute;lez Pombo, Paula</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[LWT - Food Science and Technology v. 87, 2018. -- p. 515-522]]></dcterms:source>
    <dcterms:publisher><![CDATA[Elsevier]]></dcterms:publisher>
    <dcterms:date><![CDATA[2018]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong> La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong> ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.1016/j.lwt.2017.09.026]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5334">
    <dcterms:title><![CDATA[<strong>Butylamine as an alternative amine donor for the stereoselective biocatalytic transamination of ketones</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIOCATALISIS]]></dcterms:subject>
    <dcterms:subject><![CDATA[TRANSAMINASAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[CETONAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BUTILAMINA]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2018]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Formal reductive amination has been a main focus of biocatalysis research in recent times. Among the enzymes able to perform this transformation, pyridoxal-5&prime;-phosphate-dependent transaminases have shown the greatest promise in terms of extensive substrate scope and industrial application. Despite concerted research efforts in this area, there exist relatively few options regarding efficient amino donor co-substrates capable of allowing high conversion and atom efficiency with stable enzyme systems. Herein we describe the implementation of the recently described spuC gene, coding for a putrescine transaminase, exploiting its unusual amine donor tolerance to allow use of inexpensive and readily-available n-butylamine as an alternative to traditional methods. Via the integration of SpuC homologues with tandem co-product removal and cofactor regeneration enzymes, high conversion could be achieved with just 1.5 equivalents of the amine with products displaying excellent enantiopurity.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Slabu, Justina</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Galman, James L.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Iglesias, Cesar</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Weise, Nicholas J.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Lloyd, Richard C.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Turner, Nicholas J.</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[Catalysis Today v. 306, 2018. -- p. 96-101]]></dcterms:source>
    <dcterms:publisher><![CDATA[Elsevier]]></dcterms:publisher>
    <dcterms:date><![CDATA[2018]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong> La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI:10.1016/j.cattod.2017.01.025]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5306">
    <dcterms:title><![CDATA[<strong>Antiacanthain A : New proteases isolated from Bromelia antiacantha Bertol. (Bromeliaceae)</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[ENZIMAS PROTEOLITICAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[PROTEASA VEGETAL]]></dcterms:subject>
    <dcterms:subject><![CDATA[BROMELIACEAE]]></dcterms:subject>
    <dcterms:subject><![CDATA[CISTEINA PEPTIDASA]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2018]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Crude extract (CE) from pulp of Bromelia antiacantha Bertol. mature fruit, contains at least 3 cysteine proteases with proteolytic activity. By single step cation exchange chromatography (Hi-trap SP-HP) of partially purified CE, the protease with the lowest pI, Antiacanthain A (AntA), was isolated. It showed maximum activity at pH9, and 75% of remaining activity was maintained over a wide pH range (pH6-10). The AntA activity exhibits a constant increase up to 70&deg;C. Maintains almost 100% of its activity at 45 at pH6 and 9. A 60% of AntA was active by titration with specific inhibitor, E64. Amidasic activity was studied with pyroglutamyl-phenyl-leucyl-paranitroaniline (PFLNA) substrate having higher AntA catalytic efficiency of (kcat/Km=470s-1M-1) relative to stem bromelain (kcat/Km=305s-1M-1). Esterase activity using p-nitrophenyl esters of N-&alpha;-CBZ-l-Lysine (z-L-LysONp) showed a 10-fold higher catalytic efficiency for AntA (kcat/Km=6376s-1M-1) relative to stem bromelain (kcat/Km=688s-1M-1). Incubation with 8M Urea did not affect AntA activity and remained unchanged for 18h, with 6M GndHCl resulted in a 41% decrease in activity after 30min incubation, maintained this activity 18h. AntA exhibits high sequence identity with proteases of the Bromeliaceae family.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Vall&eacute;s, Diego</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=c9b619bc33041fed5a5c6f6644c2e410" target="_self"><strong>Cantera, Ana M. B.</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[International Journal of Biological Macromolecules v. 113, 2018. -- p. 916-923]]></dcterms:source>
    <dcterms:publisher><![CDATA[Elsevier]]></dcterms:publisher>
    <dcterms:date><![CDATA[2018]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.1016/j.ijbiomac.2018.03.025]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5296">
    <dcterms:title><![CDATA[<strong>An isomerase completes the circuit for a redox switch</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[TRANSGLUTAMINASA 2]]></dcterms:subject>
    <dcterms:subject><![CDATA[ESTADOS PATOLOGICOS]]></dcterms:subject>
    <dcterms:subject><![CDATA[REDOX]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2018]]></dcterms:subject>
    <dcterms:abstract><![CDATA[The activity of human transglutaminase 2 (TG2), which forms protein cross-links between glutamine and lysine residues, is controlled by an allosteric disulfide bond. However, the mechanism by which this bond is formed, like many systems regulated by oxidative cysteine modifications, was not clear. A new study from Khosla and colleagues shows that TG2 is oxidatively inactivated by the protein disulfide isomerase ERp57, providing the first example of a defined and reversible protein-controlled redox switch and pointing to new strategies to inhibit undesirable TG2 activity in pathological states.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=8b2cacb0aafc512133624fa7b9bf174c" target="_self"><strong>Salinas, Gustavo.</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[Journal of Biological Chemistry&nbsp; v. 293, no. 8, 2018. -- p. 2650-2651]]></dcterms:source>
    <dcterms:publisher><![CDATA[American Society for Biochemistry and Molecular Biology]]></dcterms:publisher>
    <dcterms:date><![CDATA[2018]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong> La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI 10.1074/jbc.H118.001807]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5232">
    <dcterms:title><![CDATA[<strong>Identification of novel glutathione transferases in Echinococcus granulosus : An evolutionary perspective</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[GLUTATION TRANSFERASA]]></dcterms:subject>
    <dcterms:subject><![CDATA[ECHINOCOCCUS GRANULOSUS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2012]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Glutathione transferase enzymes (GSTs) constitute a major detoxification system in helminth parasites and have been related to the modulation of host immune response mechanisms. At least three different GSTs classes have been described in Platyhelminthes: Mu, Sigma and Omega. Mining the genome of Echinococcus multilocularis and the ESTs databases of Taenia solium and E. granulosus identified two new GSTs from the cestode E. granulosus, named EgGST2 and EgGST3. It also revealed that the Omega class of GSTs was absent from the Taenidae family. EgGST2 and EgGST3 are actively expressed in the parasite. In order to know the origin of these new GSTs, in silico analyses were performed. While EgGST2 is classified as belonging to the Sigma class, the data obtained for EgGST3 allowed a less clear interpretation. The study of the evolutionary relatedness based on the C-terminal domain sequence, gene structure conservation and three-dimensional structure predictions, suggests that EgGST3 is derived from the Platyhelminthes' Sigma-class cluster. Interestingly, the N-terminal domain displays some characteristic Omega-class residues, including a Cys residue that is likely to be involved in the catalytic mechanism. We discuss different evolutionary scenarios that could explain the observed patterns.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Iriarte, Ana</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Arbildi Torres, Paula.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>La Rocca, Silvana.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Musto, H&eacute;ctor</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Fern&aacute;ndez, Ver&oacute;nica.</strong>]]></dcterms:creator>
    <dcterms:source><![CDATA[Acta Tropica v. 123, 2012. -- p. 208-216]]></dcterms:source>
    <dcterms:publisher><![CDATA[Elsevier]]></dcterms:publisher>
    <dcterms:date><![CDATA[2012]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong></p>
<p>(Por favor lea este aviso antes de abrir los documentos u objetos)</p>
<p><strong>La legislaci&oacute;n uruguaya protege el derecho</strong> de autor sobre toda creaci&oacute;n literaria, cient&iacute;fica o art&iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&oacute;n a lo establecido por el derecho com&uacute;n y las siguientes leyes (LEY 9.739 DE 17 DE DICIEMBRE DE 1937 SOBRE PROPIEDAD LITERARIA Y ARTISTICA CON LAS MODIFICACIONES INTRODUCIDAS POR LA LEY DE DERECHO DE AUTOR Y DERECHOS CONEXOS No. 17.616 DE 10 DE ENERO DE 2003, LEY 17.805 DE 26 DE AGOSTO DE 2004, LEY 18.046 DE 24 DE OCTUBRE DE 2006)</p>
<p><strong>ADVERTENCIA -</strong> La consulta de este documento queda condicionada a la aceptaci&oacute;n de las siguientes condiciones de uso: Este documento es &uacute;nicamente para usos privados enmarcados en actividades de investigaci&oacute;n y docencia. No se autoriza su reproducci&oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&oacute;n o cita de partes debe indicarse el nombre de la persona autora.</p>]]></dcterms:rights>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Art&iacute;culo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI:10.1016/j.actatropica.2012.05.010]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5220">
    <dcterms:title><![CDATA[<strong>Enzimas proteol&iacute;ticas de origen vegetal</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[<strong>ENZIMAS</strong>]]></dcterms:subject>
    <dcterms:subject><![CDATA[<strong>PLANTAS (BOTANICA)</strong>]]></dcterms:subject>
    <dcterms:subject><![CDATA[<strong>PAPAINA</strong>]]></dcterms:subject>
    <dcterms:subject><![CDATA[<strong>BROMELINA</strong>]]></dcterms:subject>
    <dcterms:publisher><![CDATA[Biblioteca-FQ]]></dcterms:publisher>
    <dcterms:date><![CDATA[1985]]></dcterms:date>
    <dcterms:format><![CDATA[Papel]]></dcterms:format>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Bibliograf&iacute;a]]></dcterms:type>
    <dcterms:temporal><![CDATA[1978-1982]]></dcterms:temporal>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5211">
    <dcterms:title><![CDATA[<strong>Metalotioneina (enzima)</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[<strong>METALOTIONEINA</strong>]]></dcterms:subject>
    <dcterms:subject><![CDATA[<strong>ENZIMAS</strong>]]></dcterms:subject>
    <dcterms:subject><![CDATA[<strong>METALLOTHIONEIN</strong>]]></dcterms:subject>
    <dcterms:publisher><![CDATA[Biblioteca-FQ]]></dcterms:publisher>
    <dcterms:date><![CDATA[1985]]></dcterms:date>
    <dcterms:format><![CDATA[Papel]]></dcterms:format>
    <dcterms:format><![CDATA[PDF]]></dcterms:format>
    <dcterms:language><![CDATA[Ingl&eacute;s]]></dcterms:language>
    <dcterms:type><![CDATA[Bibliograf&iacute;a]]></dcterms:type>
    <dcterms:temporal><![CDATA[1981-1982]]></dcterms:temporal>
</rdf:Description></rdf:RDF>
