<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/5338">
    <dcterms:title><![CDATA[<strong>Immobilization of &beta;-galactosidase and &alpha;-mannosidase onto magnetic nanoparticles : A strategy for increasing the potentiality of valuable glycomic tools for glycosylation analysis and biological role determination of glycoconjugates</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[INMOVILIZACION DE ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[GLICOSIDASAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[ANALISIS GLICOMICO]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2018]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Glycans present in biological glycoconjugates have several structural and functional roles. Elucidation of glycan structure and biological function is critical to understand their role in physiological and pathogenic process, enabling the development of diagnostic methods and disease treatment. Immobilized glycosidases are powerful tools for glycan analysis, as they are able to remove specific carbohydrates without altering the protein structure. Here we describe the individual immobilization of Aspergillus oryzae &beta;-galactosidase and Canavalia ensiformis &alpha;-mannosidase onto agarose and silica magnetic nanoparticles activated with cyanate ester groups. High immobilization yields (70&ndash;90%) were achieved, keeping above 60% of its original activity. Immobilized glycosidases were effective in the selective deglycosylation of model glycoproteins and a Fasciola hepatica lysate, evidenced by a decrease in specific lectin recognition of 40&ndash;50% after enzymatic deglycosylation. Immobilized glycosidases were reused for several deglycosylation cycles without loss of effectiveness. Their use was extended to the elucidation of the glycan role of native glycoconjugates. A decrease in the recognition of lactoferrin treated with &alpha;-mannosidase by a C-type lectin receptor, DC-SIGN was found. Also the specific deglycosylation of a F. hepatica lysate demonstrated the relevance of mannosylated glycans in the induction of Th2/Treg immune responses during the infection. Our results show successful immobilization of specific glycosidases in nano-supports and validate their utility to identify glycans biological functions.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Rodr&iacute;guez, Ernesto</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Francia, Karen.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Brossard, Natalie</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Garc&iacute;a Vallejo, Juan J.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Kalay, Hakan</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>van Kooyk, Ivette</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Freire, Teresa</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=3c8a423235a59fcbc901eec52b2b7794" target="_self"><strong>Giacomini, Cecilia</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[Enzyme and Microbial Technology&nbsp; v. 117, 2018. --&nbsp;&nbsp;&nbsp;&nbsp; p. 45-55]]></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.enzmictec.2018.05.012]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/5328">
    <dcterms:title><![CDATA[<strong>General Method for the Synthesis of -Conduritol C and Analogs from Chiral Cyclohexadienediol Scaffolds</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[GLICOSIDASA]]></dcterms:subject>
    <dcterms:subject><![CDATA[GLICOSIDASA-INHIBIDORES]]></dcterms:subject>
    <dcterms:subject><![CDATA[CONDURITOL C]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIOCATALISIS]]></dcterms:subject>
    <dcterms:subject><![CDATA[ESTRUCTURA CRISTALINA]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2018]]></dcterms:subject>
    <dcterms:abstract><![CDATA[An efficient and facile general method for the synthesis of conduritol C analogs, taking advantage of an enantioselective biocatalysis process of monosubstituted benzenes, is described. The absolute stereochemical patterns of the target molecules (&minus;)-conduritol C, (&minus;)-bromo-conduritol C, and (&minus;)-methyl-conduritol C were achieved by means of chemoenzymatic methods. The stereochemistry present at the homochiral cyclohexadiene-cis-1,2-diols derived from the arene biotransformation and the enantioselective ring opening of a non-isolated vinylepoxide derivative permitted the absolute configuration of the carbon bearing the hydroxyl groups at the target molecules to be established. All three conduritols and two intermediates were crystallized, and their structures were confirmed by X-ray diffraction. The three conduritols and intermediates were isostructural. The versatility of our methodology is noteworthy to expand the preparation of conduritol C analogs starting from toluene dioxygenase (TDO) monosubstituted arene substrates.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Tibhe, Gaurao D.</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Mac&iacute;as, Mario A</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=0b6d7b4c1f21766e03e6c9354d672f8d" target="_self"><strong>Schapiro, Valeria</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=8b1a957170f0b5988597d2cc3d6f732b" target="_self"><strong>Suescun, Leopoldo</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="ttp://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=1ad085b4305ec8d8997ce8a565b947d4" target="_self"><strong>Pandolfi Graziosi, Enrique.</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[Molecules&nbsp; v. 23, 2018. --9p.--e1653]]></dcterms:source>
    <dcterms:publisher><![CDATA[MDPI]]></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[Articulo]]></dcterms:type>
    <dcterms:identifier><![CDATA[DOI: 10.3390/molecules23071653]]></dcterms:identifier>
</rdf:Description><rdf:Description rdf:about="https://riquim.fq.edu.uy/items/show/3761">
    <dcterms:title><![CDATA[<strong>Enzymatic synthesis of 3-aminopropyl-1-O-&beta;-Dgalactopyranoside catalyzed by Aspergillus oryzae &beta;-galactosidase</strong>]]></dcterms:title>
    <dcterms:subject><![CDATA[ENZIMAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[GALACTOSIDASAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[GLICOSIDASAS]]></dcterms:subject>
    <dcterms:subject><![CDATA[BIBLIOGRAFIA NACIONAL QUIMICA]]></dcterms:subject>
    <dcterms:subject><![CDATA[2015]]></dcterms:subject>
    <dcterms:abstract><![CDATA[Glycosidases represent excellent green chemistry alternatives as catalysts for the synthesis of glycosides, and in particular their stereoselectivity allows the production of anomerically pure glycosides, in only one reaction step using mild reaction conditions. Here, we report the enzymatic synthesis and structural characterization of 3-aminopropyl-1-O-&beta;-D-galactopyranoside. Optimal reaction conditions for the transgalactosylation reaction were 100&thinsp;mM lactose, 500&thinsp;mM 3-amino-1-propanol and 24 h of incubation at 50&thinsp;&deg;C with 6 U/mL of &beta;-galactosidase from Aspergillus oryzae. The fact that the synthesis of 1-propyl-2-O-&beta;-D-galactopyranoside using 1-amino-2-propanol as acceptor was not achieved, and that N-glycoside formation was not observed, confirms the selectivity of &beta;-galactosidase for the synthesis of O-glycosides, and particularly for primary alcohols. The synthesized galactosides were evaluated for their ability to interact with bovine spleen galectin-1 (Gal-1) by using the hemagglutination inhibition assay; results demonstrated that 3-aminopropyl-1-O-&beta;-D-galactopyranoside may be considered as a functionalized galactose moiety more than an efficient Gal-1 inhibitor. The proposed approach constitutes a promising tool for the generation of glycopolymers and glyconanoparticles with potential applications in the development of biosensors as well as construction blocks in chemical synthesis.]]></dcterms:abstract>
    <dcterms:creator><![CDATA[<strong>Porci&uacute;ncula Gonz&aacute;lez, Cecilia</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<strong>Rodr&iacute;guez, Ernesto</strong>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=1502d6d114aace9e148166840e515f38" target="_blank"><strong>Soul&eacute;, Silvia</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=729d3d9bb07d7be0ba5e4dc762c01e29" target="_blank"><strong>Franco Fraguas, Laura</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=586cda0b970a37c5463af91ae8481fed" target="_blank"><strong>Brena, Beatriz M.</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=3c8a423235a59fcbc901eec52b2b7794" target="_blank"><strong>Giacomini, Cecilia</strong></a>]]></dcterms:creator>
    <dcterms:creator><![CDATA[<a title="Curriculum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=da4f071f890fec490234707830d5f695" target="_blank"><strong>Irazoqui, Gabriela</strong></a>]]></dcterms:creator>
    <dcterms:source><![CDATA[Biocatalysis and Biotransformation v. 33, no. 4, 2015. -- p. 197-207]]></dcterms:source>
    <dcterms:publisher><![CDATA[Taylor Francis]]></dcterms:publisher>
    <dcterms:date><![CDATA[2015]]></dcterms:date>
    <dcterms:rights><![CDATA[<p><strong>Informaci&oacute;n sobre Derechos de Autor</strong><br /> <br /> (Por favor lea este aviso antes de abrir los documentos u objetos)<br /> <br /> <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<br /> <br /> (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)<br /> <br /> <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: 10.3109/10242422.2015.1095678]]></dcterms:identifier>
</rdf:Description></rdf:RDF>
