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                <text>&lt;strong&gt;Identification of universal diagnostic peptide candidates for neglected tropical diseases caused by cestodes through the integration of multi-genome-wide analyses and immunoinformatic predictions&lt;/strong&gt;</text>
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                <text>Neglected tropical diseases caused by helminth infections currently affect millions of people worldwide. Among them, there are three tapeworm species of outstanding importance: Echinococcus granulosus, E. multilocularis, and Taenia solium, which are responsible for cystic echinococcosis, alveolar echinococcosis, and cysticercosis, respectively. Despite several attempts, there is still a need for an effective and low-cost serological diagnostic test that can be used in endemic countries. In the present work, we described an innovative bioinformatic workflow for a rational prediction of putative peptide candidates for one-step serological diagnosis of any of these infections. First, we predicted the theoretical secretome shared by the three tapeworms starting from their full reported proteomes. Then, through immunoinformatics, we identified proteins within the shared secretome displaying high antigenicity scores and bearing T cell epitopes able to bind most human MHC-II alleles. Secondly, in such proteins, we identified linear B cell epitopes without post-translational modifications, and mapped them on 3D modelled structures to visualize their antibody accessibilities. As a result, we finally suggested two antigenic peptides shared between the secretomes of the three parasite species, which could be further tested for their immunodiagnostic potential.</text>
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                <text>Infection, Genetics and Evolution&amp;nbsp; v. 54, 2017. -- p. 338-346</text>
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
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                <text>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 &amp;minus;24.8 kcal/mol) exhibited the most promising interaction with NS2B-NS3 protease in comparison to crystallography ligand (Grid score &amp;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 &amp;plusmn; 7.3 &amp;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.</text>
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                <text>Chiral amines are essential precursors in the production of biologically active compounds, including several important drugs. Among the biocatalytic strategies that have been developed for their synthesis, the use of &amp;omega;-transaminases (&amp;omega;-TA) appears as an attractive alternative allowing the stereoselective amination of prochiral ketones. However, the problems associated with narrow substrate specificity, unfavourable reaction equilibrium and expensive amine donors still hamper its industrial application. The search for novel enzymes from nature can contribute to expand the catalytic repertoire of &amp;omega;-TA and help to circumvent some of these problems. A genome mining approach, based on the work described by H&amp;ouml;hne et al., was applied for selection of potential R-&amp;omega;-TA. Additional criteria were used to select an enzyme that differs from previously described ones. A candidate R-&amp;omega;-TA from Capronia semiimmersa was selected, cloned and expressed in Escherichia coli. Interestingly, alignment of this enzyme with previously reported TA sequences revealed the presence of two additional amino acid residues in a loop close to the active site. The impact of this change was analysed with a structural model based on crystallized R-&amp;omega;-TAs. Analysis of the substrate specificity of R-&amp;omega;-TA from C. semiimmersa indicates that it accepts a diversity of ketones as substrates yielding the corresponding amine with good yields and excellent enantioselectivity. The expressed enzyme accepts isopropylamine as amine donor what makes it suitable for industrial processes.</text>
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                <text>Applied Microbiology and Biotechnology v. 101, no. 14, 2017. -- p. 5677-5687</text>
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&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>Taking into account the impact of texture on consumers&amp;rsquo; liking of milk desserts, it is important for dairy companies to understand how consumers describe it. In this context, the aim of the present study was to identify consumers&amp;rsquo; texture vocabulary of milk desserts using free listing and a check-all-that-apply question. A free listing task was carried out with 66 consumers, who were asked to list all the positive and negative texture characteristics of milk desserts. Moreover, 65 consumers tried 8 commercial milk dessert samples and answer a check-all-that-apply question with 27 texture terms. Both methodologies enabled the identification of the texture characteristics more relevant for consumers and the texture vocabulary they usually use to describe this type of product. Creaminess and smoothness were the most relevant characteristics, followed by attributes related to thickness. Some similarities and differences were identified between the results of both methodologies.</text>
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                <text>Brazilian Journal of Food Technology 6&amp;ordm;SENSIBER, 19-21 agosto, 2010.-- p. 98-105</text>
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&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>&lt;strong&gt;Identifying ideal products using three different consumer profiling methodologies : Comparison with external preference mapping&lt;/strong&gt;</text>
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                <text>The aim of the present work was to identify consumers&amp;rsquo; ideal product by three consumer profiling techniques and to compare the agreement among the three techniques. Two studies were carried out in which consumers evaluated seven samples of orange-flavoured powdered drinks. In the first study 108 consumers scored their overall liking, whereas in the second one three groups of 50 consumers evaluated the sensory characteristics of the samples using projective mapping, a check-all-that-apply question or intensity scales. After completing the task consumers were asked to identify their ideal product. The different approaches yielded similar information regarding the sensory characteristics of the products and consumers&amp;rsquo; ideal product, providing similar recommendations for product improvement. However, they differed in the position of consumers&amp;rsquo; optimum product within the sensory space defined by the sensory characteristics of the evaluated samples. Projective mapping identified the consensus position of the ideal product within the range of sensory characteristics of the evaluated samples, providing similar results than external preference mapping. Differences and similarities between the methodologies are discussed, as well as potential applications.</text>
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;&#13;
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&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya&lt;/strong&gt; protege el derecho de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes&lt;/p&gt;&#13;
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>&lt;strong&gt;Identifying motives underlying wine purchase decisions :&amp;nbsp; Results from an exploratory free listing task with Burgundy wine consumers&lt;/strong&gt;</text>
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                <text>Logos on environmental sustainability could consist of an effective strategy to provide consumers with accurate, understandable and trustworthy information to encourage them to buy environmentally sustainable wines. However, the large number of different logos indicating environmental sustainability available in the market raises the question ofwhether their associated messages are successfully conveyed to consumers. In this context, the aim of the present exploratory study was to investigate how Burgundy wine consumers perceive a series of logos indicating environmental sustainability in wine production. Fourteen logos available in the French market were selected: three logos being specific to wine and eleven nonspecific. The logos were presented to 127 wine consumers from Dijon area (France), following an incomplete balanced block design. For each logo, participants had to answer the question: &amp;ldquo;What does a bottle of wine with this logo suggest to you?&amp;rdquo;. Responses were qualitatively analyzed and grouped into different categories. Chi-square tests and Correspondence analysiswere used to identify the relationship among logos and categories. Results showed large differences in how consumers perceived the logos. Biodyvin, the former European AB and the French AB organic logos were the logos that most successfully conveyed their messages, being strongly associated to organic wine. Most logos did not communicate a message related to environmental sustainability, which reaffirms the need to provide consumers with adequate information on environmental sustainability and to conduct further research on this subject.</text>
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&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
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&lt;p style="margin-bottom: 0cm;"&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>&lt;p style="margin-bottom: 0cm;"&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;br /&gt;&lt;br /&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;br /&gt;&lt;br /&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya&lt;/strong&gt; protege el derecho de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes&lt;br /&gt;&lt;br /&gt;(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)&lt;br /&gt;&lt;br /&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>YERBA MATE</text>
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                <text>&lt;p&gt;Ilex paraguariensis St. Hil., from the family of holy plants, Aquifoliaceae, is a native South American tree that can reach 18 m in height and is used to produce &amp;ldquo;yerba mate&amp;rdquo;. It is found primarily in the southern regions of South America, namely, Brazil (Mato Grosso do Sul, Minas Gerais, Parana, Rio Grande do Sul, Rio de Janeiro, Santa Catarina, Sao Paulo), Argentina (Corrientes, Misiones), Paraguay (Alto Paran&amp;aacute;, Amambay, Caaguaz&amp;uacute;, Canendiy&amp;uacute;, Central, Guaira, Itapu&amp;aacute;, Misiones,&lt;br /&gt;San Pedro), and Uruguay. &amp;ldquo;Yerba mate&amp;rdquo; tea, an infusion made from the leaves of this tree, is a widely consumed nonalcoholic beverage in South America which is gaining rapid introduction into the world market, either as tea itself or as ingredient&lt;br /&gt;in formulated foods or dietary supplements. The indigenous people have used it for centuries as a social and medicinal beverage. The container in which it is generally served is a gourd made from the dry and hollowed fruit of Lagenaria vulgaris Ser. (Cucurbitaceae), whose dimensions vary according the region and uses. It is called &amp;ldquo;mate&amp;rdquo; in the region. &amp;ldquo;Mate&amp;rdquo; has a very important social role. The act of offering and sharing it has connotations like those of the tea ceremony for some Oriental cultures.&lt;/p&gt;</text>
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                <text>Medicinal and Aromatic Plants of South America Vol. 2 : Argentina, Chile and Uruguay / &amp;Aacute;kos M&amp;aacute;th&amp;eacute; and Arnaldo Bandoni, ed. --&amp;nbsp;[s.l.] : Springer, 2021. --&amp;nbsp;p. 279-294</text>
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                <text>&lt;p dir="ltr"&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p dir="ltr"&gt;&lt;span&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/span&gt;&lt;/p&gt;&#13;
&lt;p dir="ltr"&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya protege el derecho&amp;nbsp;de autor&lt;/strong&gt;&lt;span&gt;&amp;nbsp;sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;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)&lt;/span&gt;&lt;/p&gt;&#13;
&lt;span id="docs-internal-guid-314533d8-7fff-2a15-1167-20ffe49bbf45"&gt;&lt;strong&gt;ADVERTENCIA:&lt;/strong&gt;&lt;span&gt;&amp;nbsp;La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/span&gt;&lt;/span&gt;</text>
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        <name>Aquifoliaceae</name>
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        <name>Mate</name>
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        <name>Tereré</name>
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        <name>Yerba mate</name>
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                <text>&lt;strong&gt;Imazalil concentration for in vitro monitoring of imazalil resistant isolates of Penicillium digitatum in citrus packinghouses&lt;/strong&gt;</text>
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                <text>ALMACENAMIENTO DE ALIMENTOS</text>
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                <text>The extensive use of imazalil (IMZ) in Uruguayan citrus packinghouses to control Penicillium spp. favored the selection and proliferation of resistant isolates. With the aim of detecting Penicillium digitatum biotypes that are not controlled by commercial doses of IMZ, the IMZ concentration within amended potato dextrose agar (PDA) plates was adjusted to 1.0mgL&amp;minus;1 IMZ. This concentration allowed the detection of resistant isolates that were not controlled by commercial applications of 3.0 g L&amp;minus;1 IMZ. These isolates were able to grow in fruit with IMZ residues of 0.92 and 3.08mgkg&amp;minus;1. Therefore, environmental monitoring of facilities where commercial dip applications containing 3.0 g L&amp;minus;1 IMZ are employed, should be done with 1.0mgL&amp;minus;1 of IMZ in Petri dishes. We can conclude that use of IMZ in postharvest applications of 3.0 g L&amp;minus;1 remains effective to control wild Uruguayan P. digitatum isolates but not for resistant ones. A survey of 26 P. digitatum isolates collected in Uruguay indicated IMZ resistant isolates occurred in packinghouses and not in citrus groves.</text>
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                <text>&lt;strong&gt;P&amp;eacute;rez, E.&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Blanco, O.&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Berreta, C.&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Lado, Joanna&lt;/strong&gt;</text>
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                <text>Postharvest Biology and Technology v. 60, no. 3, 2011. -- p. 258-262</text>
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                <text>Elsevier</text>
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                <text>Postharvest Biology and Technology&amp;nbsp; v. 60, no. 3, 2011. -- p. 258-262</text>
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                <text>doi:10.1016/j.postharvbio.2011.01.002</text>
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        <name>Almacenamiento de alimentos</name>
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>Imidazolidine derivatives were studied as anti-Trypanosoma cruzi agents. Imidazolines can be considered as ethylenediamine/ carbonyl precursors and therefore interfere with the biosynthesis of polyamines into the parasite. Some of the derivatives were found to have high and selective activity against the proliferative stages of the parasite, with IC50 values against the epimastigote form in the low micromolar range as the reference drug Nifurtimox. The imidazolidines demonstrated to be stable after five days of incubation in buffer glucose, pH 7, indicating that diamines were not obtained in these conditions. But it was found that two of the studied diamine precursors were as active as the parent compounds. Probably, the imidazolidines affect the mitochondrial integrity according to the excreted end-products found in the NMR studies. The QSAR studies indicated that the bioactivities are correlated with the lipophilicities. In conclusion, we have described a new and relevant bioactivity for imidazolidines. The results support further in vivo studies of some of these imidazolidine derivatives.</text>
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&lt;p&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;&#13;
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                <text>&lt;strong&gt;Imidazolium compounds are active against all stages of Trypanosoma cruzi&lt;/strong&gt;</text>
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                <text>Imidazolium salts are best known for their applications in organic synthesis as room-temperature ionicliquids, or as precursors of stable carbenes, but they also show important biological properties suchas anti-oxidative effects, induction of mitochondrial membrane permeabilisation and inhibition of theinfection cycle of Plasmodium falciparum. For these reasons, and since chemotherapy for Chagas diseaseis inefficient, the aim of this study was to test the use of imidazolium compounds against the kineto-plastid haemoflagellate aetiological agent for this disease, namely Trypanosoma cruzi. The results showthat five of the tested compounds are more effective than the reference drug benznidazole against theepimastigote and trypomastigote forms of T. cruzi. Moreover, intracellular amastigotes were also affectedby the compounds, which showed lower toxicity in host cells. Transmission electron microscopy anal-ysis demonstrated that the tested agents induced alterations of the kinetoplast and particularly of themitochondria, leading to extraordinary swelling of the organelle. These results further demonstrate thatthe test agents with the best profile are those bearing symmetrical bulky substituents at N1and N3, dis-playing promising activity against all forms of T. cruzi, interesting selectivity indexes and exceptionalactivity at low doses. Accordingly, these agents represent promising candidates for the treatment ofChagas disease.</text>
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                <text>Objective: To assess the effects of nutritional warnings during the first month after the date of full compliance by the food industry in Uruguay in terms of citizen awareness, self-reported use and ability to understand nutritional information. Design: The present work encompassed two online studies, conducted before (Study 1) and during the first month after the date of full compliance by the food industry (Study 2). An after-only design was used to assess awareness of the policy, exposure to nutritional warnings on food packages and self-reported use of warnings for making purchase decisions in Study 2. An after-only with control group experimental design was used to assess the effect of nutritional warnings on understanding of nutrition information in Studies 1 and 2. Setting: Uruguay, one of the Latin American countries, that has recently implemented nutritional warnings. Participants: A non-probabilistic sample of 1772 participants was recruited using Facebook advertisements targeted at Uruguayan adult users. Results: High awareness and self-reported use of nutritional warnings during the first month after the date of full compliance in Uruguay were observed. In addition, the before and after comparison showed that the implementation of warnings increased citizens&amp;rsquo; ability to use nutritional information to compare products and to identify products with excessive content of sugar, fat, saturated fat and sodium. Conclusions: The current study confirms results from experimental studies and provides additional evidence to support the implementation of nutritional warnings as one of the public policies that can contribute to tackle obesity and non-communicable diseases.&#13;
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                <text>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 &amp;beta;-galactosidase and Canavalia ensiformis &amp;alpha;-mannosidase onto agarose and silica magnetic nanoparticles activated with cyanate ester groups. High immobilization yields (70&amp;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&amp;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 &amp;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.</text>
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                <text>&lt;p&gt;The enzyme B-galactosidase from Bacillus circulans was immobilized onto the epoxy-activated acrylic supports Sepabeads EC-EP and Sepabeads EC-HFA. The influence of immobilization conditions on the process yield was studied. Optimal conditions for Sepabeads EC-EP were 1.4 M potassium phosphate buffer pH 8.5, enzyme loads in the range 3&amp;ndash;30 mg/g of gel, and an incubation period of 48 h, achieving protein immobilization yields of 98&amp;ndash;100% with activity yields of 85&amp;ndash;98%. For Sepabeads HFA, low ionic strength (0.02 M potassium phosphate buffer), enzyme loads in the range 1.5&amp;ndash;15 mg/g of gel, and shorter&lt;br /&gt;incubation periods (24 h) were required; however, when the whole process was performed at pH 8.5,&lt;br /&gt;maximum yields achieved were below 60%. This process was improved by performing a fast adsorption at pH 7.5 and then raising the pH to 8.5 to favor covalent coupling, achieving protein immobilization yields of 100% and enzyme activity yields of 83%.&lt;br /&gt;The remarkable thermal stability of derivatives obtained at low enzyme loads, and the fact that the thermal stability of medium load enzyme derivatives improved when a post-immobilization alkaline treatment was performed, support the hypothesis that stabilization was achieved through multipoint covalent attachment.&lt;/p&gt;</text>
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                <text>Journal of Insect Physiology v. 58, no. 1, 2012. -- p. 110-115</text>
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&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya&lt;/strong&gt; protege el derecho de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes&lt;/p&gt;&#13;
&lt;p&gt;(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)&lt;/p&gt;&#13;
&lt;p style="margin-bottom: 0cm;"&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>&lt;strong&gt;Immobilization of B-galactosidase from Kluyveromyces lactis on silica and agarose : comparison of different methods.&lt;/strong&gt;</text>
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                <text>The covalent immobilization of &amp;beta;-galactosidase from Kluyveromyces lactis (&amp;beta;-gal) on to two different porous carriers, CPC-silica and agarose, is reported. CPC-silica was silanizated and activated with glutaraldehyde. The activation of agarose via a cyanylating agent (CDAP) was optimized. Gel-bound protein and gel-bound activity were both measured directly, allowing the determination of apparent specific activities (S.A.). Higher amounts of &amp;beta;-gal were immobilized on the activated CPC-silica (maximum capacity, 23 mg ml&amp;minus;1 of packed support) than on the CDAP-activated agarose. For the lower enzyme loading assayed (12.6 mg ml&amp;minus;1 packed support), 100% of the enzyme was immobilized but only 34% of its activity was expressed. This inactivation during immobilization was confirmed by the S.A. values (22&amp;ndash;29 EU mg&amp;minus;1 for the CPC-derivatives and 80 EU mg&amp;minus;1 for soluble &amp;beta;-gal). The Kapp (3.4 mM) for the CDAP-derivative with ONPG as substrate was higher than the KM value for soluble &amp;beta;-gal (2 mM). When the enzyme loading was increased five-fold, the Kapp increased four-fold, to 13 mM. The Vapp values for the CPC-derivatives were remarkably lower than the Vmax for soluble &amp;beta;-galactosidase. CDAP-derivatives showed better thermal stabilities than CPC-derivatives but neither of them enhanced the stability of the soluble enzyme. When stored at 4&amp;deg;C, the activity of both derivatives remained stable for at least 2 months. Both derivatives displayed high percentages of lactose conversion (90%) in packed bed mini-reactors. Glucose production was 3.3-fold higher for the CPC-derivative than for the CDAP-derivative, as a consequence of the higher flow rates achieved.</text>
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                <text>Journal of Molecular Catalysis B:Enzymatic v. 4, 1998. -- p. 313-327</text>
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya&lt;/strong&gt; protege el derecho de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes&lt;/p&gt;&#13;
&lt;p&gt;(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)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA&lt;/strong&gt; - La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>The term immobilized enzymes refers to "enzymes physically confined or localized in a certain defined region of space with retention of their catalytic activities, and which can be used repeatedly and continuously." Immobilized enzymes are currently the subject of considerable interest because of their advantages over soluble enzymes. In addition to their use in industrial processes, the immobilization techniques are the basis for making a number of biotechnology products with application in diagnostics, bioaffinity chromatography, and biosensors. At the beginning, only immobilized single enzymes were used, after 1970s more complex systems including two-enzyme reactions with cofactor regeneration and living cells were developed. The enzymes can be attached to the support by interactions ranging from reversible physical adsorption and ionic linkages to stable covalent bonds. Although the choice of the most appropriate immobilization technique depends on the nature of the enzyme and the carrier, in the last years the immobilization technology has increasingly become a matter of rational design. As a consequence of enzyme immobilization, some properties such as catalytic activity or thermal stability become altered. These effects have been demonstrated and exploited. The concept of stabilization has been an important driving force for immobilizing enzymes. Moreover, true stabilization at the molecular level has been demonstrated, e.g., proteins immobilized through multipoint covalent binding</text>
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&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;br /&gt; &lt;br /&gt; (Por favor lea este aviso antes de abrir los documentos u objetos)&lt;br /&gt; &lt;br /&gt; &lt;strong&gt;La legislaci&amp;oacute;n uruguaya&lt;/strong&gt; protege el derecho de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;uacute;n y las siguientes leyes&lt;br /&gt; &lt;br /&gt; (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)&lt;br /&gt; &lt;br /&gt; &lt;strong&gt;ADVERTENCIA -&lt;/strong&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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&lt;p&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya protege el derecho&lt;/strong&gt;&amp;nbsp;de autor sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;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)&lt;/p&gt;&#13;
&lt;p&gt;&lt;strong&gt;ADVERTENCIA -&lt;/strong&gt;&amp;nbsp;La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/p&gt;</text>
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                <text>&lt;p style="text-align: left;"&gt;The elucidation of glycans biological function is essential to&lt;br /&gt;understand their role in biological processes, both normal and&lt;br /&gt;pathological. Immobilized glycoenzymes are excellent tools for this purpose as they can selectively release glycans from glycoproteins without altering their backbone. They can be easily removed from the reaction mixture avoiding their&lt;br /&gt;interference in subsequent experiments. Here, we describe the&lt;br /&gt;immobilization of peptide-N-glycosidase F (PNGase F) onto&lt;br /&gt;silica magnetic nanoparticles with immobilization yields of&lt;br /&gt;86% and activity yields of 12%. Immobilized PNGase F showed&lt;br /&gt;higher thermal stability than its soluble counterpart, and could&lt;br /&gt;be reused for at least seven deglycosylation cycles. It was&lt;br /&gt;efficient in the deglycosylation of several glycoproteins (ribonuclease B, bovine fetuin, and ovalbumin) and a protein lysate from the parasite Fasciola hepatica under nativeconditions, with similar performance to that of the solubleenzyme. Successful deglycosylation was evidenced by adecrease in specific lectin recognition of the glycoproteins (40%&amp;ndash;80%). Moreover, deglycosylated F. hepatica lysate allowed us to confirm the role of parasite N-glycans in the inhibition of the lipopolysaccharide-induced maturation of dendritic cells. Immobilized PNGase F probed to be a robust biotechnological tool for deglycosylation of glycoproteins and complex biological samples under native conditions.&lt;/p&gt;</text>
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                <text>&lt;p dir="ltr"&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p dir="ltr"&gt;&lt;span&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/span&gt;&lt;/p&gt;&#13;
&lt;p dir="ltr"&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya protege el derecho&amp;nbsp;de autor&lt;/strong&gt;&lt;span&gt; sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;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)&lt;/span&gt;&lt;/p&gt;&#13;
&lt;span id="docs-internal-guid-314533d8-7fff-2a15-1167-20ffe49bbf45"&gt;&lt;strong&gt;ADVERTENCIA:&lt;/strong&gt;&lt;span&gt; La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/span&gt;&lt;/span&gt;</text>
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&lt;div class="epub-section"&gt;&lt;a class="epub-doi" href="https://doi.org/10.1002/bab.2099"&gt;https://doi.org/10.1002/bab.2099&lt;/a&gt;&lt;/div&gt;</text>
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                <text>&lt;strong&gt;Immobilized peptide-N-glycosidase F onto magnetic nanoparticles: a biotechnological tool for protein&lt;/strong&gt;</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="49">
            <name>Subject</name>
            <description>The topic of the resource</description>
            <elementTextContainer>
              <elementText elementTextId="634492">
                <text>GLICANOS</text>
              </elementText>
              <elementText elementTextId="634493">
                <text>DESGLICOSILACION</text>
              </elementText>
              <elementText elementTextId="634494">
                <text>ANALISIS GLICOMICO</text>
              </elementText>
              <elementText elementTextId="634495">
                <text>INMOVILIZACION ENZIMATICA</text>
              </elementText>
              <elementText elementTextId="634496">
                <text>NANOPARTICULAS</text>
              </elementText>
              <elementText elementTextId="634497">
                <text>PEPTIDOS</text>
              </elementText>
              <elementText elementTextId="634498">
                <text>GLUCOSIDASA</text>
              </elementText>
              <elementText elementTextId="634499">
                <text>BIBLIOGRAFIA NACIONAL QUIMICA</text>
              </elementText>
              <elementText elementTextId="634500">
                <text>2022</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="87">
            <name>Abstract</name>
            <description>A summary of the resource.</description>
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              <elementText elementTextId="634501">
                <text>&lt;p&gt;The elucidation of glycans biological function is essential to&lt;br /&gt;understand their role in biological processes, both normal and&lt;br /&gt;pathological. Immobilized glycoenzymes are excellent tools&lt;br /&gt;for this purpose as they can selectively release glycans from&lt;br /&gt;glycoproteins without altering their backbone. They can be&lt;br /&gt;easily removed from the reaction mixture avoiding their&lt;br /&gt;interference in subsequent experiments. Here, we describe the&lt;br /&gt;immobilization of peptide-N-glycosidase F (PNGase F) onto&lt;br /&gt;silica magnetic nanoparticles with immobilization yields of&lt;br /&gt;86% and activity yields of 12%. Immobilized PNGase F showed&lt;br /&gt;higher thermal stability than its soluble counterpart, and could&lt;br /&gt;be reused for at least seven deglycosylation cycles. It was&lt;br /&gt;efficient in the deglycosylation of several glycoproteins&lt;br /&gt;(ribonuclease B, bovine fetuin, and ovalbumin) and a protein&lt;br /&gt;lysate from the parasite Fasciola hepatica under native&lt;br /&gt;conditions, with similar performance to that of the soluble&lt;br /&gt;enzyme. Successful deglycosylation was evidenced by a&lt;br /&gt;decrease in specific lectin recognition of the glycoproteins&lt;br /&gt;(40%&amp;ndash;80%). Moreover, deglycosylated F. hepatica lysate&lt;br /&gt;allowed us to confirm the role of parasite N-glycans in the&lt;br /&gt;inhibition of the lipopolysaccharide-induced maturation of&lt;br /&gt;dendritic cells. Immobilized PNGase F probed to be a robust&lt;br /&gt;biotechnological tool for deglycosylation of glycoproteins and&lt;br /&gt;complex biological samples under native conditions.&lt;/p&gt;</text>
              </elementText>
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          </element>
          <element elementId="39">
            <name>Creator</name>
            <description>An entity primarily responsible for making the resource</description>
            <elementTextContainer>
              <elementText elementTextId="634502">
                <text>&lt;strong&gt;Bidondo, Luc&amp;iacute;a&lt;/strong&gt;</text>
              </elementText>
              <elementText elementTextId="634503">
                <text>&lt;strong&gt;Festari, Florencia&lt;/strong&gt;</text>
              </elementText>
              <elementText elementTextId="634504">
                <text>&lt;strong&gt;Freire, Teresa&lt;/strong&gt;</text>
              </elementText>
              <elementText elementTextId="634505">
                <text>&lt;a href="https://exportcvuy.anii.org.uy/cv/?8c80c1ae8b95cb6b8bc4b6ce3a8d3a39b297d1bd27a3804c09be97adcbe35a3741bd28180c0446feac51238afbedb3cf67010e8ed6fa462a13806c083463ea87" target="_blank"&gt;&lt;strong&gt;Giacomini, Cecilia&lt;/strong&gt;&lt;/a&gt;</text>
              </elementText>
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          </element>
          <element elementId="48">
            <name>Source</name>
            <description>A related resource from which the described resource is derived</description>
            <elementTextContainer>
              <elementText elementTextId="634506">
                <text>Biotechnology and Applied Biochemistry, v. 69, n&amp;deg; 1, 2022. -- pp. 209-220.</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="45">
            <name>Publisher</name>
            <description>An entity responsible for making the resource available</description>
            <elementTextContainer>
              <elementText elementTextId="634507">
                <text>Wiley</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="40">
            <name>Date</name>
            <description>A point or period of time associated with an event in the lifecycle of the resource</description>
            <elementTextContainer>
              <elementText elementTextId="634508">
                <text>2022</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="47">
            <name>Rights</name>
            <description>Information about rights held in and over the resource</description>
            <elementTextContainer>
              <elementText elementTextId="634509">
                <text>&lt;p dir="ltr"&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt;&lt;/p&gt;&#13;
&lt;p dir="ltr"&gt;&lt;span&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/span&gt;&lt;/p&gt;&#13;
&lt;p dir="ltr"&gt;&lt;strong&gt;La legislaci&amp;oacute;n uruguaya protege el derechode autor&lt;/strong&gt;&lt;span&gt;&amp;nbsp;sobre toda creaci&amp;oacute;n literaria, cient&amp;iacute;fica o art&amp;iacute;stica, tanto en lo que tiene que ver con sus derechos morales, como en lo referente a los derechos patrimoniales con sujeci&amp;oacute;n a lo establecido por el derecho com&amp;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)&lt;/span&gt;&lt;/p&gt;&#13;
&lt;span id="docs-internal-guid-9d2103f7-7fff-c813-00c7-2528fd4891ff"&gt;&lt;strong&gt;ADVERTENCIA:&lt;/strong&gt;&lt;span&gt;&amp;nbsp;La consulta de este documento queda condicionada a la aceptaci&amp;oacute;n de las siguientes condiciones de uso: Este documento es &amp;uacute;nicamente para usos privados enmarcados en actividades de investigaci&amp;oacute;n y docencia. No se autoriza su reproducci&amp;oacute;n con fines de lucro. Esta reserva de derechos afecta tanto los datos del documento como a sus contenidos. En la utilizaci&amp;oacute;n o cita de partes debe indicarse el nombre de la persona autora.&lt;/span&gt;&lt;/span&gt;</text>
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          <element elementId="42">
            <name>Format</name>
            <description>The file format, physical medium, or dimensions of the resource</description>
            <elementTextContainer>
              <elementText elementTextId="634510">
                <text>PDF</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="44">
            <name>Language</name>
            <description>A language of the resource</description>
            <elementTextContainer>
              <elementText elementTextId="634511">
                <text>Ingl&amp;eacute;s</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="51">
            <name>Type</name>
            <description>The nature or genre of the resource</description>
            <elementTextContainer>
              <elementText elementTextId="634512">
                <text>Art&amp;iacute;culo</text>
              </elementText>
            </elementTextContainer>
          </element>
          <element elementId="43">
            <name>Identifier</name>
            <description>An unambiguous reference to the resource within a given context</description>
            <elementTextContainer>
              <elementText elementTextId="634513">
                <text>10.1002/bab.2099</text>
              </elementText>
            </elementTextContainer>
          </element>
        </elementContainer>
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    </elementSetContainer>
    <tagContainer>
      <tag tagId="5850">
        <name>Analisis Glicómico</name>
      </tag>
      <tag tagId="7287">
        <name>Desglicosilación</name>
      </tag>
      <tag tagId="7135">
        <name>Glicanos</name>
      </tag>
      <tag tagId="5864">
        <name>Glucosidasa</name>
      </tag>
      <tag tagId="7133">
        <name>Inmovilización enzimática</name>
      </tag>
      <tag tagId="2853">
        <name>Nanopartículas</name>
      </tag>
      <tag tagId="329">
        <name>Péptidos</name>
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  </item>
</itemContainer>
