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                <text>&lt;strong&gt;Residual infection of 15 Toxoplasma strains in the brain of rats fed cysts.&lt;/strong&gt;</text>
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                <text>Thirty-seven groups of 4&amp;ndash;32 Wistar rats were fed 2&amp;ndash;103 cysts of 15 Toxoplasma strains. After 2 months, the rats were euthanized and their brains screened for Toxoplasma cysts and bioassayed in mice if negative. The brains of 323 of 411 rats (78.6%) were found to be infected 2 months after inoculation with Toxoplasma cysts. Two hundred cysts were necessary to infect nearly 90% of the rats. With lower doses, only 60% of the rats had residual brain infection. Brain cysts were formed only in 146 of 411 rats (35.5%). The numbers of cysts formed were in the order of tens to hundreds, only occasionally one or two thousands. The mean percentage of rats with brain cysts, and the number of cysts formed in rat brains by different inocula, increased with higher doses of cysts and then declined. This pattern is difficult to explain and similar results regarding the number of cysts formed have been published. In relation to the mean percentage of rats infected, there appears to be a plateau in infection with the higher inocula. Neither the number of rats with cysts in their brains nor the numbers of cysts formed were dependent on the Toxoplasma strain used, with the exception of one strain. Instead, individual variations were marked, and are presumably related to variations in the individual genetic resistance to Toxoplasma infection in the rat. The information gathered is considered a preliminary step for a rat model of immunity against acquired toxoplasmosis.</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;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.</text>
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                <text>The larva of the cestode Echinococcus granulosus (hydatid cyst) is protected by the acellular laminated layer (LL). The mechanisms that make this thick coat a poor activator of host complement are incompletely understood. The structure binds, through unknown motifs, the host regulator of the alternative complement pathway (ACP), factor H. A second potential mechanism of ACP regulation, the inhibition of factor B activation, was detected in assays employing purified components (Immunopharmacology 42 : 91). The inhibitor was subsequently identified as myo-inositol hexakisphosphate (InsP(6)), which in the form of nano-deposits is a major component of the LL (Biochem J 362 : 297; J Cell Biochem 93 : 1272; FEBS J 273 : 3192). In this report we show that colloidal InsP(6 )solids inhibit factor B activation, through adsorption and associated impairment of C3b binding. However, this interaction is not relevant in the presence of serum proteins. In serum, InsP(6) deposits instead bind C1q, and initiate complement activation. This activation is curtailed through efficient C3b inactivation, previously shown to be entirely factor H-dependent, and now observed to be independent of the InsP(6) deposits. Therefore the complement resistance of the LL must be based on functional factor H binding sites present on the mucin-based meshwork that is its other major constituent.</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; 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)&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>&lt;strong&gt;Resistencia a fungicidas en Botrytis cinerea en el Uruguay&lt;/strong&gt;</text>
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                <text>&lt;p&gt;Botrytis cinerea provoca p&amp;eacute;rdidas importantes en numerosos cultivos y posee alta capacidad para hacerse resistente a fungicidas. Para conocer la situaci&amp;oacute;n en Uruguay se evalu&amp;oacute; la sensibilidad a fungicidas de 169 aislamientos provenientes de seis cultivos monosp&amp;oacute;ricos provenientes de ar&amp;aacute;ndano, tomate, frutilla, vi&amp;ntilde;a, rosal y eucalipto de diferentes zonas. Se determin&amp;oacute; la concentraci&amp;oacute;n inhibitoria m&amp;iacute;nima (CIM) de Carbendazim (Carbendazim, 50,0% i.a.), Iprodione (Rovral, 50,0% i.a., BAYER), Pyrimetanil (Mythos, 30,0% i.a., BAYER) y Pyraclostrobin + Boscalid (Bellis, 12,80% y 25,20% i.a., respectivamente, BASF). Se evalu&amp;oacute; crecimiento a las 48 horas en placas con agar papa dextrosa (gelatina&amp;ndash;glucosa para Pyrimetanil) con diferentes concentraciones de fungicida. Se encontraron poblaciones con diferente comportamiento. La resistencia a Carbendazim (CIM&amp;gt;128 mg/l) predomin&amp;oacute; en todos los cultivos muestreados, menos en ar&amp;aacute;ndano. Para Iprodione las CIM se distribuyeron por todos los valores desde 16 mg/l y para pirimetanil 30% presentaron CIM &amp;ge; 8 mg/l. La mayor&amp;iacute;a de los aislamientos presentaron CIM &amp;le; 4 mg/l de Boscalid + 1 mg/l de Pyraclostrobin, pero 7% presentaron CIM &amp;gt;32 mg/l + &amp;gt; 16 mg/l. El efecto hospedero fue altamente significativo sobre la sensibilidad a los fungicidas. Los aislamientos provenientes de ar&amp;aacute;ndano y eucalipto fueron los m&amp;aacute;s sensibles, salvo cuando los de eucalipto fueron testeados con Carbendazim. Los aislamientos de tomate y rosa fueron los m&amp;aacute;s resistentes, y los de frutilla intemedios.&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&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;&#13;
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                <text>&lt;strong&gt;Resoluci&amp;oacute;n de un problema real en el aula de qu&amp;iacute;mica anal&amp;iacute;tica&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Ortega, Andrea&lt;/strong&gt;</text>
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                <text>Anuario Latinoamericano de Educación Química  v. 20, no. 22, 2006-2007. -- p. 93-97</text>
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                <text>Universidad Nacional de San Luis</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 protege el derecho&lt;/strong&gt; 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; 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>ISSN 0328-087X.</text>
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                <text>The Asian citrus psyllid, Diaphorina citri, is currently the most important pest of citrus worldwide because it vectors &amp;lsquo;Candidatus Liberibacter&amp;rsquo; spp., the etiological agents of lethal Huanglongbing (HLB). Reduction of D. citri populations is a key component of HLB management. Identifying potential D. citri attractants, such as volatiles, could be useful for behavioral management of this insect. This could, for instance, enhance catches of adults on monitoring traps. The overall aim of this study was to investigate the response of D. citri to volatiles characteristic of preferred citrus hosts. An ancillary objective was to formulate a synthetic blend of volatiles based on preferred host odors that could enhance monitoring traps. Volatile collections of two preferred citrus species, Duncan grapefruit (Citrus paradise) and sweet orange (Citrus sinensis), were performed in aeration chambers and analyzed by gas chromatography-mass spectrometry. Based on the grapefruit volatile profile, a synthetic blend consisting in d-limonene (0.62 mg), methyl N-methylanthranilate (0.19 mg), &amp;beta;-ocimene (0.11 mg), &amp;beta;-elemene (0.02 mg), and &amp;beta;-caryophyllene (0.02 mg) was prepared in 9.9 mL of dichloromethane and evaluated for attractiveness, as well as the individual compounds, and compared with a positive control of natural volatiles collected from Citrus sinensis. Behavior of D. citri adults was evaluated in two-choice behavioral assays comparing response to lures with different combinations and dosages of the volatiles deployed on yellow sticky traps. Individually, neither d-limonene nor methyl N-methylanthranilate affected behavior of D. citri. However, these volatiles increased catches of D. citri, as compared with solvent control, when presented as components of the synthetic grapefruit blend, as did the natural citrus odor positive control. Importantly, catch of D. citri appeared to vary with the release rate of the identified grapefruit volatile blend, which was attractive at a 0.1 mg loading dosage, but repellent at a dosage only 1 log step higher.</text>
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                <text>&lt;strong&gt;Amor&amp;oacute;s, Mar&amp;iacute;a Eugenia&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Pereira das Neves, Virginia.&lt;/strong&gt;</text>
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                <text>&lt;p&gt;Alpeorujo is a semi-solid residue from the olive oil industry that accounts for around 80&amp;ndash;85% of the total processed olives; it contains phenolic compounds that could be used as natural preservatives in the food industry.&lt;br /&gt;The objective of this study was to optimize supercritical fluid extraction (SFE) of antioxidant compounds from alperujo using a Box-Behnken Design and response surface methodology. Antioxidant (ABTS and ORAC assays) and antimicrobial (MIC) potential of SFE extracts from Arbequina and Coratina were compared for extracts obtained in the optimal conditions to maximize the antioxidant activity (200 bar, 60 ◦C and 10% ethanol as modifier). Extracts from Coratina presented a significantly higher (p &amp;lt; 0.05) TPC (1487&amp;ndash;2073 mg GAE/kg) and tocopherol content (345&amp;ndash;454 ppm), although, in general, a correlation between these values and antioxidant activity of extracts was not observed. Moreover, Arbequina and Coratina SFE extracts showed moderate bacterial inhibitory potential against most of the bacteria studied.&lt;/p&gt;</text>
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                <text>Se evalu&amp;oacute; la respuesta de cerdos a soja desactivada artesanalmente en dietas isoenerg&amp;eacute;ticas e isoproteicas en base a ma&amp;iacute;z. Se utilizaron 28 machos castrados entre 40 y 105 kg de peso vivo asignados a cuatro tratamientos variando el suplemento proteico: T1: harina de soja, T2: poroto de soja cocido, T3: poroto de soja tostado, T4: poroto de soja crudo. Se evaluaron: consumo diario (CD) y total (CT) de alimento, ganancia diaria de peso (GP), &amp;iacute;ndice de conversi&amp;oacute;n (IC), rendimiento de carcasa (R), largo de res (L), espesor de grasa dorsal (GD), perfil lip&amp;iacute;dico de la grasa dorsal (PL). Los animales del T4 presentaron menor CD (P&amp;le;0,01) sin diferencias en el CT. La GP fue mayor (P&amp;le;0,01) para T1, sin diferencias entre T2 y T3 y menor para T4. T1 tuvo mejor IC que T4 (P&amp;le;0,01) y T2 y T3 (P&amp;le;0,05) mientras que T4 fue inferior (P&amp;le;0,01). No se observaron diferencias en R ni GD, mientras que L fue mayor (P&amp;le;0,01) para el T1. Se observaron diferencias en PL, con mayor contenido en PUFA y en los &amp;aacute;cidos oleico, linoleico y linol&amp;eacute;nico en los tratamientos incluyendo poroto de soja integral (P&amp;le;0,01). Se concluye que los tratamientos realizados al grano de soja mejoraron su valor nutricional con respecto al poroto crudo, aunque no se igualaron los resultados de la dieta testigo. Las carcasas provenientes de dietas con poroto de soja integral presentan menor valor industrial, pero mejor valor nutricional para consumo fresco que las basadas en harina de soja.</text>
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                <text>&lt;strong&gt;Bauz&amp;aacute;, Roberto&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Bratschi,Cecilia&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Ben&amp;iacute;tez, Valentina&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Hirigoyen Dominguez, Andr&amp;eacute;s Eduardo&lt;/strong&gt;</text>
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                <text>Agrociencia Uruguay v. 19, 2015. -- p. 81-92</text>
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                <text>&lt;p align="LEFT"&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 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>Ingl&amp;eacute;s</text>
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                <text>ISSN : 2301-1548</text>
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        <name>Alimentación</name>
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        <name>Soja</name>
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                <text>&lt;strong&gt;Respuesta farmacocin&amp;eacute;tica de los sistemas y terap&amp;eacute;utica&lt;/strong&gt;</text>
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                <text>&lt;a title="Curr&amp;iacute;culum Vitae" href="http://buscadores.anii.org.uy/buscador_sni/exportador/ExportarPdf?hash=caabbc98478c9c9fb71e4b0eb4e4ccd5" target="_blank"&gt;&lt;strong&gt;Fagiolino, Pietro&lt;/strong&gt;&lt;/a&gt;</text>
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              <elementText elementTextId="432970">
                <text>Revista Farmac&amp;eacute;utica v.149, no. 2, 2007. -- p. 16-27</text>
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            <elementTextContainer>
              <elementText elementTextId="432972">
                <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 protege&lt;/strong&gt; 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 (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 document o 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>Espa&amp;ntilde;ol</text>
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              <elementText elementTextId="432418">
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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;p&gt;In this study, we assessed the capacity of Pedobacter sp. 3.14.7 &amp;mdash;a novel Antarctic keratinolytic bacterium&amp;mdash; of producing a feather protein hydrolysate (FPH) with high antioxidant activity. This strain was able to degrade raw feather into protein hydrolysate under optimal conditions of 30 g l- 1 of feather concentration, pH 6.0, and 20 ◦C. Maximum enzymatic activity was detected after a 192-h cultivation period (125.67 &amp;plusmn; 3.06 U ml- 1). Quenching of the ABTS radical (2,20-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid) by the hydrolysate reached a value of approximately 95%, with a 50% Inhibitory Concentration (IC50) value of 0.57 &amp;plusmn; 0.01 g l- 1. An interesting reducing power of the FPH towards Fe+3 was also detected (2.19 Abs700 units in the presence of 2.03 g - 1 protein). The hydrolysate also displayed a moderate nitric oxide-scavenging activity, with an IC50 of 0.53 &amp;plusmn; 0.01 g l- 1. This FPH&amp;rsquo;s free amino acid content is high (almost 5 g l- 1). Results indicate that this hydrolysate may be useful as supplementary protein and antioxidant in animal feed formulations.&lt;/p&gt;</text>
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                <text>Biocatalysis and Agricultural Biotechnology,&amp;nbsp;v.32, 2021. -- e101925</text>
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                <text>This enzyme immobilization approach involves the formation of disulfide (&amp;minus;S&amp;ndash;S&amp;ndash;) bonds with the support. Thus, enzymes bearing exposed nonessential thiol (SH) groups can be immobilized onto thiol-reactive supports provided with reactive disulfides or disulfide oxides under mild conditions. The great potential advantage of this approach is the reversibility of the bonds formed between the activated solid phase and the thiol-enzyme, because the bound protein can be released with an excess of a low-molecular-weight thiol (e.g., dithiothreitol [DTT]). This is of particular interest when the enzyme degrades much faster than the adsorbent, which can be reloaded afterwards. The possibility of reusing the polymeric support after inactivation of the enzyme may be of interest for the practical use of immobilized enzymes in large-scale processes in industry, where their use has often been hampered by the high cost of the support material. Disulfide oxides (thiolsulfinate or thiolsulfonate groups) can be introduced onto a wide variety of support materials with different degrees of porosity and with different mechanical resistances. Procedures are given for the preparation of thiol-activated solid phases and the covalent attachment of thiol-enzymes to the support material via disulfide bonds. The possibility of reusing the polymeric support is also shown.</text>
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                <text>Methods in Molecular Biology v.1051, 2013. -- p. 89-116</text>
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                <text>The development of a solid-phase biocatalyst based on the reversible covalent immobilization of laccase onto thiol-reactive supports (thiolsulfinate-agarose [TSI-agarose]) was performed. To achieve this goal, laccase-producing strains isolated from Eucalyptus globulus were screened and white rot fungus Trametes villosa was selected as the best strain for enzyme production. Reduction of disulfide bonds and introduction of &amp;ldquo;de novo&amp;rdquo; thiol groups in partially purified laccase were assessed to perform its reversible covalent immobilization onto thiol-reactive supports (TSI-agarose). Only the thiolation process dramatically improved the immobilization yield, from 0% for the native and reduced enzyme to 60% for the thiolated enzyme. Mild conditions for the immobilization process (pH 7.5 and 4&amp;deg;C) allowed the achievement of nearly 100% of coupling efficiency when low loads were applied. The kinetic parameters, pH, and thermal stabilities for the immobilized biocatalyst were similar to those for the native enzyme. After the first use and three consecutives reuses, the insoluble derivative kept more than 80% of its initial capacity for decolorizing Remazol Brilliant Blue R, showing its suitability for color removal from textile industrial effluents. The possibility of reusing the support was demonstrated by the reversibility of enzyme-support binding.</text>
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