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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>This work explores theoretically the gas phase oxidation of allyl methyl sulfide (AMS, H2C&amp;ndash;&amp;ndash; CHCH2SCH3) initiated by &amp;bull;OH radicals, focusing on the H-abstraction pathway at the M06-2X-D3/aug-cc-pVTZ and MN15/ aug-cc-pVTZ levels of theory (m06Tz and mn15Tz). The formation of a prereactive complex (PRC) is involved in H-abstraction processes with two potential directions of approach for the OH radical, denoted as &amp;ldquo;&amp;alpha;&amp;rdquo; and &amp;ldquo;&amp;beta;&amp;rdquo;. The PRCs, demonstrate increased reactivity, primarily due to the interaction between the sulfur atoms and the hydroxyl hydrogen. A scheme for the H-abstraction mechanism that supports the experimentally identified products and predicts the formation of some S-containing low volatility products is proposed. The comparison of the potential energy surface (PES) between the double bond addition and H-abstraction paths in the AMS molecule shows that at the m06Tz level of theory, the H-abstraction on C3 and the addition to C1 have nearly the same profile of energy, while at the mn15Tz level, the minimum energy channel is the addition to C1. The theoretical rate coefficient for each reaction channel was calculated, considering the formation of a PRC prior to reaching the transition state of each channel and assuming thermal equilibrium between reactants and the PRC. The rate constants were calculated in a multi-TS/multi-conformer way at the SVECV-f12/m06Tz and SVECVf12/ mn15Tz levels of theory. The SVECV-f12 method is consistent in its predictions in both systems and exhibits only minor deviations from the experimental rate constants. Despite some specific differences due to the DFT method supporting the SVECV-f12 calculations, both methodologies predict a significant H-abstraction contribution in the AMS + OH gas phase reaction, which explains the high formation yield for acrolein determined experimentally.</text>
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&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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&lt;p class="western" lang="es-ES"&gt;(Por favor lea este aviso antes de abrir los documentos u objetos)&lt;/p&gt;&#13;
&lt;p class="western" lang="es-ES"&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 class="western" style="margin-bottom: 0cm;" lang="es-ES"&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;&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>URUGUAY&#13;
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                <text>BIBLIOGRAFIA NACIONAL QUIMICA&#13;
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                <text>2020&#13;
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                <text>ABSTRACT&lt;br /&gt;Background: Detoxification of inorganic arsenic (iAs) occurs when it methylates to form monomethylarsonic acid (MMA) and dimethylarsinic acid (DMA). Lower proportions of urinary iAs and MMA, and higher proportions of DMA indicate efficient methylation. The role of B-vitamins in iAs methylation in children with low-level arsenic exposure is understudied.&lt;br /&gt;Objectives: Our study objectivewas to assess the association between B-vitamin intake and iAsmethylation in children with low-level arsenic exposure (&amp;lt;50 &amp;mu;g/L in water; urinary arsenic 5&amp;ndash;50 &amp;mu;g/L).&lt;br /&gt;Methods: We conducted a cross-sectional study in 290 &amp;sim;7-y-old children in Montevideo. Intake of thiamin, riboflavin, niacin, vitamin B-6, and vitamin B-12 was calculated by averaging 2 nonconsecutive 24-h recalls. Total urinary arsenic&lt;br /&gt;concentration was measured as the sum of urinary iAs, MMA, and DMA, and adjusted for urinary specific gravity; iAs methylation was measured as urinary percentage As, percentage MMA, and percentage DMA. Arsenic concentrations&lt;br /&gt;from household water sources were assessed. Linear regressions tested the relationships between individual energyadjusted B-vitamins and iAs methylation.&lt;br /&gt;Results: Median (range) arsenic concentrations in urine and water were 9.9 (2.2&amp;ndash;48.7) and 0.45 (0.1&amp;ndash;18.9) &amp;mu;g/L, respectively. The median (range) of urinary percentage iAs, percentage MMA, and percentage DMA was 10.6% (0.0&amp;ndash;&lt;br /&gt;33.8), 9.7% (2.6&amp;ndash;24.8), and 79.1% (58.5&amp;ndash;95.4), respectively. The median (range) intake levels of thiamin, riboflavin, niacin, and vitamin B-6 were 0.81 (0.19&amp;ndash;2.56), 1.0 (0.30&amp;ndash;2.24), 8.6 (3.5&amp;ndash;23.3), and 0.67 (0.25&amp;ndash;1.73) mg/1000 kcal, respectively,&lt;br /&gt;whereas those of folate and vitamin B-12 were 216 (75&amp;ndash;466) and 1.7 (0.34&amp;ndash;8.3) &amp;mu;g/1000 kcal, respectively. Vitamin B-6 intake was inversely associated with urinary percentage MMA (&amp;beta; =&amp;minus;1.60; 95% CI: &amp;minus;3.07, &amp;minus;0.15). No other statistically&lt;br /&gt;significant associations were observed.&lt;br /&gt;Conclusions: Although vitamin B-6 intake was inversely associated with urinary percentage MMA, our findings suggest limited support for a relation between B-vitamin intake and iAs methylation in children exposed to low-level arsenic.&#13;
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                <text>&lt;p&gt;&lt;strong&gt;Desai, Gauri&lt;/strong&gt;&lt;/p&gt;</text>
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                <text>&lt;p&gt;&lt;strong&gt;Vahther, Marie&lt;/strong&gt;&lt;/p&gt;&#13;
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                <text>&lt;p&gt;&lt;strong&gt;Queirolo, Elena I.&lt;/strong&gt;&lt;/p&gt;&#13;
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                <text>&lt;p&gt;&lt;strong&gt;Peregalli, Fabiana&lt;/strong&gt;&lt;/p&gt;&#13;
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                <text>&lt;p&gt;&lt;strong&gt;Ma&amp;ntilde;ay, Nelly&lt;/strong&gt;&lt;/p&gt;&#13;
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                <text>&lt;p&gt;&lt;strong&gt;Millen, Amy E.&lt;/strong&gt;&lt;/p&gt;&#13;
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                <text>&lt;p&gt;&lt;strong&gt;Yu, &lt;/strong&gt;&lt;strong&gt;Jihnhee&lt;/strong&gt;&lt;/p&gt;&#13;
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                <text>&lt;p&gt;&lt;strong&gt;Browne, Richard W.&lt;/strong&gt;&lt;/p&gt;&#13;
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                <text>&lt;p&gt;&lt;strong&gt;Kordas, Katarzyna&lt;/strong&gt;&lt;/p&gt;&#13;
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                <text>Journal of Nutrition v. 150, no. 5, 2020. -- p. 1223-1229&#13;
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                <text>American Society for Nutrition&#13;
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                <text>&lt;p&gt;&lt;strong&gt;Informaci&amp;oacute;n sobre Derechos de Autor&lt;/strong&gt; (Por favor lea este aviso antes de abrir los documentos u objetos)&lt;strong&gt; La legislaci&amp;oacute;n uruguaya protege el derecho de autor &lt;/strong&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) ADVERTENCIA - 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>Azocasein, diffused into gels after polyacrylamide gel electrophoresis, provides a useful substrate for simple and rapid protease detection. After electrophoresis, the gels are incubated in an azocasein solution, immersed in trichloroacetic acid and then treated with NaOH. Proteolytic zones appear as uncolored bands on an orange background. The gels can be stored in trichloroacetic acid for months. This technique gives good results with serine proteases, acid proteases and metalloproteases. The method can be used under nondenaturing conditions and in the presence of sodium dodecyl sulfate. The sensitivity of this method is at the submicrogram protein level for trypsin.</text>
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&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;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 kinetic parameters of E.coli -galactosidase were not altered by the addition of 2-propanol or ethyl acetate (1.6% v/v). While ethylene glycol (1.6% v/v) doubled the values of both KM (0.29 mM) and kcat (1393 s&amp;ndash;), tetraethyleneglycol-dimethylether (Tetraglyme,1.6% v/v) preserved KM, but decreased kcat. At 50C all the cosolvents dramatically shortened the enzymatic half life, and so did Tetraglyme and 2-propanol at 28C. At 28C, both ethyl acetate and ethylene glycol stabilised the enzyme 9- and 6-fold respectively. This fact, together with the activation effect of ethylene glycol may lead to practical applications Activity and stability of Escherichia coli &amp;beta;-galactosidase in cosolvent systems.</text>
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&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>&lt;strong&gt; Antibody response of Echinococcus granulosus infected mice : Protoscolex specific response during infection is associated with decreasing specific IgG1/IgG3 ratio as well as decreasing avidity.&lt;/strong&gt;</text>
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                <text>ECHINOCOCCUS GRANULOSUS</text>
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                <text>The antibody response was followed during 68 weeks in 17 Balb/c mice intraperitoneally (i.p.) infected with Echinococcus granulosus protoscoleces (PSC) and in three mice i.p. immunized with dead PSC. Titres of antibodies recognizing peptidic and glucidic PSC epitopes, as well as their isotypic and avidity profiles were followed by ELISA. In addition, antigen recognition patterns were analysed by immunoblot. The response against carbohydrate epitopes was dominant in infected and immunized mice but stronger in the first group. Infected mice showed similar profiles of specific IgG and IgM with maximum titres from week 38 to 53. Although IgG1 and IgG3 were the predominant antibody subclasses, the ratio of IgG1/IgG3 antibody titres as well as antibody avidity decreased during the experiment, encompassing a decrease in recognition of peptidic epitopes. Immunized mice did not show significant levels of specific IgM and, after week 15, showed IgG titres lower than the infected mice. IgG1 was the predominant IgG subclass during all the experiment with background levels of IgG3. The mean Ab avidity was high and showed no significant changes during immunization. Different patterns of response were thus produced by dead and developing live parasites. Although high avidity IgG1 antibodies were early found in both cases, lower avidity IgG3 antibodies were increasingly produced afterwards only in infected animals. The isotype switch and avidity decrease observed only during infection are consistent with a possible parasitic mechanism to evade host immunity.</text>
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                <text>&lt;strong&gt;Severi, M&lt;/strong&gt;</text>
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                <text>&lt;strong&gt;Ferragut, G&lt;/strong&gt;</text>
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                <text>Parasite Immunology v. 19, , 1997. -- p. 545-552</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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            <name>Title</name>
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                <text>&lt;strong&gt; Aplicaci&amp;oacute;n de t&amp;eacute;cnicas estad&amp;iacute;sticas para la comprobaci&amp;oacute;n de la exactitud en el desarrollo de m&amp;eacute;todos anal&amp;iacute;ticos farmac&amp;eacute;uticos.&lt;/strong&gt;</text>
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                <text>Acta Farmac&amp;eacute;utica Bonaerense v. 13, no. 1, 1994. -- p. 49-52</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;</text>
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                <text>The use of oxidoreductases as biocatalysts for the production of a wide number of chiral building blocks is presently a mature (bio-)technology. In this context some industrial applications are currently performed by means of those enzymatic approaches, and new examples are expected to be realized. Moreover, oxidoreductases provide an interesting academic platform to undertake fundamental research in enzymology, to acquire a better understanding on catalytic mechanisms, and to facilitate the development of new biocatalytic applications. Within this area, a wide number of oxidoreductases from genus Candida spp. have been characterized and used as biocatalysts. These enzymes are rather diverse, and are able to carry out many useful reactions, like highly (enantio)selective keto-reductions, (de)racemizations and stereoinversions, and promiscuous catalytic imine reductions. In addition, some Candida spp. dehydrogenases are very useful for regenerating the cofactors, with the aid of sacrificial substrates. Addressing those features, the present paper aims to give an overview of these enzymes, by focusing on practical applications that these biocatalysts can provide. Furthermore, when possible, academic insights on the enzymatic performances will be discussed as well.</text>
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