<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>2304-0106</journal-id>
<journal-title><![CDATA[Anales de la Academia de Ciencias de Cuba]]></journal-title>
<abbrev-journal-title><![CDATA[Anales de la ACC]]></abbrev-journal-title>
<issn>2304-0106</issn>
<publisher>
<publisher-name><![CDATA[Academia de Ciencias de Cuba]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S2304-01062022000100012</article-id>
<title-group>
<article-title xml:lang="en"><![CDATA[Modeling and experimental validation of covalent immobilization of Trametes versicolor laccase in gold nanoparticles]]></article-title>
<article-title xml:lang="es"><![CDATA[Modelación y validación experimental de la inmovilización covalente de la lacasa de Trametes versicolor en nanopartículas de oro]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[González Abradelo]]></surname>
<given-names><![CDATA[Deborah]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Cutiño Ávila]]></surname>
<given-names><![CDATA[Bessy V.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[González Abradelo]]></surname>
<given-names><![CDATA[Darío]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Guisán Seijas]]></surname>
<given-names><![CDATA[José M.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[González-Bacerio]]></surname>
<given-names><![CDATA[Jorge]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
<xref ref-type="aff" rid="Aaf"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[del Monte-Martínez]]></surname>
<given-names><![CDATA[Alberto]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad de La Habana Facultad de Biología Centro de Estudio de Proteínas]]></institution>
<addr-line><![CDATA[ La Habana]]></addr-line>
<country>Cuba</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,Universidad de La Habana Facultad de Química Laboratorio de Bioinorgánica]]></institution>
<addr-line><![CDATA[ La Habana]]></addr-line>
<country>Cuba</country>
</aff>
<aff id="Af3">
<institution><![CDATA[,Instituto de Catálisis y Petroleoquímica Departamento de Biocatálisis ]]></institution>
<addr-line><![CDATA[ Madrid]]></addr-line>
<country>España</country>
</aff>
<aff id="Af4">
<institution><![CDATA[,Universidad de La Habana Facultad de Biología Departamento de Bioquímica]]></institution>
<addr-line><![CDATA[ La Habana]]></addr-line>
<country>Cuba</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>04</month>
<year>2022</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>04</month>
<year>2022</year>
</pub-date>
<volume>12</volume>
<numero>1</numero>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://scielo.sld.cu/scielo.php?script=sci_arttext&amp;pid=S2304-01062022000100012&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://scielo.sld.cu/scielo.php?script=sci_abstract&amp;pid=S2304-01062022000100012&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://scielo.sld.cu/scielo.php?script=sci_pdf&amp;pid=S2304-01062022000100012&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="en"><p><![CDATA[ABSTRACT  Introduction:  Protein immobilization is one of the most used technologies to increase the enzyme operational stability and improve their usage in biotechnological applications. Usually, the synthesis of immobilized derivatives is performed by the trial and error method. Our strategy for the rational design of immobilized derivatives (RDID) allows to select the optimal conditions for their synthesis. Gold nanoparticles (AuNPs), as non-porous solid supports, represent excellent systems for protein immobilization, with successful applications in nanomedicine, biocatalysis and electronics.  Methods:  The objective of this work was to validate the RDID strategy for covalent immobilization of the enzyme laccase from the basidiomycete white-rot fungus Trametes versicolor on AuNPs, activated with mercaptoundecanoic acid (AuNP-MUA) and MUA-ethylenediamine (AuNP-MUAen), for the potential use of the resultant biocatalysts in bioconversion processes.  Results:  As a result, the laccase-AuNP-MUA immobilized derivative is better than laccase-AuNP-MUAen in predicted immobilized derivative functional competence (42,8 % vs 26,1 %, respectively). In addition, all clusters predicted for laccase binding on AuNP-MUA resulted in immobilized enzymes with accessible active sites. In contrast, the half clusters predicted for interaction of laccase with AuNP-MUAen resulted in enzymes with poorly accessible active sites. Activity prediction was confirmed by an experimental expressed enzymatic activity of 45 % in laccase-AuNP-MUA system. Experimental maximal protein load matches the theoretical value (12,7 ( 0,7 ( 10-12 vs 12 ( 10-12 protein mg / activated AuNP mL). The results obtained in this research suggest the possibility of using this biocatalyst on a large scale.]]></p></abstract>
<abstract abstract-type="short" xml:lang="es"><p><![CDATA[RESUMEN  Introducción:  La inmovilización de proteínas es una de las tecnologías más utilizadas para incrementar la estabilidad operacional de las enzimas y potenciar su uso en aplicaciones biotecnológicas. Usualmente, la síntesis de derivados inmovilizados se realiza mediante el método de ensayo-error. Nuestra estrategia de diseño racional de derivados inmovilizados (DRDI) permite seleccionar las condiciones óptimas para su síntesis. Las nanopartículas de oro (AuNPs), como soportes sólidos no pororosos, representan sistemas excelentes para la inmovilización de proteínas, con aplicaciones exitosas en nanomedicina, biocatálisis y electrónica.  Métodos:  El objetivo de este trabajo fue validar la estrategia DRDI para la inmovilización covalente de la enzima lacasa del hongo basidiomiceto de la podredumbre blanca Trametes versicolor en AuNPs activadas con ácido mercaptoundecanóico (AuNP-MUA) y MUA-etiléndiamina (AuNP-MUAen), para el uso potencial de los biocatalizadores resultantes en procesos de bioconversión.  Resultados:  Como resultado, el derivado inmovilizado lacasa-AuNP-MUA es mejor que lacasa-AuNP-MUAen en la competencia funcional del derivado inmovilizado predicha (42,8 % vs. 26,1 %, respectivamente). Además, todas las agrupaciones de residuos superficiales predichas para la unión de la lacasa a AuNP-MUA resultaron en enzimas inmovilizadas con sitios activos accesibles. Por el contrario, la mitad de las agrupaciones predichas para la interacción de la lacasa con AuNP-MUAen resultaron en enzimas con sitios activos pobremente accesibles. La predicción de la actividad se confirmó por una actividad enzimática expresada experimental de 45 % en el sistema lacasa-AuNP-MUA. La carga proteica máxima experimental coincide con el valor teórico (12,7 ( 0,7 ( 10-12 vs 12 ( 10-12 mg de proteína / mL de AuNP activadas). Los resultados obtenidos en este trabajo sugieren la posibilidad de utilizar este biocatalizador a gran escala.]]></p></abstract>
<kwd-group>
<kwd lng="en"><![CDATA[covalent immobilization on gold nanoparticles through amide bonds]]></kwd>
<kwd lng="en"><![CDATA[immobilized derivative functional competence]]></kwd>
<kwd lng="en"><![CDATA[protein load for immobilization]]></kwd>
<kwd lng="en"><![CDATA[rational design of immobilized derivatives strategy]]></kwd>
<kwd lng="en"><![CDATA[Trametes versicolor laccase]]></kwd>
<kwd lng="es"><![CDATA[carga proteica para la inmovilización]]></kwd>
<kwd lng="es"><![CDATA[competencia funcional del derivado inmovilizado]]></kwd>
<kwd lng="es"><![CDATA[estrategia de diseño racional de derivados inmovilizados]]></kwd>
<kwd lng="es"><![CDATA[inmovilización covalente en nanopartículas de oro mediante enlaces amida]]></kwd>
<kwd lng="es"><![CDATA[lacasa de Trametes versicolor]]></kwd>
</kwd-group>
</article-meta>
</front><back>
<ref-list>
<ref id="B1">
<label>1</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[&#304;spirli Do&#287;aç]]></surname>
<given-names><![CDATA[Y]]></given-names>
</name>
<name>
<surname><![CDATA[Teke]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Immobilization of bovine catalase onto magnetic nanoparticles]]></article-title>
<source><![CDATA[Prep Biochem Biotech]]></source>
<year>2013</year>
<volume>43</volume>
<page-range>750-65</page-range></nlm-citation>
</ref>
<ref id="B2">
<label>2</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Pe&#269;ová]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[&#352;ebela]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Marková]]></surname>
<given-names><![CDATA[Z]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Thermostable trypsin conjugates immobilized to biogenic magnetite show a high operational stability and remarkable reusability for protein digestion]]></article-title>
<source><![CDATA[Nanotechnol]]></source>
<year>2013</year>
<volume>24</volume>
</nlm-citation>
</ref>
<ref id="B3">
<label>3</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Wu]]></surname>
<given-names><![CDATA[S-C]]></given-names>
</name>
<name>
<surname><![CDATA[Wang]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
<name>
<surname><![CDATA[Hansen]]></surname>
<given-names><![CDATA[D]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[A simple approach for preparation of affinity matrices: Simultaneous purification and reversible immobilization of a streptavidin mutein to agarose matrix]]></article-title>
<source><![CDATA[Sci Rep]]></source>
<year>2017</year>
<volume>7</volume>
</nlm-citation>
</ref>
<ref id="B4">
<label>4</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[de Melo Rêgo]]></surname>
<given-names><![CDATA[MJB]]></given-names>
</name>
<name>
<surname><![CDATA[Amorim de Lima]]></surname>
<given-names><![CDATA[LR]]></given-names>
</name>
<name>
<surname><![CDATA[Partes Longo]]></surname>
<given-names><![CDATA[AF]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[PVA-Glutaraldehyde as support for lectin immobilization and affinity chromatography]]></article-title>
<source><![CDATA[Acta Scient Biol Sci]]></source>
<year>2016</year>
<volume>38</volume>
<page-range>291-5</page-range></nlm-citation>
</ref>
<ref id="B5">
<label>5</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Homaei AA]]></surname>
<given-names><![CDATA[Sariri R]]></given-names>
</name>
<name>
<surname><![CDATA[Vianello]]></surname>
<given-names><![CDATA[F]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Enzyme immobilization: an update]]></article-title>
<source><![CDATA[J Chem Biol]]></source>
<year>2013</year>
<volume>6</volume>
<page-range>185-205</page-range></nlm-citation>
</ref>
<ref id="B6">
<label>6</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Basso]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Serban]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Industrial applications of immobilized enzymes(A review]]></article-title>
<source><![CDATA[Mol Catal]]></source>
<year>2019</year>
<volume>479</volume>
</nlm-citation>
</ref>
<ref id="B7">
<label>7</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Kim]]></surname>
<given-names><![CDATA[D]]></given-names>
</name>
<name>
<surname><![CDATA[Herr]]></surname>
<given-names><![CDATA[AE]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Protein immobilization techniques for microfluidic assays]]></article-title>
<source><![CDATA[Biomicrofluid]]></source>
<year>2013</year>
<volume>7</volume>
</nlm-citation>
</ref>
<ref id="B8">
<label>8</label><nlm-citation citation-type="book">
<person-group person-group-type="author">
<name>
<surname><![CDATA[del Monte-Martínez]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Cutiño-Avila]]></surname>
<given-names><![CDATA[BV]]></given-names>
</name>
<name>
<surname><![CDATA[González-Bacerio]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Rational design strategy as a novel immobilization methodology applied to lipases and phospholipases]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Sandoval]]></surname>
<given-names><![CDATA[G]]></given-names>
</name>
</person-group>
<source><![CDATA[Lipases and phospholipases: Methods and protocols. Methods in Molecular Biology]]></source>
<year>2018</year>
<page-range>243-83</page-range><publisher-name><![CDATA[Springer Science+Business Media, LLC]]></publisher-name>
</nlm-citation>
</ref>
<ref id="B9">
<label>9</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Mascarelli]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Toxic effects. Environmental concerns and more stringent laws are providing opportunities for environmental toxicologists]]></article-title>
<source><![CDATA[Nature]]></source>
<year>2012</year>
<volume>483</volume>
<page-range>363-5</page-range></nlm-citation>
</ref>
<ref id="B10">
<label>10</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Kowalczyk]]></surname>
<given-names><![CDATA[JE]]></given-names>
</name>
<name>
<surname><![CDATA[Peng]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Pawlowski]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The white-rot basidiomycete Dichomitus squalens shows highly specific transcriptional response to lignocellulose-related aromatic compounds]]></article-title>
<source><![CDATA[Front Bioeng Biotechnol]]></source>
<year>2019</year>
<volume>7</volume>
<page-range>229</page-range></nlm-citation>
</ref>
<ref id="B11">
<label>11</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Sahu]]></surname>
<given-names><![CDATA[N]]></given-names>
</name>
<name>
<surname><![CDATA[Merényi]]></surname>
<given-names><![CDATA[Z]]></given-names>
</name>
<name>
<surname><![CDATA[Bálint]]></surname>
<given-names><![CDATA[B]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Hallmarks of basidiomycete soft- and white-rot in wood-decay -omics data of two Armillaria species]]></article-title>
<source><![CDATA[Microorganisms]]></source>
<year>2021</year>
<volume>9</volume>
<page-range>149</page-range></nlm-citation>
</ref>
<ref id="B12">
<label>12</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Arregui]]></surname>
<given-names><![CDATA[L]]></given-names>
</name>
<name>
<surname><![CDATA[Ayala]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Gomez-Gil]]></surname>
<given-names><![CDATA[X]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Laccases: structure, function, and potential application in water bioremediation]]></article-title>
<source><![CDATA[Microb Cell Fact]]></source>
<year>2019</year>
<volume>18</volume>
<page-range>200</page-range></nlm-citation>
</ref>
<ref id="B13">
<label>13</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Janusz]]></surname>
<given-names><![CDATA[G]]></given-names>
</name>
<name>
<surname><![CDATA[Pawlik]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[&#346;widerska-Burek]]></surname>
<given-names><![CDATA[U]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Laccase properties, physiological functions, and evolution]]></article-title>
<source><![CDATA[Int J Mol Sci]]></source>
<year>2020</year>
<volume>21</volume>
<page-range>966</page-range></nlm-citation>
</ref>
<ref id="B14">
<label>14</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Sousa]]></surname>
<given-names><![CDATA[LM]]></given-names>
</name>
<name>
<surname><![CDATA[Vilarinho]]></surname>
<given-names><![CDATA[LM]]></given-names>
</name>
<name>
<surname><![CDATA[Ribeiro]]></surname>
<given-names><![CDATA[GH]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[An electronic device based on gold nanoparticles and tetraruthenated porphyrin as an electrochemical sensor for catechol]]></article-title>
<source><![CDATA[R Soc Open Sci]]></source>
<year>2017</year>
<volume>4</volume>
</nlm-citation>
</ref>
<ref id="B15">
<label>15</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Elahi]]></surname>
<given-names><![CDATA[N]]></given-names>
</name>
<name>
<surname><![CDATA[Kamali]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Baghersad]]></surname>
<given-names><![CDATA[MH]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Recent biomedical applications of gold nanoparticles: A review]]></article-title>
<source><![CDATA[Talanta]]></source>
<year>2018</year>
</nlm-citation>
</ref>
<ref id="B16">
<label>16</label><nlm-citation citation-type="book">
<person-group person-group-type="author">
<name>
<surname><![CDATA[DeLano]]></surname>
<given-names><![CDATA[WL]]></given-names>
</name>
</person-group>
<source><![CDATA[The PyMOL molecular graphics system]]></source>
<year>2002</year>
<publisher-loc><![CDATA[San Carlos ]]></publisher-loc>
<publisher-name><![CDATA[DeLano Scientific]]></publisher-name>
</nlm-citation>
</ref>
<ref id="B17">
<label>17</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[del Monte]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Cutiño]]></surname>
<given-names><![CDATA[B]]></given-names>
</name>
<name>
<surname><![CDATA[Gil]]></surname>
<given-names><![CDATA[D]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Rational design strategy on immobilized derivatives synthesis. Their implementation via RDID1.0 program]]></article-title>
<source><![CDATA[Serie Científica Universidad de las Ciencias Informáticas (Cuba)]]></source>
<year>2010</year>
<volume>3</volume>
<page-range>185-202</page-range></nlm-citation>
</ref>
<ref id="B18">
<label>18</label><nlm-citation citation-type="book">
<person-group person-group-type="author">
<name>
<surname><![CDATA[del Monte-Martínez]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Cutiño-Avila]]></surname>
<given-names><![CDATA[B]]></given-names>
</name>
<name>
<surname><![CDATA[González-Bacerio]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Modelado in silico de derivados inmovilizados]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Chávez]]></surname>
<given-names><![CDATA[MÁ]]></given-names>
</name>
<name>
<surname><![CDATA[Díaz]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
<name>
<surname><![CDATA[Arias]]></surname>
<given-names><![CDATA[O]]></given-names>
</name>
</person-group>
<source><![CDATA[Nano-micro-biotecnologías y sus aplicaciones]]></source>
<year>2019</year>
<page-range>155-80</page-range><publisher-loc><![CDATA[Habana ]]></publisher-loc>
<publisher-name><![CDATA[Editorial UH]]></publisher-name>
</nlm-citation>
</ref>
<ref id="B19">
<label>19</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Bradford]]></surname>
<given-names><![CDATA[MM]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding]]></article-title>
<source><![CDATA[Anal Biochem]]></source>
<year>1976</year>
<volume>72</volume>
<page-range>248-54</page-range></nlm-citation>
</ref>
<ref id="B20">
<label>20</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[del Monte-Martínez]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[González-Bacerio]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
<name>
<surname><![CDATA[Aragón-Abreu]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Selective and oriented immobilization of (phospho)lipases from the Caribbean Sea anemone Stichodactyla helianthus (Ellis, 1768) by interfacial adsorption]]></article-title>
<source><![CDATA[Rev CENIC Cienc Biol]]></source>
<year>2012</year>
<volume>43</volume>
<page-range>3-8</page-range></nlm-citation>
</ref>
<ref id="B21">
<label>21</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Zouari-Mechichi]]></surname>
<given-names><![CDATA[H]]></given-names>
</name>
<name>
<surname><![CDATA[Mechichi]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
<name>
<surname><![CDATA[Dhouib]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Laccase purification and characterization from Trametes trogii isolated in Tunisia: decolorization of textile dyes by the purified enzyme]]></article-title>
<source><![CDATA[Enz Microb Technol]]></source>
<year>2006</year>
<volume>39</volume>
<page-range>141-8</page-range></nlm-citation>
</ref>
<ref id="B22">
<label>22</label><nlm-citation citation-type="book">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Cutiño-Avila]]></surname>
<given-names><![CDATA[BV]]></given-names>
</name>
<name>
<surname><![CDATA[Sánchez-López]]></surname>
<given-names><![CDATA[MI]]></given-names>
</name>
<name>
<surname><![CDATA[Cárdenas-Moreno]]></surname>
<given-names><![CDATA[Y]]></given-names>
</name>
</person-group>
<source><![CDATA[Modeling and experimental validation of covalent immobilization of Trametes maxima laccase on glyoxyl and MANA-Sepharose CL 4B supports, for the use in bioconversion of residual colorants]]></source>
<year>2021</year>
<publisher-name><![CDATA[Biotechnol Appl Biochem]]></publisher-name>
</nlm-citation>
</ref>
<ref id="B23">
<label>23</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[del Monte-Martínez]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[González-Bacerio]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
<name>
<surname><![CDATA[Cutiño-Avila]]></surname>
<given-names><![CDATA[B]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Esters biotransformation by immobilized interfacial esterases from the Caribbean Sea anemone Stichodactyla helianthus]]></article-title>
<source><![CDATA[Biotecnología Aplicada]]></source>
<year>2015</year>
<volume>32</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>3201-10</page-range></nlm-citation>
</ref>
</ref-list>
</back>
</article>
