<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-04-17T08:07:34Z</responseDate><request verb="GetRecord" identifier="oai:www.recercat.cat:2445/172223" metadataPrefix="marc">https://recercat.cat/oai/request</request><GetRecord><record><header><identifier>oai:recercat.cat:2445/172223</identifier><datestamp>2026-01-31T10:58:18Z</datestamp><setSpec>com_2072_1057</setSpec><setSpec>col_2072_478916</setSpec><setSpec>col_2072_478917</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
   <leader>00925njm 22002777a 4500</leader>
   <datafield ind2=" " ind1=" " tag="042">
      <subfield code="a">dc</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Bello Gil, Daniel</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Roig Molina, Emma</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Fonseca, Jennifer</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Sarmiento Ferrández, Mar ıa Dolores</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Ferrándiz, Marcela</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Franco, Esther</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Mira, Elena</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Maestro, Beatriz</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="720">
      <subfield code="a">Sanz, Jesús M.</subfield>
      <subfield code="e">author</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="260">
      <subfield code="c">2020-11-20T11:28:33Z</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="260">
      <subfield code="c">2020-11-20T11:28:33Z</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="260">
      <subfield code="c">2018-09-01</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="260">
      <subfield code="c">2020-11-11T17:42:01Z</subfield>
   </datafield>
   <datafield ind2=" " ind1=" " tag="520">
      <subfield code="a">The presence of synthetic dyes in wastewaters generated by the textile industry constitutes a serious environmental and health problem that urges the scientific community on an appropriate action. As a proof-of-concept, we have developed a novel approach to design enzymatic bioreactors with the ability to decolorize dye solutions through the immobilization of the bacterial CueO laccase-like multicopper oxidase from Escherichia coli on polyhydroxybutyrate (PHB) beads by making use of the BioF affinity tag. The decolorization efficiency of the system was characterized by a series of parameters, namely maximum enzyme adsorption capacity, pH profile, kinetic constants, substrate range, temperature and bioreactor recycling. Depending on the tested dye, immobilization increased the catalytic activity of CueO by up to 40-fold with respect to the soluble enzyme, reaching decolorization efficiencies of 45-90%. Our results indicate that oxidase bioreactors based on polyhydroxyalkanoates are a promising alternative for the treatment of coloured industrial wastewaters.</subfield>
   </datafield>
   <datafield tag="653" ind2=" " ind1=" ">
      <subfield code="a">Aigües residuals</subfield>
   </datafield>
   <datafield tag="653" ind2=" " ind1=" ">
      <subfield code="a">Indústria tèxtil</subfield>
   </datafield>
   <datafield tag="653" ind2=" " ind1=" ">
      <subfield code="a">Escheríchia coli</subfield>
   </datafield>
   <datafield tag="653" ind2=" " ind1=" ">
      <subfield code="a">Sewage</subfield>
   </datafield>
   <datafield tag="653" ind2=" " ind1=" ">
      <subfield code="a">Textile industry</subfield>
   </datafield>
   <datafield tag="653" ind2=" " ind1=" ">
      <subfield code="a">Escherichia coli</subfield>
   </datafield>
   <datafield ind2="0" ind1="0" tag="245">
      <subfield code="a">An enzymatic system for decolorization of wastewater dyes using immobilized CueO laccase-like multicopper oxidase on poly-3-hydroxybutyrate</subfield>
   </datafield>
</record></metadata></record></GetRecord></OAI-PMH>