<?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>2026-04-17T14:00:21Z</responseDate><request verb="GetRecord" identifier="oai:www.recercat.cat:20.500.12327/206" metadataPrefix="qdc">https://recercat.cat/oai/request</request><GetRecord><record><header><identifier>oai:recercat.cat:20.500.12327/206</identifier><datestamp>2025-10-22T11:14:37Z</datestamp><setSpec>com_2072_4428</setSpec><setSpec>com_2072_4427</setSpec><setSpec>col_2072_487898</setSpec></header><metadata><qdc:qualifieddc xmlns:qdc="http://dspace.org/qualifieddc/" xmlns:dc="http://purl.org/dc/elements/1.1/" 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://purl.org/dc/elements/1.1/ http://dublincore.org/schemas/xmls/qdc/2006/01/06/dc.xsd http://purl.org/dc/terms/ http://dublincore.org/schemas/xmls/qdc/2006/01/06/dcterms.xsd http://dspace.org/qualifieddc/ http://www.ukoln.ac.uk/metadata/dcmi/xmlschema/qualifieddc.xsd">
   <dc:title>A new approach to obtain pure and active proteins from Lactococcus lactis protein aggregates</dc:title>
   <dc:creator>Gifre-Renom, L.</dc:creator>
   <dc:creator>Cano-Garrido, O.</dc:creator>
   <dc:creator>Fàbregas, F.</dc:creator>
   <dc:creator>Roca-Pinilla, R.</dc:creator>
   <dc:creator>Seras-Franzoso, J.</dc:creator>
   <dc:creator>Ferrer-Miralles, N.</dc:creator>
   <dc:creator>Villaverde, A.</dc:creator>
   <dc:creator>Bach, A.</dc:creator>
   <dc:creator>Devant, M.</dc:creator>
   <dc:creator>Arís, A.</dc:creator>
   <dc:creator>Garcia-Fruitós, E.</dc:creator>
   <dc:contributor>Producció Animal</dc:contributor>
   <dc:contributor>Producció de Remugants</dc:contributor>
   <dcterms:abstract>The production of pure and soluble proteins is a complex, protein-dependent and time-consuming&#xd;
process, in particular for those prone-to-aggregate and/or difcult-to-purify. Although Escherichia coli is&#xd;
widely used for protein production, recombinant products must be co-purifed through costly processes&#xd;
to remove lipopolysaccharide (LPS) and minimize adverse efects in the target organism. Interestingly,&#xd;
Lactococcus lactis, which does not contain LPS, could be a promising alternative for the production&#xd;
of relevant proteins. However, to date, there is no universal strategy to produce and purify any&#xd;
recombinant protein, being still a protein-specifc process. In this context and considering that L. lactis&#xd;
is also able to form functional protein aggregates under overproduction conditions, we explored the use&#xd;
of these aggregates as an alternative source of soluble proteins. In this study, we developed a widely&#xd;
applicable and economically afordable protocol to extract functional proteins from these nanoclusters.&#xd;
For that, two model proteins were used: mammary serum amyloid A3 (M-SAA3) and metalloproteinase&#xd;
9 (MMP-9), a difcult-to-purify and a prone-to-aggregate protein, respectively. The results show that&#xd;
it is possible to obtain highly pure, soluble, LPS-free and active recombinant proteins from L. lactis&#xd;
aggregates through a cost-efective and simple protocol with special relevance for difcult-to-purify or&#xd;
highly aggregated proteins.</dcterms:abstract>
   <dcterms:dateAccepted>2025-10-22T11:14:37Z</dcterms:dateAccepted>
   <dcterms:available>2025-10-22T11:14:37Z</dcterms:available>
   <dcterms:created>2025-10-22T11:14:37Z</dcterms:created>
   <dcterms:issued>2018-09-17</dcterms:issued>
   <dc:type>info:eu-repo/semantics/article</dc:type>
   <dc:identifier>Gifre-Renom, L., O. Cano-Garrido, F. Fàbregas, R. Roca-Pinilla, J. Seras-Franzoso, N. Ferrer-Miralles, and A. Villaverde et al. 2018. "A New Approach To Obtain Pure And Active Proteins From Lactococcus Lactis Protein Aggregates". Scientific Reports 8 (1). Springer Nature America, Inc. doi:10.1038/s41598-018-32213-8.</dc:identifier>
   <dc:identifier>2045-2322</dc:identifier>
   <dc:identifier>http://hdl.handle.net/20.500.12327/206</dc:identifier>
   <dc:identifier>https://doi.org/10.1038/s41598-018-32213-8</dc:identifier>
   <dc:language>eng</dc:language>
   <dc:relation>Scientific Reports</dc:relation>
   <dc:relation>INIA/Programa Estatal de I+D+I orientada a los retos de la sociedad/RTA2015-00064-C02-01/ES/Validación del uso de las proteínas M-SAA3 y MMP-9 en la mejora del secado de la vaca de leche y optimización de su dosis efectiva mediante su nanoestructuración/</dc:relation>
   <dc:relation>INIA/Programa Estatal de I+D+I orientada a los retos de la sociedad/RTA2015-00064-C02-02/ES/Validación del uso de las proteínas M-SAA3 y MMP-9 en la mejora del secado de la vaca de leche y optimización de su dosis efectiva mediante su nanoestructuración/</dc:relation>
   <dc:rights>http://creativecommons.org/licenses/by/4.0/</dc:rights>
   <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
   <dc:rights>Attribution 4.0 International</dc:rights>
   <dc:publisher>Nature Research</dc:publisher>
</qdc:qualifieddc></metadata></record></GetRecord></OAI-PMH>