<?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>0188-4999</journal-id>
<journal-title><![CDATA[Revista internacional de contaminación ambiental]]></journal-title>
<abbrev-journal-title><![CDATA[Rev. Int. Contam. Ambient]]></abbrev-journal-title>
<issn>0188-4999</issn>
<publisher>
<publisher-name><![CDATA[Universidad Nacional Autónoma de México, Instituto de Ciencias de la Atmósfera y Cambio Climático]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S0188-49992025000100121</article-id>
<article-id pub-id-type="doi">10.20937/rica.55266</article-id>
<title-group>
<article-title xml:lang="en"><![CDATA[Studies for lipase production ability of Aspergillus sp. strains from the misiones rainforest of paranaense]]></article-title>
<article-title xml:lang="es"><![CDATA[Estudio de la capacidad de producción de lipasas de Aspergillus sp. provenientes de la selva misionera paranaense]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Ortellado]]></surname>
<given-names><![CDATA[Laura Ester]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
<xref ref-type="aff" rid="Aaf"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Villalba]]></surname>
<given-names><![CDATA[Laura Lidia]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Zapata]]></surname>
<given-names><![CDATA[Pedro Darío]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
<xref ref-type="aff" rid="Aaf"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Fonseca]]></surname>
<given-names><![CDATA[María Isabel]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
<xref ref-type="aff" rid="Aaf"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Nacional de Misiones Instituto de Biotecnología de Misiones &#8220;Dra. Maria Ebe Reca&#8221; Facultad de Ciencias Exactas Químicas y Naturales]]></institution>
<addr-line><![CDATA[ ]]></addr-line>
<country>Argentina</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,Consejo Nacional de Investigaciones Científicas y Técnicas  ]]></institution>
<addr-line><![CDATA[Buenos Aires ]]></addr-line>
<country>Argentina</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>00</month>
<year>2025</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>00</month>
<year>2025</year>
</pub-date>
<volume>41</volume>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S0188-49992025000100121&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S0188-49992025000100121&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S0188-49992025000100121&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="en"><p><![CDATA[ABSTRACT Fungi of the Aspergillus genus synthesize lipases, which are primarily extracellular enzymes secreted into the culture medium. These lipases have broad substrate specificity and are capable of hydrolyzing a variety of lipids, including triglycerides, phospholipids, and cholesterol esters, making them the focus of many studies on their applications. The present work carried out an exploratory analysis of the production of lipases in six fungi of the genus Aspergillus isolated in the Misionera Paranaense jungle (Argentina). Using simple qualitative detection techniques with tween 80% and rhodamine B as substrates, and based on the quantitative analysis carried out, it was determined that the isolate Aspergillus sp. LBM 054 showed the highest levels of lipase activity, reaching a total of 133 U/mL. A Plackett-Burman statistical test revealed that adding tributyrin to the culture medium significantly increased the activity of the lipase enzyme (p &lt; 0.05), reaching a value of 168 U/mL. Among the concentrations evaluated, the addition of 2% tributyrin demonstrated the greatest increase in lipase activity, reaching a five-fold increase compared to the initial activity observed at the beginning of the assays. Optimum activity and stability at neutral to alkaline pH values make these enzymes suitable for various biotechnological applications. The zymogram of the selected strain showed an enzymatic profile that included a protein with a molecular mass of 38 kDa.]]></p></abstract>
<abstract abstract-type="short" xml:lang="es"><p><![CDATA[RESUMEN Las lipasas sintetizadas por hongos del género Aspergillus son en su mayoría enzimas extracelulares que se secretan al medio de cultivo. Estas lipasas tienen una amplia especificidad de sustrato y son capaces de hidrolizar una variedad de lípidos, incluidos triglicéridos, fosfolípidos y ésteres de colesterol, lo que las convierte en el foco de muchos estudios sobre sus aplicaciones. El presente trabajo realizó un análisis exploratorio de la producción de lipasas en seis hongos del género Aspergillus aislados en la selva Misionera Paranaense (Argentina). Utilizando técnicas simples de detección cualitativa con tween 80% y rodamina B como sustratos, y basándonos en el análisis cuantitativo realizado, se determinó que el aislado Aspergillus sp. LBM 054 mostró los niveles más altos de actividad lipasa, alcanzando un total de 133 U/mL. Una prueba estadística de Plackett-Burman reveló que la adición de tributirina al medio de cultivo incrementaba significativamente la actividad de la enzima lipasa (p &lt; 0.05), alcanzando un valor de 168 U/mL. Entre las concentraciones evaluadas, la adición de 2% de tributirina demostró el mayor aumento en la actividad de la lipasa, alcanzando un aumento de cinco veces en comparación con la actividad inicial observada al inicio de los ensayos. La actividad óptima y estabilidad a valores de pH neutros a alcalinos hacen que estas enzimas sean adecuadas para diversas aplicaciones biotecnológicas. El zimograma de la cepa seleccionada mostró un perfil enzimático que incluyó una proteína con una masa molecular de 38 kDa.]]></p></abstract>
<kwd-group>
<kwd lng="en"><![CDATA[Fungi]]></kwd>
<kwd lng="en"><![CDATA[hydrolase]]></kwd>
<kwd lng="en"><![CDATA[enzyme activity]]></kwd>
<kwd lng="en"><![CDATA[optimization]]></kwd>
<kwd lng="en"><![CDATA[Plackett-Burman]]></kwd>
<kwd lng="es"><![CDATA[hongos]]></kwd>
<kwd lng="es"><![CDATA[hidrolasa]]></kwd>
<kwd lng="es"><![CDATA[actividad enzimática]]></kwd>
<kwd lng="es"><![CDATA[optimización]]></kwd>
<kwd lng="es"><![CDATA[Plackett-Burman]]></kwd>
</kwd-group>
</article-meta>
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