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		<identifier>oai:rcin.org.pl:253358</identifier>
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<dc:title xml:lang="en"><![CDATA[Genipin as an Effective Crosslinker for High-Performance and Flexible Direct-Printed Bioelectrodes]]></dc:title>
<dc:title xml:lang="pl"><![CDATA[K.Bobrowska; Molecules 2026]]></dc:title>
<dc:creator><![CDATA[Bobrowska, Kornelia]]></dc:creator>
<dc:creator><![CDATA[Urbanowicz, Marcin]]></dc:creator>
<dc:creator><![CDATA[Paziewska-Nowak, Agnieszka]]></dc:creator>
<dc:creator><![CDATA[Dawgul, Marek]]></dc:creator>
<dc:creator><![CDATA[Sadowska, Kamila. kierownik projektu]]></dc:creator>
<dc:subject xml:lang="en"><![CDATA[AD-dependentglucosedehydrogenase]]></dc:subject>
<dc:subject xml:lang="en"><![CDATA[mediatedelectrontransfer]]></dc:subject>
<dc:subject xml:lang="en"><![CDATA[genipin]]></dc:subject>
<dc:subject xml:lang="en"><![CDATA[directprinting]]></dc:subject>
<dc:subject xml:lang="pl"><![CDATA[FAD-zależna dehydrogenaza glukozy]]></dc:subject>
<dc:subject xml:lang="pl"><![CDATA[druk bezpośredni]]></dc:subject>
<dc:subject xml:lang="pl"><![CDATA[bioanoda]]></dc:subject>
<dc:subject xml:lang="pl"><![CDATA[genipina]]></dc:subject>
<dc:description xml:lang="en"><![CDATA[The development of efficient bioelectrodes requires suitable fabrication strategies, starting with the electrode material, which affects the electron transfer between the biocatalyst and the electrode surface. Then, selection and adjustment of the enzyme immobilization conditions are essential to enhance the performance of the bioelectrodes for their desirable utility. In this study, we report the fabrication of a high-performance bioelectrode using a one-step crosslinking of FAD-dependent glucose dehydrogenase (FAD-GDH) and thionine acetate as a redox mediator, with genipin serving as a natural, biocompatible crosslinker. Electrodes were manufactured on flexible polyester substrates using a direct printing technique, enabling reproducible and low-cost production. Among the tested crosslinkers, genipin significantly enhanced the catalytic performance of bioelectrodes. Comparative studies on graphite, silver, and gold electrode materials identified graphite as the most suitable due to its extended electroactive surface area. The developed bioelectrodes applied to glucose biosensing demonstrated a linear amperometric response to glucose in the range of 0.02–2 mM and 0.048–30 mM, covering clinically relevant concentrations. The application of artificial sweat confirmed high detection accuracy. These findings highlight the potential integration of genipin-based enzyme–mediator networks for future non-invasive sweat glucose monitoring platforms.]]></dc:description>
<dc:description xml:lang="en"><![CDATA[24 p., 6+6 ill. ; 30 cm]]></dc:description>
<dc:description xml:lang="pl"><![CDATA[The development of efficient bioelectrodes requires suitable fabrication strategies, starting with the electrode material, which affects the electron transfer between the biocatalyst and the electrode surface. Then, selection and adjustment of the enzyme immobilization conditions are essential to enhance the performance of the bioelectrodes for their desirable utility. In this study, we report the fabrication of a high-performance bioelectrode using a one-step crosslinking of FAD-dependent glucose dehydrogenase (FAD-GDH) and thionine acetate as a redox mediator, with genipin serving as a natural, biocompatible crosslinker. Electrodes were manufactured on flexible polyester substrates using a direct printing technique, enabling reproducible and low-cost production. Among the tested crosslinkers, genipin significantly enhanced the catalytic performance of bioelectrodes. Comparative studies on graphite, silver, and gold electrode materials identified graphite as the most suitable due to its extended electroactive surface area. The developed bioelectrodes applied to glucose biosensing demonstrated a linear amperometric response to glucose in the range of 0.02–2 mM and 0.048–30 mM, covering clinically relevant concentrations. The application of artificial sweat confirmed high detection accuracy. These findings highlight the potential integration of genipin-based enzyme–mediator networks for future non-invasive sweat glucose monitoring platforms.]]></dc:description>
<dc:description xml:lang="pl"><![CDATA[24 strony, 30 cm, 6+6 rys.]]></dc:description>
<dc:publisher><![CDATA[MDPI, Basel, Switzerland]]></dc:publisher>
<dc:date><![CDATA[2026.01.17]]></dc:date>
<dc:type xml:lang="en"><![CDATA[Text]]></dc:type>
<dc:type xml:lang="pl"><![CDATA[Tekst]]></dc:type>
<dc:format xml:lang="en"><![CDATA[PDF]]></dc:format>
<dc:format xml:lang="pl"><![CDATA[PDF]]></dc:format>
<dc:identifier><![CDATA[https://rcin.org.pl/dlibra/publication/290352/edition/253358/content]]></dc:identifier>
<dc:identifier><![CDATA[oai:rcin.org.pl:253358]]></dc:identifier>
<dc:source xml:lang="en"><![CDATA[Molecules]]></dc:source>
<dc:source xml:lang="pl"><![CDATA[Molecules]]></dc:source>
<dc:language><![CDATA[ang.]]></dc:language>
<dc:language><![CDATA[eng; sum. eng.]]></dc:language>
<dc:relation><![CDATA[Molecules 2026, 31, 327]]></dc:relation>
<dc:relation><![CDATA[oai:rcin.org.pl:publication:290352]]></dc:relation>
<dc:rights xml:lang="en"><![CDATA[Rights Reserved - Free Access]]></dc:rights>
<dc:rights xml:lang="pl"><![CDATA[Prawa zastrzeżone - dostęp nieograniczony]]></dc:rights>
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