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<PubmedArticle><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31673063</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>03</Day></DateCompleted><DateRevised><Year>2021</Year><Month>01</Month><Day>10</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>Oct</Month><Day>31</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>Surface modification of polyester fabric using plasma-dendrimer for robust immobilization of glucose oxidase enzyme.</ArticleTitle><Pagination><StartPage>15730</StartPage><MedlinePgn>15730</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">15730</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41598-019-52087-8</ELocationID><Abstract><AbstractText>Robust immobilization of glucose oxidase (GOx) enzyme was achieved on poly(ethylene&#xa0;terephthalate) nonwoven fabric (PN) after integration of favourable surface functional groups through plasma treatments [atmospheric pressure-AP or cold remote plasma-CRP (N<sub>2</sub>&#x2009;+&#x2009;O<sub>2</sub>)] and/or chemical grafting of hyperbranched dendrimers [poly-(ethylene glycol)-OH or poly-(amidoamine)]. Absorption, stability, catalytic behavior of immobilized enzymes and reusability of resultant fibrous bio-catalysts were comparatively studied. Full characterization of PN before and after respective modifications was carried out by various analytical, instrumental and arithmetic techniques. Results showed that modified polyester having amine terminal functional groups pledged better surface property providing up to 31% enzyme loading, and 81% active immobilized enzymes. The activity of the enzyme was measured in terms of interaction aptitude of GOx in a given time to produce hydrogen peroxide using colorimetric assay. The immobilized GOx retained 50% of its original activity after being reused six (06) times and exhibited improved stability compared with the free enzyme in relation to temperature. The reaction kinetics, loading efficiency, leaching, and reusability analysis of enzyme allowed drawing a parallel to the type of organic moiety integrated during GOx immobilization. In addition, resultant fibrous bio-catalysts showed substantial antibacterial activity against pathogenic bacteria strains (Staphylococcus epidermidis and Escherichia coli) in the presence of oxygen and glucose. These results are of great importance because they provide proof-of-concept for robust immobilization of enzymes on surface-modified fibrous polyester fabric for potential bio-industrial applications.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Morshed</LastName><ForeName>Mohammad Neaz</ForeName><Initials>MN</Initials><AffiliationInfo><Affiliation>Textile Material Technology, Department of Textile Technology, The Swedish School of Textiles, Faculty of Textiles, Engineering and Business, University of Bor&#xe5;s, SE-50190, Bor&#xe5;s, Sweden. mohammad_neaz.morshed@hb.se.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Ecole Nationale Sup&#xe9;rieure des Arts et Industries Textiles (ENSAIT), GEMTEX Laboratory, 2 all&#xe9;e Louise et Victor Champier BP 30329, 59056, Roubaix, France. mohammad_neaz.morshed@hb.se.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Universit&#xe9; de Lille, Nord de France, F-59000, Lille, France. mohammad_neaz.morshed@hb.se.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>College of Textile and Clothing Engineering, Soochow University, 215006, Suzhou, China. mohammad_neaz.morshed@hb.se.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Behary</LastName><ForeName>Nemeshwaree</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Ecole Nationale Sup&#xe9;rieure des Arts et Industries Textiles (ENSAIT), GEMTEX Laboratory, 2 all&#xe9;e Louise et Victor Champier BP 30329, 59056, Roubaix, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Universit&#xe9; de Lille, Nord de France, F-59000, Lille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bouazizi</LastName><ForeName>Nabil</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Ecole Nationale Sup&#xe9;rieure des Arts et Industries Textiles (ENSAIT), GEMTEX Laboratory, 2 all&#xe9;e Louise et Victor Champier BP 30329, 59056, Roubaix, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Universit&#xe9; de Lille, Nord de France, F-59000, Lille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guan</LastName><ForeName>Jinping</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>College of Textile and Clothing Engineering, Soochow University, 215006, Suzhou, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Guoqiang</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>College of Textile and Clothing Engineering, Soochow University, 215006, Suzhou, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nierstrasz</LastName><ForeName>Vincent</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Textile Material Technology, Department of Textile Technology, The Swedish School of Textiles, Faculty of Textiles, Engineering and Business, University of Bor&#xe5;s, SE-50190, Bor&#xe5;s, Sweden.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>10</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Sci Rep</MedlineTA><NlmUniqueID>101563288</NlmUniqueID><ISSNLinking>2045-2322</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050091">Dendrimers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004800">Enzymes, Immobilized</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D058626">Plasma Gases</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011091">Polyesters</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.4</RegistryNumber><NameOfSubstance UI="D005949">Glucose Oxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D055162" MajorTopicYN="N">Biocatalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003124" MajorTopicYN="N">Colorimetry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050091" MajorTopicYN="N">Dendrimers</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004800" MajorTopicYN="N">Enzymes, Immobilized</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005949" MajorTopicYN="N">Glucose Oxidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058626" MajorTopicYN="N">Plasma Gases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011091" MajorTopicYN="N">Polyesters</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013212" MajorTopicYN="N">Staphylococcus epidermidis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading></MeshHeadingList><CoiStatement>The authors declare no competing interests.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>7</Month><Day>4</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>10</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>11</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>11</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>11</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pmc-release"><Year>2019</Year><Month>10</Month><Day>31</Day></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31673063</ArticleId><ArticleId IdType="pmc">PMC6823486</ArticleId><ArticleId IdType="doi">10.1038/s41598-019-52087-8</ArticleId><ArticleId IdType="pii">10.1038/s41598-019-52087-8</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Kirk O, Borchert TV, Fuglsang CC. 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               <h2><a href="https://www.litmetric.com/detail/31673063/Surface-modification-of-polyester-fabric-using-plasma-dendrimer-for-robust-immobilization-of-glucose" >Surface modification of polyester fabric using plasma-dendrimer for robust immobilization of glucose oxidase enzyme.</a></h2>
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                <div class="publication-auther"><a href="https://www.litmetric.com/author/Mohammad+Neaz+Morshed" class="tag" style="margin-bottom: 5px;">Mohammad Neaz Morshed</a> <a href="https://www.litmetric.com/author/Nemeshwaree+Behary" class="tag" style="margin-bottom: 5px;">Nemeshwaree Behary</a> <a href="https://www.litmetric.com/author/Nabil+Bouazizi" class="tag" style="margin-bottom: 5px;">Nabil Bouazizi</a> <a href="https://www.litmetric.com/author/Jinping+Guan" class="tag" style="margin-bottom: 5px;">Jinping Guan</a> <a href="https://www.litmetric.com/author/Guoqiang+Chen" class="tag" style="margin-bottom: 5px;">Guoqiang Chen</a> <a href="https://www.litmetric.com/author/Vincent+Nierstrasz" class="tag" style="margin-bottom: 5px;">Vincent Nierstrasz</a></div>                   
                    <p class="mb-0 dark-color fz15 fw500 list-inline-item ml15 mb5-sm ml0-xs"><i class="flaticon-contract vam fz20 me-2"></i> Sci Rep</p>
              
                   <p class="mb-0 dark-color fz15 fw500 list-inline-item mr15  mb5-sm ml0-xs"><i class="flaticon-place text-thm2 vam fz20 me-2"></i> Textile Material Technology, Department of Textile Technology, The Swedish School of Textiles, Faculty of Textiles, Engineering and Business, <a href='https://www.litmetric.com/search/University+of+Bor%C3%A5s%5BAffiliation%5D' style='text-decoration: underline'>University of Borås</a>, SE-50190, Borås, Sweden.</p>
                    
                     
                   <p class="mb-0 dark-color fz15 fw500 list-inline-item ml15 mb5-sm ml0-xs"><i class="flaticon-calendar vam fz20 me-2"></i> Published: October 2019</p>
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                   <p class="text mb30"><p class="text mt10">Robust immobilization of glucose oxidase (GOx) enzyme was achieved on poly(ethylene terephthalate) nonwoven fabric (PN) after integration of favourable surface functional groups through plasma treatments [atmospheric pressure-AP or cold remote plasma-CRP (N + O)] and/or chemical grafting of hyperbranched dendrimers [poly-(ethylene glycol)-OH or poly-(amidoamine)]. Absorption, stability, catalytic behavior of immobilized enzymes and reusability of resultant fibrous bio-catalysts were comparatively studied. Full characterization of PN before and after respective modifications was carried out by various analytical, instrumental and arithmetic techniques. Results showed that modified polyester having amine terminal functional groups pledged better surface property providing up to 31% enzyme loading, and 81% active immobilized enzymes. The activity of the enzyme was measured in terms of interaction aptitude of GOx in a given time to produce hydrogen peroxide using colorimetric assay. The immobilized GOx retained 50% of its original activity after being reused six (06) times and exhibited improved stability compared with the free enzyme in relation to temperature. The reaction kinetics, loading efficiency, leaching, and reusability analysis of enzyme allowed drawing a parallel to the type of organic moiety integrated during GOx immobilization. In addition, resultant fibrous bio-catalysts showed substantial antibacterial activity against pathogenic bacteria strains (Staphylococcus epidermidis and Escherichia coli) in the presence of oxygen and glucose. These results are of great importance because they provide proof-of-concept for robust immobilization of enzymes on surface-modified fibrous polyester fabric for potential bio-industrial applications.</p><table class="table table-bordered table-striped downloadTable" >
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										  <div class="list-number">robust immobilization</div>
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