Preparation of a Cu(II)-PVA/PA6 composite nanofibrous membrane for enzyme immobilization
PVA/PA6 composite nanofibers were formed by electrospinning. Cu(II)-PVA/PA6 metal chelated nanofibers, prepared by the reaction between PVA/PA6 composite nanofibers and Cu2+ solution, were used as the support for catalase immobilization. The result of the experiments showed that PVA/PA6 composite na...
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creator | Feng, Quan Tang, Bin Wei, Qufu Hou, Dayin Bi, Songmei Wei, Anfang |
description | PVA/PA6 composite nanofibers were formed by electrospinning. Cu(II)-PVA/PA6 metal chelated nanofibers, prepared by the reaction between PVA/PA6 composite nanofibers and Cu2+ solution, were used as the support for catalase immobilization. The result of the experiments showed that PVA/PA6 composite nanofibers had an excellent chelation capacity for Cu2+ ions, and the structures of nanofibers were stable during the reaction with Cu2+ solution. The adsorption of Cu(II) onto PVA/PA6 composite nanofibers was studied by the Langmuir isothermal adsorption model. The maximum amount of coordinated Cu(II) (q(m)) was 3.731 mmol/g (dry fiber), and the binding constant (K(l)) was 0.0593 L/mmol. Kinetic parameters were analyzed for both immobilized and free catalases. The value of V(max) (3774 μmol/mg·min) for the immobilized catalases was smaller than that of the free catalases (4878 μmol/mg·min), while the K(m) for the immobilized catalases was larger. The immobilized catalases showed better resistance to pH and temperature than that of free form, and the storage stabilities, reusability of immobilized catalases were significantly improved. The half-lives of free and immobilized catalases were 8 days and 24 days, respectively. |
doi_str_mv | 10.3390/ijms131012734 |
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Cu(II)-PVA/PA6 metal chelated nanofibers, prepared by the reaction between PVA/PA6 composite nanofibers and Cu2+ solution, were used as the support for catalase immobilization. The result of the experiments showed that PVA/PA6 composite nanofibers had an excellent chelation capacity for Cu2+ ions, and the structures of nanofibers were stable during the reaction with Cu2+ solution. The adsorption of Cu(II) onto PVA/PA6 composite nanofibers was studied by the Langmuir isothermal adsorption model. The maximum amount of coordinated Cu(II) (q(m)) was 3.731 mmol/g (dry fiber), and the binding constant (K(l)) was 0.0593 L/mmol. Kinetic parameters were analyzed for both immobilized and free catalases. The value of V(max) (3774 μmol/mg·min) for the immobilized catalases was smaller than that of the free catalases (4878 μmol/mg·min), while the K(m) for the immobilized catalases was larger. The immobilized catalases showed better resistance to pH and temperature than that of free form, and the storage stabilities, reusability of immobilized catalases were significantly improved. The half-lives of free and immobilized catalases were 8 days and 24 days, respectively.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms131012734</identifier><identifier>PMID: 23202922</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Adsorption ; Caprolactam - analogs & derivatives ; Caprolactam - chemistry ; Catalase - chemistry ; Catalase - metabolism ; Copper - chemistry ; Energy consumption ; Enzymes ; Enzymes, Immobilized - chemistry ; Enzymes, Immobilized - metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Membranes ; Nanofibers - chemistry ; Polymers ; Polymers - chemistry ; Polyvinyl Alcohol - chemistry ; Temperature ; Textiles</subject><ispartof>International journal of molecular sciences, 2012-10, Vol.13 (10), p.12734-12746</ispartof><rights>Copyright MDPI AG 2012</rights><rights>2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c481t-9b48089ab83f0919b24a0758d6ca034e604f91f1254fb254effae63f16038d33</citedby><cites>FETCH-LOGICAL-c481t-9b48089ab83f0919b24a0758d6ca034e604f91f1254fb254effae63f16038d33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3497296/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3497296/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23202922$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Feng, Quan</creatorcontrib><creatorcontrib>Tang, Bin</creatorcontrib><creatorcontrib>Wei, Qufu</creatorcontrib><creatorcontrib>Hou, Dayin</creatorcontrib><creatorcontrib>Bi, Songmei</creatorcontrib><creatorcontrib>Wei, Anfang</creatorcontrib><title>Preparation of a Cu(II)-PVA/PA6 composite nanofibrous membrane for enzyme immobilization</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>PVA/PA6 composite nanofibers were formed by electrospinning. Cu(II)-PVA/PA6 metal chelated nanofibers, prepared by the reaction between PVA/PA6 composite nanofibers and Cu2+ solution, were used as the support for catalase immobilization. The result of the experiments showed that PVA/PA6 composite nanofibers had an excellent chelation capacity for Cu2+ ions, and the structures of nanofibers were stable during the reaction with Cu2+ solution. The adsorption of Cu(II) onto PVA/PA6 composite nanofibers was studied by the Langmuir isothermal adsorption model. The maximum amount of coordinated Cu(II) (q(m)) was 3.731 mmol/g (dry fiber), and the binding constant (K(l)) was 0.0593 L/mmol. Kinetic parameters were analyzed for both immobilized and free catalases. The value of V(max) (3774 μmol/mg·min) for the immobilized catalases was smaller than that of the free catalases (4878 μmol/mg·min), while the K(m) for the immobilized catalases was larger. The immobilized catalases showed better resistance to pH and temperature than that of free form, and the storage stabilities, reusability of immobilized catalases were significantly improved. The half-lives of free and immobilized catalases were 8 days and 24 days, respectively.</description><subject>Adsorption</subject><subject>Caprolactam - analogs & derivatives</subject><subject>Caprolactam - chemistry</subject><subject>Catalase - chemistry</subject><subject>Catalase - metabolism</subject><subject>Copper - chemistry</subject><subject>Energy consumption</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Enzymes, Immobilized - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Membranes</subject><subject>Nanofibers - chemistry</subject><subject>Polymers</subject><subject>Polymers - chemistry</subject><subject>Polyvinyl Alcohol - chemistry</subject><subject>Temperature</subject><subject>Textiles</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpVUU1LAzEUDKLYWj16lYAXPazN12Y3F6EUPwoFeyjiLWS3iaY0mzXZFdpf72prqZc3D94wb5gB4BKjO0oFGtqli5hihElG2RHoY0ZIghDPjg_2HjiLcYkQoSQVp6DXISKCkD54mwVdq6Aa6yvoDVRw3N5MJrfJ7HU0nI04LL2rfbSNhpWqvLFF8G2ETrsiqEpD4wPU1WbtNLTO-cKu7OZX7BycGLWK-mKHAzB_fJiPn5Ppy9NkPJomJctxk4iC5SgXqsipQQKLgjCFsjRf8FIhyjRHzAhsMEmZKbqhjVGaU4M5ovmC0gG438rWbeH0otRVE9RK1sE6FdbSKyv_Xyr7Id_9l6RMZETwTuB6JxD8Z6tjI5e-DVVnWeKU8C5XinHHSrasMvgYgzb7DxjJnx7kvx46_tWhrT37L3j6DTwyg8w</recordid><startdate>20121005</startdate><enddate>20121005</enddate><creator>Feng, Quan</creator><creator>Tang, Bin</creator><creator>Wei, Qufu</creator><creator>Hou, Dayin</creator><creator>Bi, Songmei</creator><creator>Wei, Anfang</creator><general>MDPI AG</general><general>Molecular Diversity Preservation International (MDPI)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>5PM</scope></search><sort><creationdate>20121005</creationdate><title>Preparation of a Cu(II)-PVA/PA6 composite nanofibrous membrane for enzyme immobilization</title><author>Feng, Quan ; Tang, Bin ; Wei, Qufu ; Hou, Dayin ; Bi, Songmei ; Wei, Anfang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c481t-9b48089ab83f0919b24a0758d6ca034e604f91f1254fb254effae63f16038d33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Adsorption</topic><topic>Caprolactam - analogs & derivatives</topic><topic>Caprolactam - chemistry</topic><topic>Catalase - chemistry</topic><topic>Catalase - metabolism</topic><topic>Copper - chemistry</topic><topic>Energy consumption</topic><topic>Enzymes</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Enzymes, Immobilized - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Membranes</topic><topic>Nanofibers - chemistry</topic><topic>Polymers</topic><topic>Polymers - chemistry</topic><topic>Polyvinyl Alcohol - chemistry</topic><topic>Temperature</topic><topic>Textiles</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Feng, Quan</creatorcontrib><creatorcontrib>Tang, Bin</creatorcontrib><creatorcontrib>Wei, Qufu</creatorcontrib><creatorcontrib>Hou, Dayin</creatorcontrib><creatorcontrib>Bi, Songmei</creatorcontrib><creatorcontrib>Wei, Anfang</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Feng, Quan</au><au>Tang, Bin</au><au>Wei, Qufu</au><au>Hou, Dayin</au><au>Bi, Songmei</au><au>Wei, Anfang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation of a Cu(II)-PVA/PA6 composite nanofibrous membrane for enzyme immobilization</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2012-10-05</date><risdate>2012</risdate><volume>13</volume><issue>10</issue><spage>12734</spage><epage>12746</epage><pages>12734-12746</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>PVA/PA6 composite nanofibers were formed by electrospinning. Cu(II)-PVA/PA6 metal chelated nanofibers, prepared by the reaction between PVA/PA6 composite nanofibers and Cu2+ solution, were used as the support for catalase immobilization. The result of the experiments showed that PVA/PA6 composite nanofibers had an excellent chelation capacity for Cu2+ ions, and the structures of nanofibers were stable during the reaction with Cu2+ solution. The adsorption of Cu(II) onto PVA/PA6 composite nanofibers was studied by the Langmuir isothermal adsorption model. The maximum amount of coordinated Cu(II) (q(m)) was 3.731 mmol/g (dry fiber), and the binding constant (K(l)) was 0.0593 L/mmol. Kinetic parameters were analyzed for both immobilized and free catalases. The value of V(max) (3774 μmol/mg·min) for the immobilized catalases was smaller than that of the free catalases (4878 μmol/mg·min), while the K(m) for the immobilized catalases was larger. The immobilized catalases showed better resistance to pH and temperature than that of free form, and the storage stabilities, reusability of immobilized catalases were significantly improved. The half-lives of free and immobilized catalases were 8 days and 24 days, respectively.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>23202922</pmid><doi>10.3390/ijms131012734</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adsorption Caprolactam - analogs & derivatives Caprolactam - chemistry Catalase - chemistry Catalase - metabolism Copper - chemistry Energy consumption Enzymes Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Hydrogen-Ion Concentration Kinetics Membranes Nanofibers - chemistry Polymers Polymers - chemistry Polyvinyl Alcohol - chemistry Temperature Textiles |
title | Preparation of a Cu(II)-PVA/PA6 composite nanofibrous membrane for enzyme immobilization |
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