Lipase Immobilization on Differently Functionalized Vinyl-Based Amphiphilic Polymers: Influence of Phase Segregation on the Enzyme Hydrolytic Activity
Microbial lipase from Candida rugosa was immobilized by physical adsorption onto an ethylene–vinyl alcohol polymer (EVAL) functionalized with acyl chlorides. To evaluate the influence of the reagent chain-length on the amount and activity of immobilized lipase, three differently long aliphatic fatty...
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| Veröffentlicht in: | Biomacromolecules 2012-03, Vol.13 (3), p.805-813 |
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| creator | Bellusci, Mariangela Francolini, Iolanda Martinelli, Andrea D’Ilario, Lucio Piozzi, Antonella |
| description | Microbial lipase from Candida rugosa was immobilized by physical adsorption onto an ethylene–vinyl alcohol polymer (EVAL) functionalized with acyl chlorides. To evaluate the influence of the reagent chain-length on the amount and activity of immobilized lipase, three differently long aliphatic fatty acids were employed (C8, C12, C18), obtaining EVAL functionalization degrees ranging from 5% to 65%. The enzyme–polymer affinity increased with both the length of the alkyl chain and the matrix hydrophobicity. In particular, the esterified polymers showed a tendency to give segregated hydrophilic and hydrophobic domains. It was observed the formation of an enzyme multilayer at both low and high protein concentrations. Desorption experiments showed that Candida rugosa lipase may be adsorbed in a closed form on the polymer hydrophilic domains and in an open, active structure on the hydrophobic ones. The best results were found for the EVAL-C18 13% matrix that showed hyperactivation with both the soluble and unsoluble substrate after enzyme desorption. In addition, this supported biocatalyst retained its activity for repetitive cycles. |
| doi_str_mv | 10.1021/bm2017228 |
| format | Article |
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To evaluate the influence of the reagent chain-length on the amount and activity of immobilized lipase, three differently long aliphatic fatty acids were employed (C8, C12, C18), obtaining EVAL functionalization degrees ranging from 5% to 65%. The enzyme–polymer affinity increased with both the length of the alkyl chain and the matrix hydrophobicity. In particular, the esterified polymers showed a tendency to give segregated hydrophilic and hydrophobic domains. It was observed the formation of an enzyme multilayer at both low and high protein concentrations. Desorption experiments showed that Candida rugosa lipase may be adsorbed in a closed form on the polymer hydrophilic domains and in an open, active structure on the hydrophobic ones. The best results were found for the EVAL-C18 13% matrix that showed hyperactivation with both the soluble and unsoluble substrate after enzyme desorption. In addition, this supported biocatalyst retained its activity for repetitive cycles.</description><identifier>ISSN: 1525-7797</identifier><identifier>EISSN: 1526-4602</identifier><identifier>DOI: 10.1021/bm2017228</identifier><identifier>PMID: 22295868</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Applied sciences ; Biological and medical sciences ; Biotechnology ; Candida - enzymology ; Candida rugosa ; Enzymes, Immobilized - chemistry ; Exact sciences and technology ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Hydrolysis ; Hydrophobic and Hydrophilic Interactions ; Immobilization of enzymes and other molecules ; Immobilization techniques ; Kinetics ; Lipase - chemistry ; Lipase - metabolism ; Magnetic Resonance Spectroscopy ; Methods. Procedures. Technologies ; Organic polymers ; Physicochemistry of polymers ; Polymers - chemistry ; Polymers - metabolism ; Properties and characterization ; Special properties (catalyst, reagent or carrier) ; Temperature ; Vinyl Compounds - chemistry</subject><ispartof>Biomacromolecules, 2012-03, Vol.13 (3), p.805-813</ispartof><rights>Copyright © 2012 American Chemical Society</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a377t-d907e538b5594a1900f48ae06b8787d032e57a447905c0b362b51f471831b543</citedby><cites>FETCH-LOGICAL-a377t-d907e538b5594a1900f48ae06b8787d032e57a447905c0b362b51f471831b543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bm2017228$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bm2017228$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25835791$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22295868$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bellusci, Mariangela</creatorcontrib><creatorcontrib>Francolini, Iolanda</creatorcontrib><creatorcontrib>Martinelli, Andrea</creatorcontrib><creatorcontrib>D’Ilario, Lucio</creatorcontrib><creatorcontrib>Piozzi, Antonella</creatorcontrib><title>Lipase Immobilization on Differently Functionalized Vinyl-Based Amphiphilic Polymers: Influence of Phase Segregation on the Enzyme Hydrolytic Activity</title><title>Biomacromolecules</title><addtitle>Biomacromolecules</addtitle><description>Microbial lipase from Candida rugosa was immobilized by physical adsorption onto an ethylene–vinyl alcohol polymer (EVAL) functionalized with acyl chlorides. To evaluate the influence of the reagent chain-length on the amount and activity of immobilized lipase, three differently long aliphatic fatty acids were employed (C8, C12, C18), obtaining EVAL functionalization degrees ranging from 5% to 65%. The enzyme–polymer affinity increased with both the length of the alkyl chain and the matrix hydrophobicity. In particular, the esterified polymers showed a tendency to give segregated hydrophilic and hydrophobic domains. It was observed the formation of an enzyme multilayer at both low and high protein concentrations. Desorption experiments showed that Candida rugosa lipase may be adsorbed in a closed form on the polymer hydrophilic domains and in an open, active structure on the hydrophobic ones. The best results were found for the EVAL-C18 13% matrix that showed hyperactivation with both the soluble and unsoluble substrate after enzyme desorption. In addition, this supported biocatalyst retained its activity for repetitive cycles.</description><subject>Applied sciences</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Candida - enzymology</subject><subject>Candida rugosa</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Exact sciences and technology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolysis</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Immobilization of enzymes and other molecules</subject><subject>Immobilization techniques</subject><subject>Kinetics</subject><subject>Lipase - chemistry</subject><subject>Lipase - metabolism</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Methods. Procedures. Technologies</subject><subject>Organic polymers</subject><subject>Physicochemistry of polymers</subject><subject>Polymers - chemistry</subject><subject>Polymers - metabolism</subject><subject>Properties and characterization</subject><subject>Special properties (catalyst, reagent or carrier)</subject><subject>Temperature</subject><subject>Vinyl Compounds - chemistry</subject><issn>1525-7797</issn><issn>1526-4602</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90d1qFDEUB_Agiv3QC19AciPVi6n5nCTerbW1CwstWLwdMpkz3ZTMzJrMFKYP0uc1a9ftjQgHEsLvnAP5I_SOklNKGP1cd4xQxZh-gQ6pZGUhSsJe_rnLQimjDtBRSneEEMOFfI0OGGNG6lIfoseV39gEeNl1Q-2Df7CjH3qc65tvW4jQj2HGF1Pvtu82A2jwT9_Pofia-xq86DZrnyt4h6-HMHcQ0xe87NswQe8ADy2-Xm83_IDbCLf78eMa8Hn_kD2-nJuYO8c8YZHX3PtxfoNetTYkeLs7j9HNxfnN2WWxuvq-PFusCsuVGovGEAWS61pKIyw1hLRCWyBlrZVWDeEMpLJCKEOkIzUvWS1pKxTVnNZS8GN08jR2E4dfE6Sx6nxyEILtYZhSZZjSnChJs_z4X5m_WnCjtFSZfnqiLg4pRWirTfSdjXNFSbXNq9rnle373dip7qDZy78BZfBhB2xyNrTR9s6nZyc1l8rQZ2ddqu6GKeas0j8W_gaEfal7</recordid><startdate>20120312</startdate><enddate>20120312</enddate><creator>Bellusci, Mariangela</creator><creator>Francolini, Iolanda</creator><creator>Martinelli, Andrea</creator><creator>D’Ilario, Lucio</creator><creator>Piozzi, Antonella</creator><general>American Chemical Society</general><scope>IQODW</scope><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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20120312</creationdate><title>Lipase Immobilization on Differently Functionalized Vinyl-Based Amphiphilic Polymers: Influence of Phase Segregation on the Enzyme Hydrolytic Activity</title><author>Bellusci, Mariangela ; Francolini, Iolanda ; Martinelli, Andrea ; D’Ilario, Lucio ; Piozzi, Antonella</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a377t-d907e538b5594a1900f48ae06b8787d032e57a447905c0b362b51f471831b543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Applied sciences</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Candida - enzymology</topic><topic>Candida rugosa</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Exact sciences and technology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolysis</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Immobilization of enzymes and other molecules</topic><topic>Immobilization techniques</topic><topic>Kinetics</topic><topic>Lipase - chemistry</topic><topic>Lipase - metabolism</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Methods. Procedures. Technologies</topic><topic>Organic polymers</topic><topic>Physicochemistry of polymers</topic><topic>Polymers - chemistry</topic><topic>Polymers - metabolism</topic><topic>Properties and characterization</topic><topic>Special properties (catalyst, reagent or carrier)</topic><topic>Temperature</topic><topic>Vinyl Compounds - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bellusci, Mariangela</creatorcontrib><creatorcontrib>Francolini, Iolanda</creatorcontrib><creatorcontrib>Martinelli, Andrea</creatorcontrib><creatorcontrib>D’Ilario, Lucio</creatorcontrib><creatorcontrib>Piozzi, Antonella</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biomacromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bellusci, Mariangela</au><au>Francolini, Iolanda</au><au>Martinelli, Andrea</au><au>D’Ilario, Lucio</au><au>Piozzi, Antonella</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lipase Immobilization on Differently Functionalized Vinyl-Based Amphiphilic Polymers: Influence of Phase Segregation on the Enzyme Hydrolytic Activity</atitle><jtitle>Biomacromolecules</jtitle><addtitle>Biomacromolecules</addtitle><date>2012-03-12</date><risdate>2012</risdate><volume>13</volume><issue>3</issue><spage>805</spage><epage>813</epage><pages>805-813</pages><issn>1525-7797</issn><eissn>1526-4602</eissn><abstract>Microbial lipase from Candida rugosa was immobilized by physical adsorption onto an ethylene–vinyl alcohol polymer (EVAL) functionalized with acyl chlorides. To evaluate the influence of the reagent chain-length on the amount and activity of immobilized lipase, three differently long aliphatic fatty acids were employed (C8, C12, C18), obtaining EVAL functionalization degrees ranging from 5% to 65%. The enzyme–polymer affinity increased with both the length of the alkyl chain and the matrix hydrophobicity. In particular, the esterified polymers showed a tendency to give segregated hydrophilic and hydrophobic domains. It was observed the formation of an enzyme multilayer at both low and high protein concentrations. Desorption experiments showed that Candida rugosa lipase may be adsorbed in a closed form on the polymer hydrophilic domains and in an open, active structure on the hydrophobic ones. The best results were found for the EVAL-C18 13% matrix that showed hyperactivation with both the soluble and unsoluble substrate after enzyme desorption. In addition, this supported biocatalyst retained its activity for repetitive cycles.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>22295868</pmid><doi>10.1021/bm2017228</doi><tpages>9</tpages></addata></record> |
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| subjects | Applied sciences Biological and medical sciences Biotechnology Candida - enzymology Candida rugosa Enzymes, Immobilized - chemistry Exact sciences and technology Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolysis Hydrophobic and Hydrophilic Interactions Immobilization of enzymes and other molecules Immobilization techniques Kinetics Lipase - chemistry Lipase - metabolism Magnetic Resonance Spectroscopy Methods. Procedures. Technologies Organic polymers Physicochemistry of polymers Polymers - chemistry Polymers - metabolism Properties and characterization Special properties (catalyst, reagent or carrier) Temperature Vinyl Compounds - chemistry |
| title | Lipase Immobilization on Differently Functionalized Vinyl-Based Amphiphilic Polymers: Influence of Phase Segregation on the Enzyme Hydrolytic Activity |
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