Immobilized Aspergillus niger Lipase with SiO2 Nanoparticles in Sol-Gel Materials
Lipase from Aspergillus niger was "doubly immobilized" with SiO2 nanoparticles in sol-gel powders prepared via the base-catalyzed polymerization of tetramethoxysilane (TMOS) and methyltreimethoxysilane (MTMS). The hydrolytic activity of the immobilized lipase was measured using the p-nitro...
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| Veröffentlicht in: | Catalysts 2016-01, Vol.6 (10), p.149-149 |
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| creator | Xu, Li Ke, Caixia Huang, Ying Yan, Yunjun |
| description | Lipase from Aspergillus niger was "doubly immobilized" with SiO2 nanoparticles in sol-gel powders prepared via the base-catalyzed polymerization of tetramethoxysilane (TMOS) and methyltreimethoxysilane (MTMS). The hydrolytic activity of the immobilized lipase was measured using the p-nitrophenyl palmitate hydrolysis method. The results showed that the optimum preparation conditions for the gels were made using a MTMS/TMOS molar ratio of 5, 60 mg of SiO2 nanoparticles, a water/silane molar ratio of 12, 120 mg of enzyme supply, and 120 mu L of PEG400. Under the optimal conditions, the immobilized lipase retained 92% of the loading protein and 94% of the total enzyme activity. Characteristic tests indicated that the immobilized lipase exhibited much higher thermal and pH stability than its free form, which shows great potential for industrial applications. |
| doi_str_mv | 10.3390/catal6100149 |
| format | Article |
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The hydrolytic activity of the immobilized lipase was measured using the p-nitrophenyl palmitate hydrolysis method. The results showed that the optimum preparation conditions for the gels were made using a MTMS/TMOS molar ratio of 5, 60 mg of SiO2 nanoparticles, a water/silane molar ratio of 12, 120 mg of enzyme supply, and 120 mu L of PEG400. Under the optimal conditions, the immobilized lipase retained 92% of the loading protein and 94% of the total enzyme activity. Characteristic tests indicated that the immobilized lipase exhibited much higher thermal and pH stability than its free form, which shows great potential for industrial applications.</description><identifier>ISSN: 2073-4344</identifier><identifier>EISSN: 2073-4344</identifier><identifier>DOI: 10.3390/catal6100149</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>Aspergillus niger ; Catalysts ; Chemical reactions ; Enzymes ; Lipase ; Nanoparticles ; Optimization ; Polymerization ; Silicon dioxide ; Sol gel process</subject><ispartof>Catalysts, 2016-01, Vol.6 (10), p.149-149</ispartof><rights>Copyright MDPI AG 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c367t-3e125e4df4317b540f51f351850925c6a7991a6593dad307fe9d3dbe61158df83</citedby><cites>FETCH-LOGICAL-c367t-3e125e4df4317b540f51f351850925c6a7991a6593dad307fe9d3dbe61158df83</cites><orcidid>0000-0001-6643-597X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Xu, Li</creatorcontrib><creatorcontrib>Ke, Caixia</creatorcontrib><creatorcontrib>Huang, Ying</creatorcontrib><creatorcontrib>Yan, Yunjun</creatorcontrib><title>Immobilized Aspergillus niger Lipase with SiO2 Nanoparticles in Sol-Gel Materials</title><title>Catalysts</title><description>Lipase from Aspergillus niger was "doubly immobilized" with SiO2 nanoparticles in sol-gel powders prepared via the base-catalyzed polymerization of tetramethoxysilane (TMOS) and methyltreimethoxysilane (MTMS). The hydrolytic activity of the immobilized lipase was measured using the p-nitrophenyl palmitate hydrolysis method. The results showed that the optimum preparation conditions for the gels were made using a MTMS/TMOS molar ratio of 5, 60 mg of SiO2 nanoparticles, a water/silane molar ratio of 12, 120 mg of enzyme supply, and 120 mu L of PEG400. Under the optimal conditions, the immobilized lipase retained 92% of the loading protein and 94% of the total enzyme activity. Characteristic tests indicated that the immobilized lipase exhibited much higher thermal and pH stability than its free form, which shows great potential for industrial applications.</description><subject>Aspergillus niger</subject><subject>Catalysts</subject><subject>Chemical reactions</subject><subject>Enzymes</subject><subject>Lipase</subject><subject>Nanoparticles</subject><subject>Optimization</subject><subject>Polymerization</subject><subject>Silicon dioxide</subject><subject>Sol gel process</subject><issn>2073-4344</issn><issn>2073-4344</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNqN0U1LAzEQBuAgCpbamz8g4MWDq8lOsrs5lqK1UC1SPS_p7qSmZD9MdhH99W6ph-LJubxzeHhhGEIuObsFUOyu0J12CWeMC3VCRjFLIRIgxOnRfk4mIezYMIpDxuWIvCyqqtlYZ7-xpNPQot9a5_pAa7tFT5e21QHpp-3e6dquYvqs66bVvrOFw0BtTdeNi-bo6JPu0FvtwgU5M0Pg5DfH5O3h_nX2GC1X88VsuowKSNIuAuSxRFEaATzdSMGM5AYkzyRTsSwSnSrFdSIVlLoElhpUJZQbTDiXWWkyGJPrQ2_rm48eQ5dXNhTonK6x6UM-NEnIQCTsH1TEkmWxSgd69Yfumt7XwyGDggEKme7VzUEVvgnBo8lbbyvtv3LO8v038uNvwA-mqnsf</recordid><startdate>20160101</startdate><enddate>20160101</enddate><creator>Xu, Li</creator><creator>Ke, Caixia</creator><creator>Huang, Ying</creator><creator>Yan, Yunjun</creator><general>MDPI AG</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>KB.</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>M7N</scope><orcidid>https://orcid.org/0000-0001-6643-597X</orcidid></search><sort><creationdate>20160101</creationdate><title>Immobilized Aspergillus niger Lipase with SiO2 Nanoparticles in Sol-Gel Materials</title><author>Xu, Li ; Ke, Caixia ; Huang, Ying ; Yan, Yunjun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c367t-3e125e4df4317b540f51f351850925c6a7991a6593dad307fe9d3dbe61158df83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Aspergillus niger</topic><topic>Catalysts</topic><topic>Chemical reactions</topic><topic>Enzymes</topic><topic>Lipase</topic><topic>Nanoparticles</topic><topic>Optimization</topic><topic>Polymerization</topic><topic>Silicon dioxide</topic><topic>Sol gel process</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xu, Li</creatorcontrib><creatorcontrib>Ke, Caixia</creatorcontrib><creatorcontrib>Huang, Ying</creatorcontrib><creatorcontrib>Yan, Yunjun</creatorcontrib><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>SciTech Premium Collection</collection><collection>Materials Research Database</collection><collection>Materials Science Database</collection><collection>Materials Science Collection</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Catalysts</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xu, Li</au><au>Ke, Caixia</au><au>Huang, Ying</au><au>Yan, Yunjun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immobilized Aspergillus niger Lipase with SiO2 Nanoparticles in Sol-Gel Materials</atitle><jtitle>Catalysts</jtitle><date>2016-01-01</date><risdate>2016</risdate><volume>6</volume><issue>10</issue><spage>149</spage><epage>149</epage><pages>149-149</pages><issn>2073-4344</issn><eissn>2073-4344</eissn><abstract>Lipase from Aspergillus niger was "doubly immobilized" with SiO2 nanoparticles in sol-gel powders prepared via the base-catalyzed polymerization of tetramethoxysilane (TMOS) and methyltreimethoxysilane (MTMS). The hydrolytic activity of the immobilized lipase was measured using the p-nitrophenyl palmitate hydrolysis method. The results showed that the optimum preparation conditions for the gels were made using a MTMS/TMOS molar ratio of 5, 60 mg of SiO2 nanoparticles, a water/silane molar ratio of 12, 120 mg of enzyme supply, and 120 mu L of PEG400. Under the optimal conditions, the immobilized lipase retained 92% of the loading protein and 94% of the total enzyme activity. Characteristic tests indicated that the immobilized lipase exhibited much higher thermal and pH stability than its free form, which shows great potential for industrial applications.</abstract><cop>Basel</cop><pub>MDPI AG</pub><doi>10.3390/catal6100149</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0001-6643-597X</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MDPI - Multidisciplinary Digital Publishing Institute; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Aspergillus niger Catalysts Chemical reactions Enzymes Lipase Nanoparticles Optimization Polymerization Silicon dioxide Sol gel process |
| title | Immobilized Aspergillus niger Lipase with SiO2 Nanoparticles in Sol-Gel Materials |
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