Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles
We report a method of glycosylated enzymes' surface immobilisation and stabilisation. The enzyme is immobilised at the surface of silica nanoparticles through the reversible covalent binding of vicinal diols of the enzyme glycans with a surface-attached boronate derivative. A soft organosilica...
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Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2021-11, Vol.57 (9), p.1196-11963 |
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creator | Nazemi, Seyed Amirabbas Olesi ska, Magdalena Pezzella, Cinzia Varriale, Simona Lin, Chia-Wei Corvini, Philippe F.-X Shahgaldian, Patrick |
description | We report a method of glycosylated enzymes' surface immobilisation and stabilisation. The enzyme is immobilised at the surface of silica nanoparticles through the reversible covalent binding of vicinal diols of the enzyme glycans with a surface-attached boronate derivative. A soft organosilica layer of controlled thickness is grown at the silica surface, entrapping the enzyme and thus avoiding enzyme leaching. We demonstrate that this approach results not only in high and durable activity retention but also enzyme stabilisation.
We report a method of glycosylated enzyme immobilisation and stabilisation based on the formation of boronate esters between a surface-attached boronate and the enzyme glycans, followed by the growth of an organosilica layer of controlled thickness. |
doi_str_mv | 10.1039/d1cc04916j |
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We report a method of glycosylated enzyme immobilisation and stabilisation based on the formation of boronate esters between a surface-attached boronate and the enzyme glycans, followed by the growth of an organosilica layer of controlled thickness.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/d1cc04916j</identifier><language>eng</language><publisher>Cambridge: Royal Society of Chemistry</publisher><subject>Diols ; Enzymes ; Immobilization ; Leaching ; Nanoparticles ; Silicon dioxide ; Thickness</subject><ispartof>Chemical communications (Cambridge, England), 2021-11, Vol.57 (9), p.1196-11963</ispartof><rights>Copyright Royal Society of Chemistry 2021</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c314t-e5636f0ea8a2706f4e4b339dec33577cf215a5e15d2c0fe658f200ebad0d6b9f3</citedby><cites>FETCH-LOGICAL-c314t-e5636f0ea8a2706f4e4b339dec33577cf215a5e15d2c0fe658f200ebad0d6b9f3</cites><orcidid>0000-0002-1743-0387</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>Nazemi, Seyed Amirabbas</creatorcontrib><creatorcontrib>Olesi ska, Magdalena</creatorcontrib><creatorcontrib>Pezzella, Cinzia</creatorcontrib><creatorcontrib>Varriale, Simona</creatorcontrib><creatorcontrib>Lin, Chia-Wei</creatorcontrib><creatorcontrib>Corvini, Philippe F.-X</creatorcontrib><creatorcontrib>Shahgaldian, Patrick</creatorcontrib><title>Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles</title><title>Chemical communications (Cambridge, England)</title><description>We report a method of glycosylated enzymes' surface immobilisation and stabilisation. The enzyme is immobilised at the surface of silica nanoparticles through the reversible covalent binding of vicinal diols of the enzyme glycans with a surface-attached boronate derivative. A soft organosilica layer of controlled thickness is grown at the silica surface, entrapping the enzyme and thus avoiding enzyme leaching. We demonstrate that this approach results not only in high and durable activity retention but also enzyme stabilisation.
We report a method of glycosylated enzyme immobilisation and stabilisation based on the formation of boronate esters between a surface-attached boronate and the enzyme glycans, followed by the growth of an organosilica layer of controlled thickness.</description><subject>Diols</subject><subject>Enzymes</subject><subject>Immobilization</subject><subject>Leaching</subject><subject>Nanoparticles</subject><subject>Silicon dioxide</subject><subject>Thickness</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNpd0UtLxDAQAOAgCq6rF-9CwYsI1aR5tD1KfbPgRcFbSfOQLGmyJu2h_npTV1TMZYbkm4GZAHCM4AWCuL6USAhIasTWO2CBMCM5JdXr7pzTOi8xofvgIMY1TAfRagHsQ9_7zlgT-WC8y7iTWRz4nxuvszc7CR8nywclM-U-pl7FLD11PnhnRMaFkbkenZgLeKpMLKYOgmeOO7_hYTDCqngI9jS3UR19xyV4ub15bu7z1dPdQ3O1ygVGZMgVZZhpqHjFixIyTRTpMK6lEhjTshS6QJRThagsBNSK0UoXEKqOSyhZV2u8BGfbvpvg30cVh7Y3UShruVN-jG1BqzLNj0iR6Ok_uvZjSEPMqmYQ1mVRJXW-VSL4GIPS7SaYnoepRbCdF99eo6b5WvxjwidbHKL4cb8fgz8BBT2CHA</recordid><startdate>20211111</startdate><enddate>20211111</enddate><creator>Nazemi, Seyed Amirabbas</creator><creator>Olesi ska, Magdalena</creator><creator>Pezzella, Cinzia</creator><creator>Varriale, Simona</creator><creator>Lin, Chia-Wei</creator><creator>Corvini, Philippe F.-X</creator><creator>Shahgaldian, Patrick</creator><general>Royal Society of Chemistry</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-1743-0387</orcidid></search><sort><creationdate>20211111</creationdate><title>Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles</title><author>Nazemi, Seyed Amirabbas ; Olesi ska, Magdalena ; Pezzella, Cinzia ; Varriale, Simona ; Lin, Chia-Wei ; Corvini, Philippe F.-X ; Shahgaldian, Patrick</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c314t-e5636f0ea8a2706f4e4b339dec33577cf215a5e15d2c0fe658f200ebad0d6b9f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Diols</topic><topic>Enzymes</topic><topic>Immobilization</topic><topic>Leaching</topic><topic>Nanoparticles</topic><topic>Silicon dioxide</topic><topic>Thickness</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nazemi, Seyed Amirabbas</creatorcontrib><creatorcontrib>Olesi ska, Magdalena</creatorcontrib><creatorcontrib>Pezzella, Cinzia</creatorcontrib><creatorcontrib>Varriale, Simona</creatorcontrib><creatorcontrib>Lin, Chia-Wei</creatorcontrib><creatorcontrib>Corvini, Philippe F.-X</creatorcontrib><creatorcontrib>Shahgaldian, Patrick</creatorcontrib><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Chemical communications (Cambridge, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nazemi, Seyed Amirabbas</au><au>Olesi ska, Magdalena</au><au>Pezzella, Cinzia</au><au>Varriale, Simona</au><au>Lin, Chia-Wei</au><au>Corvini, Philippe F.-X</au><au>Shahgaldian, Patrick</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><date>2021-11-11</date><risdate>2021</risdate><volume>57</volume><issue>9</issue><spage>1196</spage><epage>11963</epage><pages>1196-11963</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>We report a method of glycosylated enzymes' surface immobilisation and stabilisation. The enzyme is immobilised at the surface of silica nanoparticles through the reversible covalent binding of vicinal diols of the enzyme glycans with a surface-attached boronate derivative. A soft organosilica layer of controlled thickness is grown at the silica surface, entrapping the enzyme and thus avoiding enzyme leaching. We demonstrate that this approach results not only in high and durable activity retention but also enzyme stabilisation.
We report a method of glycosylated enzyme immobilisation and stabilisation based on the formation of boronate esters between a surface-attached boronate and the enzyme glycans, followed by the growth of an organosilica layer of controlled thickness.</abstract><cop>Cambridge</cop><pub>Royal Society of Chemistry</pub><doi>10.1039/d1cc04916j</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0002-1743-0387</orcidid></addata></record> |
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source | Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
subjects | Diols Enzymes Immobilization Leaching Nanoparticles Silicon dioxide Thickness |
title | Immobilisation and stabilisation of glycosylated enzymes on boronic acid-functionalised silica nanoparticles |
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