Preparation and characterization of stable core/shell Fe3O4@Au decorated with an amine group for immobilization of lipase by covalent attachment
The self-assembly approach was used for amine decoration of core/shell Fe3O4@Au with 4-aminothiophenol. This structure was used for covalent immobilization of lipase using a Ugi 4-component reaction. The amine group on the structure and carboxylic group from lipase can react in the Ugi reaction and...
Gespeichert in:
| Veröffentlicht in: | RSC advances 2022-02, Vol.12 (10), p.5971-5977 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 5977 |
|---|---|
| container_issue | 10 |
| container_start_page | 5971 |
| container_title | RSC advances |
| container_volume | 12 |
| creator | Aghamolaei, Marziyeh Landarani-Isfahani, Amir Bahadori, Mehrnaz Zahra Zamani Nori Rezaei, Saghar Moghadam, Majid Tangestaninejad, Shahram Mirkhani, Valiollah Mohammadpoor-Baltork, Iraj |
| description | The self-assembly approach was used for amine decoration of core/shell Fe3O4@Au with 4-aminothiophenol. This structure was used for covalent immobilization of lipase using a Ugi 4-component reaction. The amine group on the structure and carboxylic group from lipase can react in the Ugi reaction and a firm and stable covalent bond is created between enzyme and support. The synthesized structure was fully characterized and its activity was explored in different situations. The results showed the pH and temperature stability of immobilized lipase compared to free lipase in a wide range of pH and temperature. Also after 60 days, it showed excellent activity while residual activity for the free enzyme was only 10%. The synthesized structure was conveniently separated using an external magnetic field and reused 6 times without losing the activity of the immobilized enzyme. |
| doi_str_mv | 10.1039/d1ra08147k |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8982027</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2635489925</sourcerecordid><originalsourceid>FETCH-LOGICAL-p307t-1d4b89a15ce36328aeed5bda064dab028684dae7dbd8795e252c4071ff103eb23</originalsourceid><addsrcrecordid>eNpdkctOxiAQhYmJUaNufAISN25-BQot3RiN8ZaY6ELXzVCmFm1LBarRp_CRJdGFOhuGMyffhAMhe5wdclbUR5YHYJrL6nmNbAkmy5VgZb1JdmN8YrlKxUXJN8hmoaSQStVb5PMu4AwBkvMThcnSts-3NmFwH9-i72hMYAakrQ94FHscBnqBxa08OV2oxaxCQkvfXOozgcLoJqSPwS8z7Xygbhy9ccMv3OBmiEjNeya-woBTopAStP2Y2x2y3sEQcffn3CYPF-f3Z1erm9vL67PTm9VcsCqtuJVG18BVi0VZCA2IVhkLrJQWDBO61LnByhqrq1qhUKKVrOJdl5NCI4ptcvzNnRczom3z6gBDMwc3QnhvPLjm72RyffPoXxtda8FElQEHP4DgXxaMqRldbHM4MKFfYiNy2qXWkrFs3f9nffJLmPLzsiv_ha5roYovjneOgQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2635489925</pqid></control><display><type>article</type><title>Preparation and characterization of stable core/shell Fe3O4@Au decorated with an amine group for immobilization of lipase by covalent attachment</title><source>DOAJ Directory of Open Access Journals</source><source>PubMed Central Open Access</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Aghamolaei, Marziyeh ; Landarani-Isfahani, Amir ; Bahadori, Mehrnaz ; Zahra Zamani Nori ; Rezaei, Saghar ; Moghadam, Majid ; Tangestaninejad, Shahram ; Mirkhani, Valiollah ; Mohammadpoor-Baltork, Iraj</creator><creatorcontrib>Aghamolaei, Marziyeh ; Landarani-Isfahani, Amir ; Bahadori, Mehrnaz ; Zahra Zamani Nori ; Rezaei, Saghar ; Moghadam, Majid ; Tangestaninejad, Shahram ; Mirkhani, Valiollah ; Mohammadpoor-Baltork, Iraj</creatorcontrib><description>The self-assembly approach was used for amine decoration of core/shell Fe3O4@Au with 4-aminothiophenol. This structure was used for covalent immobilization of lipase using a Ugi 4-component reaction. The amine group on the structure and carboxylic group from lipase can react in the Ugi reaction and a firm and stable covalent bond is created between enzyme and support. The synthesized structure was fully characterized and its activity was explored in different situations. The results showed the pH and temperature stability of immobilized lipase compared to free lipase in a wide range of pH and temperature. Also after 60 days, it showed excellent activity while residual activity for the free enzyme was only 10%. The synthesized structure was conveniently separated using an external magnetic field and reused 6 times without losing the activity of the immobilized enzyme.</description><identifier>EISSN: 2046-2069</identifier><identifier>DOI: 10.1039/d1ra08147k</identifier><identifier>PMID: 35424559</identifier><language>eng</language><publisher>Cambridge: Royal Society of Chemistry</publisher><subject>Chemistry ; Covalence ; Covalent bonds ; Enzymes ; Immobilization ; Iron oxides ; Lipase ; Self-assembly ; Synthesis</subject><ispartof>RSC advances, 2022-02, Vol.12 (10), p.5971-5977</ispartof><rights>Copyright Royal Society of Chemistry 2022</rights><rights>This journal is © The Royal Society of Chemistry 2022 The Royal Society of Chemistry</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8982027/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8982027/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,53791,53793</link.rule.ids></links><search><creatorcontrib>Aghamolaei, Marziyeh</creatorcontrib><creatorcontrib>Landarani-Isfahani, Amir</creatorcontrib><creatorcontrib>Bahadori, Mehrnaz</creatorcontrib><creatorcontrib>Zahra Zamani Nori</creatorcontrib><creatorcontrib>Rezaei, Saghar</creatorcontrib><creatorcontrib>Moghadam, Majid</creatorcontrib><creatorcontrib>Tangestaninejad, Shahram</creatorcontrib><creatorcontrib>Mirkhani, Valiollah</creatorcontrib><creatorcontrib>Mohammadpoor-Baltork, Iraj</creatorcontrib><title>Preparation and characterization of stable core/shell Fe3O4@Au decorated with an amine group for immobilization of lipase by covalent attachment</title><title>RSC advances</title><description>The self-assembly approach was used for amine decoration of core/shell Fe3O4@Au with 4-aminothiophenol. This structure was used for covalent immobilization of lipase using a Ugi 4-component reaction. The amine group on the structure and carboxylic group from lipase can react in the Ugi reaction and a firm and stable covalent bond is created between enzyme and support. The synthesized structure was fully characterized and its activity was explored in different situations. The results showed the pH and temperature stability of immobilized lipase compared to free lipase in a wide range of pH and temperature. Also after 60 days, it showed excellent activity while residual activity for the free enzyme was only 10%. The synthesized structure was conveniently separated using an external magnetic field and reused 6 times without losing the activity of the immobilized enzyme.</description><subject>Chemistry</subject><subject>Covalence</subject><subject>Covalent bonds</subject><subject>Enzymes</subject><subject>Immobilization</subject><subject>Iron oxides</subject><subject>Lipase</subject><subject>Self-assembly</subject><subject>Synthesis</subject><issn>2046-2069</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNpdkctOxiAQhYmJUaNufAISN25-BQot3RiN8ZaY6ELXzVCmFm1LBarRp_CRJdGFOhuGMyffhAMhe5wdclbUR5YHYJrL6nmNbAkmy5VgZb1JdmN8YrlKxUXJN8hmoaSQStVb5PMu4AwBkvMThcnSts-3NmFwH9-i72hMYAakrQ94FHscBnqBxa08OV2oxaxCQkvfXOozgcLoJqSPwS8z7Xygbhy9ccMv3OBmiEjNeya-woBTopAStP2Y2x2y3sEQcffn3CYPF-f3Z1erm9vL67PTm9VcsCqtuJVG18BVi0VZCA2IVhkLrJQWDBO61LnByhqrq1qhUKKVrOJdl5NCI4ptcvzNnRczom3z6gBDMwc3QnhvPLjm72RyffPoXxtda8FElQEHP4DgXxaMqRldbHM4MKFfYiNy2qXWkrFs3f9nffJLmPLzsiv_ha5roYovjneOgQ</recordid><startdate>20220216</startdate><enddate>20220216</enddate><creator>Aghamolaei, Marziyeh</creator><creator>Landarani-Isfahani, Amir</creator><creator>Bahadori, Mehrnaz</creator><creator>Zahra Zamani Nori</creator><creator>Rezaei, Saghar</creator><creator>Moghadam, Majid</creator><creator>Tangestaninejad, Shahram</creator><creator>Mirkhani, Valiollah</creator><creator>Mohammadpoor-Baltork, Iraj</creator><general>Royal Society of Chemistry</general><general>The Royal Society of Chemistry</general><scope>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20220216</creationdate><title>Preparation and characterization of stable core/shell Fe3O4@Au decorated with an amine group for immobilization of lipase by covalent attachment</title><author>Aghamolaei, Marziyeh ; Landarani-Isfahani, Amir ; Bahadori, Mehrnaz ; Zahra Zamani Nori ; Rezaei, Saghar ; Moghadam, Majid ; Tangestaninejad, Shahram ; Mirkhani, Valiollah ; Mohammadpoor-Baltork, Iraj</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p307t-1d4b89a15ce36328aeed5bda064dab028684dae7dbd8795e252c4071ff103eb23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Chemistry</topic><topic>Covalence</topic><topic>Covalent bonds</topic><topic>Enzymes</topic><topic>Immobilization</topic><topic>Iron oxides</topic><topic>Lipase</topic><topic>Self-assembly</topic><topic>Synthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Aghamolaei, Marziyeh</creatorcontrib><creatorcontrib>Landarani-Isfahani, Amir</creatorcontrib><creatorcontrib>Bahadori, Mehrnaz</creatorcontrib><creatorcontrib>Zahra Zamani Nori</creatorcontrib><creatorcontrib>Rezaei, Saghar</creatorcontrib><creatorcontrib>Moghadam, Majid</creatorcontrib><creatorcontrib>Tangestaninejad, Shahram</creatorcontrib><creatorcontrib>Mirkhani, Valiollah</creatorcontrib><creatorcontrib>Mohammadpoor-Baltork, Iraj</creatorcontrib><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>RSC advances</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Aghamolaei, Marziyeh</au><au>Landarani-Isfahani, Amir</au><au>Bahadori, Mehrnaz</au><au>Zahra Zamani Nori</au><au>Rezaei, Saghar</au><au>Moghadam, Majid</au><au>Tangestaninejad, Shahram</au><au>Mirkhani, Valiollah</au><au>Mohammadpoor-Baltork, Iraj</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation and characterization of stable core/shell Fe3O4@Au decorated with an amine group for immobilization of lipase by covalent attachment</atitle><jtitle>RSC advances</jtitle><date>2022-02-16</date><risdate>2022</risdate><volume>12</volume><issue>10</issue><spage>5971</spage><epage>5977</epage><pages>5971-5977</pages><eissn>2046-2069</eissn><abstract>The self-assembly approach was used for amine decoration of core/shell Fe3O4@Au with 4-aminothiophenol. This structure was used for covalent immobilization of lipase using a Ugi 4-component reaction. The amine group on the structure and carboxylic group from lipase can react in the Ugi reaction and a firm and stable covalent bond is created between enzyme and support. The synthesized structure was fully characterized and its activity was explored in different situations. The results showed the pH and temperature stability of immobilized lipase compared to free lipase in a wide range of pH and temperature. Also after 60 days, it showed excellent activity while residual activity for the free enzyme was only 10%. The synthesized structure was conveniently separated using an external magnetic field and reused 6 times without losing the activity of the immobilized enzyme.</abstract><cop>Cambridge</cop><pub>Royal Society of Chemistry</pub><pmid>35424559</pmid><doi>10.1039/d1ra08147k</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | EISSN: 2046-2069 |
| ispartof | RSC advances, 2022-02, Vol.12 (10), p.5971-5977 |
| issn | 2046-2069 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8982027 |
| source | DOAJ Directory of Open Access Journals; PubMed Central Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Chemistry Covalence Covalent bonds Enzymes Immobilization Iron oxides Lipase Self-assembly Synthesis |
| title | Preparation and characterization of stable core/shell Fe3O4@Au decorated with an amine group for immobilization of lipase by covalent attachment |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T21%3A25%3A30IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Preparation%20and%20characterization%20of%20stable%20core/shell%20Fe3O4@Au%20decorated%20with%20an%20amine%20group%20for%20immobilization%20of%20lipase%20by%20covalent%20attachment&rft.jtitle=RSC%20advances&rft.au=Aghamolaei,%20Marziyeh&rft.date=2022-02-16&rft.volume=12&rft.issue=10&rft.spage=5971&rft.epage=5977&rft.pages=5971-5977&rft.eissn=2046-2069&rft_id=info:doi/10.1039/d1ra08147k&rft_dat=%3Cproquest_pubme%3E2635489925%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2635489925&rft_id=info:pmid/35424559&rfr_iscdi=true |