Amidase encapsulated in TTAB reversed micelles for the study of transamidation reactions
Amidase, an amide hydrolase enzyme (E.C.3.5.1.4) with acyl transferase activity, was encapsulated in a reversed micellar system composed of the cationic surfactant tetradecyltrimethyl ammonium bromide (TTAB) in heptane/octanol (80/20%) and phosphate buffer at w0 11. The reaction used to study the ef...
Gespeichert in:
| Veröffentlicht in: | Biocatalysis and biotransformation 2005, Vol.23 (6), p.407-414 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 414 |
|---|---|
| container_issue | 6 |
| container_start_page | 407 |
| container_title | Biocatalysis and biotransformation |
| container_volume | 23 |
| creator | Pacheco, Rita Karmali, Amin Matos-Lopes, Manuel L. Serralheiro, Maria-Luisa |
| description | Amidase, an amide hydrolase enzyme (E.C.3.5.1.4) with acyl transferase activity, was encapsulated in a reversed micellar system composed of the cationic surfactant tetradecyltrimethyl ammonium bromide (TTAB) in heptane/octanol (80/20%) and phosphate buffer at w0 11. The reaction used to study the effect of the reversed micellar system on the enzyme behaviour was a transamidation reaction. The effect of surfactant concentration, buffer molarity and pH on the enzyme kinetics was evaluated. Both initial velocities and product yield were measured. The results indicated that a high initial velocity of hydroxamic acid synthesis and also the highest yield (98%) were obtained using the lowest pH value. The effect of TTAB concentration was dependent on the buffer molarity used. The effect of buffer molarity on reversed micelle dimensions was analysed by light scattering. These results showed that the buffer molarity had a strong influence on the reversed micelle radius that correlated with enzyme activity. |
| doi_str_mv | 10.1080/10242420500372419 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_17265680</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>17265680</sourcerecordid><originalsourceid>FETCH-LOGICAL-c411t-58f2f57d02dcc1dabe8d560192fa2a615aa4b026d23306b31d683070879636be3</originalsourceid><addsrcrecordid>eNp9kE9LxDAQxYsouK5-AG-56G11krRpi15W8R8IXlbwVmaTlO3SNmsmVfbbm3UVEUFyyGN4v5fJS5JjDmccCjjnINJ4IAOQuUh5uZOM4qyciDRVu586jVqI_eSAaAnApSjzUfIy7RqDZJntNa5oaDFYw5qezWbTK-btm_UUB12jbdtaYrXzLCwsozCYNXM1Cx57wk1IaFwfCdQbQYfJXo0t2aOve5w8397Mru8nj093D9fTx4lOOQ-TrKhFneUGhNGaG5zbwmQKeClqFKh4hpjOQSgjpAQ1l9yoQkIORV4qqeZWjpPTbe7Ku9fBUqi6hjbLYm_dQBXPhcpUAdHIt0btHZG3dbXyTYd-XXGoNh1WfzqMzMlXOJLGto5_1Q39gLlUioOKvsutr-ljQR2-O9-aKuC6df4bkv89c_ELX1hsw0Kjt9XSDb6P_f2z5AeihJXM</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17265680</pqid></control><display><type>article</type><title>Amidase encapsulated in TTAB reversed micelles for the study of transamidation reactions</title><source>Taylor & Francis Journals Complete</source><creator>Pacheco, Rita ; Karmali, Amin ; Matos-Lopes, Manuel L. ; Serralheiro, Maria-Luisa</creator><creatorcontrib>Pacheco, Rita ; Karmali, Amin ; Matos-Lopes, Manuel L. ; Serralheiro, Maria-Luisa</creatorcontrib><description>Amidase, an amide hydrolase enzyme (E.C.3.5.1.4) with acyl transferase activity, was encapsulated in a reversed micellar system composed of the cationic surfactant tetradecyltrimethyl ammonium bromide (TTAB) in heptane/octanol (80/20%) and phosphate buffer at w0 11. The reaction used to study the effect of the reversed micellar system on the enzyme behaviour was a transamidation reaction. The effect of surfactant concentration, buffer molarity and pH on the enzyme kinetics was evaluated. Both initial velocities and product yield were measured. The results indicated that a high initial velocity of hydroxamic acid synthesis and also the highest yield (98%) were obtained using the lowest pH value. The effect of TTAB concentration was dependent on the buffer molarity used. The effect of buffer molarity on reversed micelle dimensions was analysed by light scattering. These results showed that the buffer molarity had a strong influence on the reversed micelle radius that correlated with enzyme activity.</description><identifier>ISSN: 1024-2422</identifier><identifier>EISSN: 1029-2446</identifier><identifier>DOI: 10.1080/10242420500372419</identifier><language>eng</language><publisher>Abingdon: Informa UK Ltd</publisher><subject>Acetohydroxamic acid ; amidase ; Bioconversions. Hemisynthesis ; Biological and medical sciences ; Biotechnology ; cationic surfactant ; Fundamental and applied biological sciences. Psychology ; light scattering ; Methods. Procedures. Technologies ; reversed micelles</subject><ispartof>Biocatalysis and biotransformation, 2005, Vol.23 (6), p.407-414</ispartof><rights>2005 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 2005</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c411t-58f2f57d02dcc1dabe8d560192fa2a615aa4b026d23306b31d683070879636be3</citedby><cites>FETCH-LOGICAL-c411t-58f2f57d02dcc1dabe8d560192fa2a615aa4b026d23306b31d683070879636be3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.1080/10242420500372419$$EPDF$$P50$$Ginformaworld$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.1080/10242420500372419$$EHTML$$P50$$Ginformaworld$$H</linktohtml><link.rule.ids>314,780,784,4024,27923,27924,27925,59647,60436,61221,61402</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17366106$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Pacheco, Rita</creatorcontrib><creatorcontrib>Karmali, Amin</creatorcontrib><creatorcontrib>Matos-Lopes, Manuel L.</creatorcontrib><creatorcontrib>Serralheiro, Maria-Luisa</creatorcontrib><title>Amidase encapsulated in TTAB reversed micelles for the study of transamidation reactions</title><title>Biocatalysis and biotransformation</title><description>Amidase, an amide hydrolase enzyme (E.C.3.5.1.4) with acyl transferase activity, was encapsulated in a reversed micellar system composed of the cationic surfactant tetradecyltrimethyl ammonium bromide (TTAB) in heptane/octanol (80/20%) and phosphate buffer at w0 11. The reaction used to study the effect of the reversed micellar system on the enzyme behaviour was a transamidation reaction. The effect of surfactant concentration, buffer molarity and pH on the enzyme kinetics was evaluated. Both initial velocities and product yield were measured. The results indicated that a high initial velocity of hydroxamic acid synthesis and also the highest yield (98%) were obtained using the lowest pH value. The effect of TTAB concentration was dependent on the buffer molarity used. The effect of buffer molarity on reversed micelle dimensions was analysed by light scattering. These results showed that the buffer molarity had a strong influence on the reversed micelle radius that correlated with enzyme activity.</description><subject>Acetohydroxamic acid</subject><subject>amidase</subject><subject>Bioconversions. Hemisynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>cationic surfactant</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>light scattering</subject><subject>Methods. Procedures. Technologies</subject><subject>reversed micelles</subject><issn>1024-2422</issn><issn>1029-2446</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNp9kE9LxDAQxYsouK5-AG-56G11krRpi15W8R8IXlbwVmaTlO3SNmsmVfbbm3UVEUFyyGN4v5fJS5JjDmccCjjnINJ4IAOQuUh5uZOM4qyciDRVu586jVqI_eSAaAnApSjzUfIy7RqDZJntNa5oaDFYw5qezWbTK-btm_UUB12jbdtaYrXzLCwsozCYNXM1Cx57wk1IaFwfCdQbQYfJXo0t2aOve5w8397Mru8nj093D9fTx4lOOQ-TrKhFneUGhNGaG5zbwmQKeClqFKh4hpjOQSgjpAQ1l9yoQkIORV4qqeZWjpPTbe7Ku9fBUqi6hjbLYm_dQBXPhcpUAdHIt0btHZG3dbXyTYd-XXGoNh1WfzqMzMlXOJLGto5_1Q39gLlUioOKvsutr-ljQR2-O9-aKuC6df4bkv89c_ELX1hsw0Kjt9XSDb6P_f2z5AeihJXM</recordid><startdate>2005</startdate><enddate>2005</enddate><creator>Pacheco, Rita</creator><creator>Karmali, Amin</creator><creator>Matos-Lopes, Manuel L.</creator><creator>Serralheiro, Maria-Luisa</creator><general>Informa UK Ltd</general><general>Taylor & Francis</general><general>Taylor and Francis</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>2005</creationdate><title>Amidase encapsulated in TTAB reversed micelles for the study of transamidation reactions</title><author>Pacheco, Rita ; Karmali, Amin ; Matos-Lopes, Manuel L. ; Serralheiro, Maria-Luisa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c411t-58f2f57d02dcc1dabe8d560192fa2a615aa4b026d23306b31d683070879636be3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Acetohydroxamic acid</topic><topic>amidase</topic><topic>Bioconversions. Hemisynthesis</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>cationic surfactant</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>light scattering</topic><topic>Methods. Procedures. Technologies</topic><topic>reversed micelles</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pacheco, Rita</creatorcontrib><creatorcontrib>Karmali, Amin</creatorcontrib><creatorcontrib>Matos-Lopes, Manuel L.</creatorcontrib><creatorcontrib>Serralheiro, Maria-Luisa</creatorcontrib><collection>Pascal-Francis</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><jtitle>Biocatalysis and biotransformation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pacheco, Rita</au><au>Karmali, Amin</au><au>Matos-Lopes, Manuel L.</au><au>Serralheiro, Maria-Luisa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amidase encapsulated in TTAB reversed micelles for the study of transamidation reactions</atitle><jtitle>Biocatalysis and biotransformation</jtitle><date>2005</date><risdate>2005</risdate><volume>23</volume><issue>6</issue><spage>407</spage><epage>414</epage><pages>407-414</pages><issn>1024-2422</issn><eissn>1029-2446</eissn><abstract>Amidase, an amide hydrolase enzyme (E.C.3.5.1.4) with acyl transferase activity, was encapsulated in a reversed micellar system composed of the cationic surfactant tetradecyltrimethyl ammonium bromide (TTAB) in heptane/octanol (80/20%) and phosphate buffer at w0 11. The reaction used to study the effect of the reversed micellar system on the enzyme behaviour was a transamidation reaction. The effect of surfactant concentration, buffer molarity and pH on the enzyme kinetics was evaluated. Both initial velocities and product yield were measured. The results indicated that a high initial velocity of hydroxamic acid synthesis and also the highest yield (98%) were obtained using the lowest pH value. The effect of TTAB concentration was dependent on the buffer molarity used. The effect of buffer molarity on reversed micelle dimensions was analysed by light scattering. These results showed that the buffer molarity had a strong influence on the reversed micelle radius that correlated with enzyme activity.</abstract><cop>Abingdon</cop><pub>Informa UK Ltd</pub><doi>10.1080/10242420500372419</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1024-2422 |
| ispartof | Biocatalysis and biotransformation, 2005, Vol.23 (6), p.407-414 |
| issn | 1024-2422 1029-2446 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_17265680 |
| source | Taylor & Francis Journals Complete |
| subjects | Acetohydroxamic acid amidase Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology cationic surfactant Fundamental and applied biological sciences. Psychology light scattering Methods. Procedures. Technologies reversed micelles |
| title | Amidase encapsulated in TTAB reversed micelles for the study of transamidation reactions |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T20%3A25%3A28IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Amidase%20encapsulated%20in%20TTAB%20reversed%20micelles%20for%20the%20study%20of%20transamidation%20reactions&rft.jtitle=Biocatalysis%20and%20biotransformation&rft.au=Pacheco,%20Rita&rft.date=2005&rft.volume=23&rft.issue=6&rft.spage=407&rft.epage=414&rft.pages=407-414&rft.issn=1024-2422&rft.eissn=1029-2446&rft_id=info:doi/10.1080/10242420500372419&rft_dat=%3Cproquest_cross%3E17265680%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17265680&rft_id=info:pmid/&rfr_iscdi=true |