Dynamic light scattering of cutinase in AOT reverse micelles
The fungal lipolytic enzyme cutinase, incorporated into sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles has been investigated using dynamic light scattering. The reversed micelles form spontaneously when water is added to a solution of sodium bis-(2ethylhexyl) sulfosuccinate in isooctane....
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Veröffentlicht in: | Chemistry and physics of lipids 2000-08, Vol.106 (2), p.181-189 |
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description | The fungal lipolytic enzyme cutinase, incorporated into sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles has been investigated using dynamic light scattering. The reversed micelles form spontaneously when water is added to a solution of sodium bis-(2ethylhexyl) sulfosuccinate in isooctane. When an enzyme is previously dissolved in the water before its addition to the organic phase, the enzyme will be incorporated into the micelles. Enzyme encapsulation in reversed micelles can be advantageous namely to the conversion of water insoluble substrates and to carry out synthesis reactions. However protein unfolding occurs in several systems as for cutinase in sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles. Dynamic light scattering measurements of sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles with and without cutinase were taken at different water to surfactant ratios. The results indicate that cutinase was attached to the micellar wall and that might cause cutinase unfolding. The interactions between cutinase and the bis-(2ethylhexyl) sulfosuccinate interface are probably the driving force for cutinase unfolding at room temperature. Twenty-four hours after encapsulation, when cutinase is unfolded, a bimodal distribution was clearly observed. The radii of reversed micelles with unfolded cutinase were determined and found to be considerable larger than the radii of the empty reversed micelles. The majority of the reversed micelles were empty (90–96% of mass) and the remainder (4–10%) containing unfolded cutinase were larger by 26–89 Å. |
doi_str_mv | 10.1016/S0009-3084(00)00152-3 |
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The reversed micelles form spontaneously when water is added to a solution of sodium bis-(2ethylhexyl) sulfosuccinate in isooctane. When an enzyme is previously dissolved in the water before its addition to the organic phase, the enzyme will be incorporated into the micelles. Enzyme encapsulation in reversed micelles can be advantageous namely to the conversion of water insoluble substrates and to carry out synthesis reactions. However protein unfolding occurs in several systems as for cutinase in sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles. Dynamic light scattering measurements of sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles with and without cutinase were taken at different water to surfactant ratios. The results indicate that cutinase was attached to the micellar wall and that might cause cutinase unfolding. The interactions between cutinase and the bis-(2ethylhexyl) sulfosuccinate interface are probably the driving force for cutinase unfolding at room temperature. Twenty-four hours after encapsulation, when cutinase is unfolded, a bimodal distribution was clearly observed. The radii of reversed micelles with unfolded cutinase were determined and found to be considerable larger than the radii of the empty reversed micelles. The majority of the reversed micelles were empty (90–96% of mass) and the remainder (4–10%) containing unfolded cutinase were larger by 26–89 Å.</description><identifier>ISSN: 0009-3084</identifier><identifier>EISSN: 1873-2941</identifier><identifier>DOI: 10.1016/S0009-3084(00)00152-3</identifier><identifier>PMID: 10930568</identifier><language>eng</language><publisher>Ireland: Elsevier Ireland Ltd</publisher><subject>Carboxylic Ester Hydrolases - chemistry ; Cutinase unfolding ; Dioctyl Sulfosuccinic Acid ; Dynamic light scattering ; Light ; Micelles ; Reversed micelles ; Scattering, Radiation</subject><ispartof>Chemistry and physics of lipids, 2000-08, Vol.106 (2), p.181-189</ispartof><rights>2000 Elsevier Science Ireland Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c361t-6fb488ff416f64dbe11306fed0a81a2bce8df32d2f0627a83c8663c2bcf0f62b3</citedby><cites>FETCH-LOGICAL-c361t-6fb488ff416f64dbe11306fed0a81a2bce8df32d2f0627a83c8663c2bcf0f62b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0009-3084(00)00152-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10930568$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Melo, E.P.</creatorcontrib><creatorcontrib>Fojan, P.</creatorcontrib><creatorcontrib>Cabral, J.M.S.</creatorcontrib><creatorcontrib>Petersen, S.B.</creatorcontrib><title>Dynamic light scattering of cutinase in AOT reverse micelles</title><title>Chemistry and physics of lipids</title><addtitle>Chem Phys Lipids</addtitle><description>The fungal lipolytic enzyme cutinase, incorporated into sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles has been investigated using dynamic light scattering. The reversed micelles form spontaneously when water is added to a solution of sodium bis-(2ethylhexyl) sulfosuccinate in isooctane. When an enzyme is previously dissolved in the water before its addition to the organic phase, the enzyme will be incorporated into the micelles. Enzyme encapsulation in reversed micelles can be advantageous namely to the conversion of water insoluble substrates and to carry out synthesis reactions. However protein unfolding occurs in several systems as for cutinase in sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles. Dynamic light scattering measurements of sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles with and without cutinase were taken at different water to surfactant ratios. The results indicate that cutinase was attached to the micellar wall and that might cause cutinase unfolding. The interactions between cutinase and the bis-(2ethylhexyl) sulfosuccinate interface are probably the driving force for cutinase unfolding at room temperature. Twenty-four hours after encapsulation, when cutinase is unfolded, a bimodal distribution was clearly observed. The radii of reversed micelles with unfolded cutinase were determined and found to be considerable larger than the radii of the empty reversed micelles. The majority of the reversed micelles were empty (90–96% of mass) and the remainder (4–10%) containing unfolded cutinase were larger by 26–89 Å.</description><subject>Carboxylic Ester Hydrolases - chemistry</subject><subject>Cutinase unfolding</subject><subject>Dioctyl Sulfosuccinic Acid</subject><subject>Dynamic light scattering</subject><subject>Light</subject><subject>Micelles</subject><subject>Reversed micelles</subject><subject>Scattering, Radiation</subject><issn>0009-3084</issn><issn>1873-2941</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLw0AQgBdRbK3-BCUn0UN0NptsNiBIqU8o9GA9L5vNbF3JQ3eTQv-9aVPEm6dhmG9eHyHnFG4oUH77BgBZyEDEVwDXADSJQnZAxlSkLIyymB6S8S8yIifef_YpJAk9JiMKGYOEizG5e9jUqrI6KO3qow28Vm2LztaroDGB7lpbK4-BrYPpYhk4XKPr057HskR_So6MKj2e7eOEvD89Lmcv4Xzx_DqbzkPNOG1DbvJYCGNiyg2PixwpZcANFqAEVVGuURSGRUVkgEepEkwLzpnuCwYMj3I2IZfD3C_XfHfoW1lZvz1B1dh0XqY0jTKe8h5MBlC7xnuHRn45Wym3kRTkVpvcaZNbJxJA7rRJ1vdd7Bd0eYXFn67BUw_cDwD2b64tOum1xVpjYR3qVhaN_WfFD6BNfAU</recordid><startdate>20000801</startdate><enddate>20000801</enddate><creator>Melo, E.P.</creator><creator>Fojan, P.</creator><creator>Cabral, J.M.S.</creator><creator>Petersen, S.B.</creator><general>Elsevier Ireland Ltd</general><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>7X8</scope></search><sort><creationdate>20000801</creationdate><title>Dynamic light scattering of cutinase in AOT reverse micelles</title><author>Melo, E.P. ; Fojan, P. ; Cabral, J.M.S. ; Petersen, S.B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c361t-6fb488ff416f64dbe11306fed0a81a2bce8df32d2f0627a83c8663c2bcf0f62b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Carboxylic Ester Hydrolases - chemistry</topic><topic>Cutinase unfolding</topic><topic>Dioctyl Sulfosuccinic Acid</topic><topic>Dynamic light scattering</topic><topic>Light</topic><topic>Micelles</topic><topic>Reversed micelles</topic><topic>Scattering, Radiation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Melo, E.P.</creatorcontrib><creatorcontrib>Fojan, P.</creatorcontrib><creatorcontrib>Cabral, J.M.S.</creatorcontrib><creatorcontrib>Petersen, S.B.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Chemistry and physics of lipids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Melo, E.P.</au><au>Fojan, P.</au><au>Cabral, J.M.S.</au><au>Petersen, S.B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dynamic light scattering of cutinase in AOT reverse micelles</atitle><jtitle>Chemistry and physics of lipids</jtitle><addtitle>Chem Phys Lipids</addtitle><date>2000-08-01</date><risdate>2000</risdate><volume>106</volume><issue>2</issue><spage>181</spage><epage>189</epage><pages>181-189</pages><issn>0009-3084</issn><eissn>1873-2941</eissn><abstract>The fungal lipolytic enzyme cutinase, incorporated into sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles has been investigated using dynamic light scattering. The reversed micelles form spontaneously when water is added to a solution of sodium bis-(2ethylhexyl) sulfosuccinate in isooctane. When an enzyme is previously dissolved in the water before its addition to the organic phase, the enzyme will be incorporated into the micelles. Enzyme encapsulation in reversed micelles can be advantageous namely to the conversion of water insoluble substrates and to carry out synthesis reactions. However protein unfolding occurs in several systems as for cutinase in sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles. Dynamic light scattering measurements of sodium bis-(2ethylhexyl) sulfosuccinate reversed micelles with and without cutinase were taken at different water to surfactant ratios. The results indicate that cutinase was attached to the micellar wall and that might cause cutinase unfolding. The interactions between cutinase and the bis-(2ethylhexyl) sulfosuccinate interface are probably the driving force for cutinase unfolding at room temperature. Twenty-four hours after encapsulation, when cutinase is unfolded, a bimodal distribution was clearly observed. The radii of reversed micelles with unfolded cutinase were determined and found to be considerable larger than the radii of the empty reversed micelles. The majority of the reversed micelles were empty (90–96% of mass) and the remainder (4–10%) containing unfolded cutinase were larger by 26–89 Å.</abstract><cop>Ireland</cop><pub>Elsevier Ireland Ltd</pub><pmid>10930568</pmid><doi>10.1016/S0009-3084(00)00152-3</doi><tpages>9</tpages></addata></record> |
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subjects | Carboxylic Ester Hydrolases - chemistry Cutinase unfolding Dioctyl Sulfosuccinic Acid Dynamic light scattering Light Micelles Reversed micelles Scattering, Radiation |
title | Dynamic light scattering of cutinase in AOT reverse micelles |
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