An efficient system for catalyzing ester synthesis using a lipase from a newly isolated Burkholderia cepacia strain
The synthesis of ethyl-oleate by the lipase from the newly isolated strain Burkholderia cepacia LTEB11 in three different systems has been studied - immobilization on a hydrophobic support (Accurel EP 100®), encapsulation in reverse micelles, and direct addition of powdered free enzyme to the reacti...
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Veröffentlicht in: | Biocatalysis and biotransformation 2008, Vol.26 (3), p.197-203 |
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creator | Salum, T. F. C. Baron, A. M. Zago, E. Turra, V. Baratti, J. Mitchell, D. A. Krieger, N. |
description | The synthesis of ethyl-oleate by the lipase from the newly isolated strain Burkholderia cepacia LTEB11 in three different systems has been studied - immobilization on a hydrophobic support (Accurel EP 100®), encapsulation in reverse micelles, and direct addition of powdered free enzyme to the reaction medium. The immobilized enzyme performed best, giving a 70% ester yield in 10 h, this yield being five-fold greater than that obtained for reversed micelles, and two and a half times greater than that obtained for direct addition. An increase in the amount of immobilized enzyme preparation added gave a 100% ester yield in 3 h. The immobilized preparation was quite stable, giving a 100% yield of ethyl-oleate during 11 repeated reactions, and 50% yield after 24 reactions. These results suggest that the lipase of our strain of B. cepacia LTEB11 immobilized on Accurel has good potential for application in biocatalysis in organic media. |
doi_str_mv | 10.1080/10242420701568674 |
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The immobilized preparation was quite stable, giving a 100% yield of ethyl-oleate during 11 repeated reactions, and 50% yield after 24 reactions. These results suggest that the lipase of our strain of B. cepacia LTEB11 immobilized on Accurel has good potential for application in biocatalysis in organic media.</description><identifier>ISSN: 1024-2422</identifier><identifier>EISSN: 1029-2446</identifier><identifier>DOI: 10.1080/10242420701568674</identifier><language>eng</language><publisher>Abingdon: Informa UK Ltd</publisher><subject>Biocatalysis in organic media ; Bioconversions. Hemisynthesis ; Biological and medical sciences ; Biotechnology ; Burkholderia cepacia ; Fundamental and applied biological sciences. Psychology ; immobilization ; lipases ; Methods. Procedures. 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F. C.</creatorcontrib><creatorcontrib>Baron, A. M.</creatorcontrib><creatorcontrib>Zago, E.</creatorcontrib><creatorcontrib>Turra, V.</creatorcontrib><creatorcontrib>Baratti, J.</creatorcontrib><creatorcontrib>Mitchell, D. A.</creatorcontrib><creatorcontrib>Krieger, N.</creatorcontrib><title>An efficient system for catalyzing ester synthesis using a lipase from a newly isolated Burkholderia cepacia strain</title><title>Biocatalysis and biotransformation</title><description>The synthesis of ethyl-oleate by the lipase from the newly isolated strain Burkholderia cepacia LTEB11 in three different systems has been studied - immobilization on a hydrophobic support (Accurel EP 100®), encapsulation in reverse micelles, and direct addition of powdered free enzyme to the reaction medium. The immobilized enzyme performed best, giving a 70% ester yield in 10 h, this yield being five-fold greater than that obtained for reversed micelles, and two and a half times greater than that obtained for direct addition. An increase in the amount of immobilized enzyme preparation added gave a 100% ester yield in 3 h. The immobilized preparation was quite stable, giving a 100% yield of ethyl-oleate during 11 repeated reactions, and 50% yield after 24 reactions. These results suggest that the lipase of our strain of B. cepacia LTEB11 immobilized on Accurel has good potential for application in biocatalysis in organic media.</description><subject>Biocatalysis in organic media</subject><subject>Bioconversions. Hemisynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Burkholderia cepacia</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>immobilization</subject><subject>lipases</subject><subject>Methods. Procedures. Technologies</subject><issn>1024-2422</issn><issn>1029-2446</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNp9kE1LAzEQhhdRsFZ_gLdcPK5Ost_opRa_oOBFz8tsNnFTs9mSpJT115taFUQoOczkzTyTmTeKzilcUijhigJLw4ECaJaXeZEeRJOgVTFL0_zwK09DzthxdOLcEoAmrComkZsZIqRUXAnjiRudFz2RgyUcPerxQ5k3IoJow5vxnXDKkbXbqki0WqETRNqhDzcjNnokyg0avWjJ7dq-d4NuhVVIuFghD9F5i8qcRkcStRNn33Eavd7fvcwf48Xzw9N8toh5UoKPJWZtxrOCJQU0TUOTKilL2pZtyUXbImIjRQ4yB6QFsLwCzjiknMm84CxFnkwjuuvL7eCcFbJeWdWjHWsK9da1-p9rgbnYMWE1jlpaNFy5X5BBktMqLUPdza5OmeBWj5vB6rb2OOrB_kDJvm-u_-CdQO07jlbUy2FtTbBlz5CfiG2UUA</recordid><startdate>2008</startdate><enddate>2008</enddate><creator>Salum, T. F. C.</creator><creator>Baron, A. M.</creator><creator>Zago, E.</creator><creator>Turra, V.</creator><creator>Baratti, J.</creator><creator>Mitchell, D. 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Hemisynthesis</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Burkholderia cepacia</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>immobilization</topic><topic>lipases</topic><topic>Methods. Procedures. Technologies</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Salum, T. F. C.</creatorcontrib><creatorcontrib>Baron, A. M.</creatorcontrib><creatorcontrib>Zago, E.</creatorcontrib><creatorcontrib>Turra, V.</creatorcontrib><creatorcontrib>Baratti, J.</creatorcontrib><creatorcontrib>Mitchell, D. A.</creatorcontrib><creatorcontrib>Krieger, N.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Biocatalysis and biotransformation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Salum, T. F. C.</au><au>Baron, A. 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The immobilized enzyme performed best, giving a 70% ester yield in 10 h, this yield being five-fold greater than that obtained for reversed micelles, and two and a half times greater than that obtained for direct addition. An increase in the amount of immobilized enzyme preparation added gave a 100% ester yield in 3 h. The immobilized preparation was quite stable, giving a 100% yield of ethyl-oleate during 11 repeated reactions, and 50% yield after 24 reactions. These results suggest that the lipase of our strain of B. cepacia LTEB11 immobilized on Accurel has good potential for application in biocatalysis in organic media.</abstract><cop>Abingdon</cop><pub>Informa UK Ltd</pub><doi>10.1080/10242420701568674</doi><tpages>7</tpages></addata></record> |
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subjects | Biocatalysis in organic media Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology Burkholderia cepacia Fundamental and applied biological sciences. Psychology immobilization lipases Methods. Procedures. Technologies |
title | An efficient system for catalyzing ester synthesis using a lipase from a newly isolated Burkholderia cepacia strain |
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