Exploiting the pressure effect on lipase-catalyzed wax ester synthesis in dense carbon dioxide
The present work focuses on the thermodynamic interpretation of the lauryl oleate biosynthesis in high‐pressure carbon dioxide. Lipase‐catalyzed lauryl oleate production by oleic acid esterification with 1‐dodecanol over immobilized lipase from Rhizomucor miehei (Lipozyme RM IM) was successfully per...
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Veröffentlicht in: | Biotechnology and bioengineering 2007-08, Vol.97 (6), p.1366-1375 |
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description | The present work focuses on the thermodynamic interpretation of the lauryl oleate biosynthesis in high‐pressure carbon dioxide. Lipase‐catalyzed lauryl oleate production by oleic acid esterification with 1‐dodecanol over immobilized lipase from Rhizomucor miehei (Lipozyme RM IM) was successfully performed in a sapphire window batch stirred tank reactor (BSTR) using dense CO2 as reaction medium. The experiments were planned to elucidate the pressure effect on the reaction performance. With increasing the pressure up to 10 MPa, the catalytic efficiency of the studied enzyme improved rising up to a maximum and decreased at higher pressure values. Kinetic observations, exhibiting that dense CO2 expanded reaction mixture in subcritical conditions led to higher performance than when diluted in a single supercritical phase, were elucidated by phase‐equilibrium arguments. The experimental results were justified with emphasis on thermodynamic interpretation of the studied system. Particularly, the different reaction performances obtained were related to the position of the operating point with respect to the location of liquid–vapor phase boundaries of the reactant fatty acid/alcohol/CO2 ternary system. The outlook for exploitation of CO2 expanded phase at lower pressure compared to supercritical phase, with heterogeneous system in which the solid catalyst particles are exposed to dense CO2 expanded reaction mixture, in developing new biotransformation schemes is promising. Biotechnol. Bioneg. 2007;97: 1366–1375. © 2007 Wiley Periodicals, Inc. |
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Lipase‐catalyzed lauryl oleate production by oleic acid esterification with 1‐dodecanol over immobilized lipase from Rhizomucor miehei (Lipozyme RM IM) was successfully performed in a sapphire window batch stirred tank reactor (BSTR) using dense CO2 as reaction medium. The experiments were planned to elucidate the pressure effect on the reaction performance. With increasing the pressure up to 10 MPa, the catalytic efficiency of the studied enzyme improved rising up to a maximum and decreased at higher pressure values. Kinetic observations, exhibiting that dense CO2 expanded reaction mixture in subcritical conditions led to higher performance than when diluted in a single supercritical phase, were elucidated by phase‐equilibrium arguments. The experimental results were justified with emphasis on thermodynamic interpretation of the studied system. Particularly, the different reaction performances obtained were related to the position of the operating point with respect to the location of liquid–vapor phase boundaries of the reactant fatty acid/alcohol/CO2 ternary system. The outlook for exploitation of CO2 expanded phase at lower pressure compared to supercritical phase, with heterogeneous system in which the solid catalyst particles are exposed to dense CO2 expanded reaction mixture, in developing new biotransformation schemes is promising. Biotechnol. Bioneg. 2007;97: 1366–1375. © 2007 Wiley Periodicals, Inc.</description><identifier>ISSN: 0006-3592</identifier><identifier>EISSN: 1097-0290</identifier><identifier>DOI: 10.1002/bit.21331</identifier><identifier>PMID: 17221889</identifier><identifier>CODEN: BIBIAU</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>biocatalysis ; Biochemistry ; Biological and medical sciences ; Biotechnology ; Carbon dioxide ; Carbon Dioxide - chemistry ; Catalysis ; Chemical synthesis ; CO2 expanded reaction media ; Computer Simulation ; dense carbon dioxide ; Dodecanol - chemistry ; Enzyme Activation ; Enzymes ; Enzymes, Immobilized - chemistry ; Esterification ; Fundamental and applied biological sciences. Psychology ; Lipase - chemistry ; Lipozyme RM IM ; Models, Chemical ; Oleic Acid - chemistry ; Pressure ; Rhizomucor - enzymology ; Rhizomucor miehei ; Thermodynamics ; wax ester</subject><ispartof>Biotechnology and bioengineering, 2007-08, Vol.97 (6), p.1366-1375</ispartof><rights>Copyright © 2007 Wiley Periodicals, Inc.</rights><rights>2007 INIST-CNRS</rights><rights>(c) 2007 Wiley Periodicals, Inc.</rights><rights>Copyright John Wiley and Sons, Limited Aug 15, 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4801-8ca5c5354aa885381d2f718a76c8d55978d1fd4ac583e04128f446c8950aa8f33</citedby><cites>FETCH-LOGICAL-c4801-8ca5c5354aa885381d2f718a76c8d55978d1fd4ac583e04128f446c8950aa8f33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbit.21331$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbit.21331$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18925487$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17221889$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Knez, Željko</creatorcontrib><creatorcontrib>Laudani, Chiara Giulia</creatorcontrib><creatorcontrib>Habulin, Maja</creatorcontrib><creatorcontrib>Reverchon, Ernesto</creatorcontrib><title>Exploiting the pressure effect on lipase-catalyzed wax ester synthesis in dense carbon dioxide</title><title>Biotechnology and bioengineering</title><addtitle>Biotechnol. Bioeng</addtitle><description>The present work focuses on the thermodynamic interpretation of the lauryl oleate biosynthesis in high‐pressure carbon dioxide. Lipase‐catalyzed lauryl oleate production by oleic acid esterification with 1‐dodecanol over immobilized lipase from Rhizomucor miehei (Lipozyme RM IM) was successfully performed in a sapphire window batch stirred tank reactor (BSTR) using dense CO2 as reaction medium. The experiments were planned to elucidate the pressure effect on the reaction performance. With increasing the pressure up to 10 MPa, the catalytic efficiency of the studied enzyme improved rising up to a maximum and decreased at higher pressure values. Kinetic observations, exhibiting that dense CO2 expanded reaction mixture in subcritical conditions led to higher performance than when diluted in a single supercritical phase, were elucidated by phase‐equilibrium arguments. The experimental results were justified with emphasis on thermodynamic interpretation of the studied system. Particularly, the different reaction performances obtained were related to the position of the operating point with respect to the location of liquid–vapor phase boundaries of the reactant fatty acid/alcohol/CO2 ternary system. The outlook for exploitation of CO2 expanded phase at lower pressure compared to supercritical phase, with heterogeneous system in which the solid catalyst particles are exposed to dense CO2 expanded reaction mixture, in developing new biotransformation schemes is promising. Biotechnol. Bioneg. 2007;97: 1366–1375. © 2007 Wiley Periodicals, Inc.</description><subject>biocatalysis</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Carbon dioxide</subject><subject>Carbon Dioxide - chemistry</subject><subject>Catalysis</subject><subject>Chemical synthesis</subject><subject>CO2 expanded reaction media</subject><subject>Computer Simulation</subject><subject>dense carbon dioxide</subject><subject>Dodecanol - chemistry</subject><subject>Enzyme Activation</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Esterification</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Lipase - chemistry</subject><subject>Lipozyme RM IM</subject><subject>Models, Chemical</subject><subject>Oleic Acid - chemistry</subject><subject>Pressure</subject><subject>Rhizomucor - enzymology</subject><subject>Rhizomucor miehei</subject><subject>Thermodynamics</subject><subject>wax ester</subject><issn>0006-3592</issn><issn>1097-0290</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV1rFDEUhoModq1e-AckCApeTJvvnLnUUtdCrTcVwQtDNnNGU2dnxmSG7vrrTd3VgiC9CiHPez7yEPKUsyPOmDhexelIcCn5PbLgrLYVEzW7TxaMMVNJXYsD8ijnq3K1YMxDcsCtEBygXpAvp5uxG-IU-690-oZ0TJjznJBi22KY6NDTLo4-YxX85LvtT2zotd9QzBMmmrd9CeWYaexpg31GGnxalVATh01s8DF50Pou45P9eUg-vj29PHlXnX9Ynp28Pq-CAsYrCF4HLbXyHkBL4I1oLQdvTYBG69pCw9tG-aBBIlNcQKtUeas1K4lWykPycld3TMOPuQzn1jEH7Drf4zBnZ5kxEhjcCcryZVwzeycomJQClCrg83_Aq2FOfdnWFSfWcG5NgV7toJCGnBO2bkxx7dPWceZuHLri0P12WNhn-4Lzao3NLbmXVoAXe8Dn4Ls2-T7EfMtBLbSCmxWOd9x17HD7_47uzdnln9bVLhGL3s3fhE_fnbHSavfpYunggr9fGsXdZ_kLgEfATw</recordid><startdate>20070815</startdate><enddate>20070815</enddate><creator>Knez, Željko</creator><creator>Laudani, Chiara Giulia</creator><creator>Habulin, Maja</creator><creator>Reverchon, Ernesto</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>IQODW</scope><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>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20070815</creationdate><title>Exploiting the pressure effect on lipase-catalyzed wax ester synthesis in dense carbon dioxide</title><author>Knez, Željko ; Laudani, Chiara Giulia ; Habulin, Maja ; Reverchon, Ernesto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4801-8ca5c5354aa885381d2f718a76c8d55978d1fd4ac583e04128f446c8950aa8f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>biocatalysis</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Carbon dioxide</topic><topic>Carbon Dioxide - chemistry</topic><topic>Catalysis</topic><topic>Chemical synthesis</topic><topic>CO2 expanded reaction media</topic><topic>Computer Simulation</topic><topic>dense carbon dioxide</topic><topic>Dodecanol - chemistry</topic><topic>Enzyme Activation</topic><topic>Enzymes</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Esterification</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Lipase - chemistry</topic><topic>Lipozyme RM IM</topic><topic>Models, Chemical</topic><topic>Oleic Acid - chemistry</topic><topic>Pressure</topic><topic>Rhizomucor - enzymology</topic><topic>Rhizomucor miehei</topic><topic>Thermodynamics</topic><topic>wax ester</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Knez, Željko</creatorcontrib><creatorcontrib>Laudani, Chiara Giulia</creatorcontrib><creatorcontrib>Habulin, Maja</creatorcontrib><creatorcontrib>Reverchon, Ernesto</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Knez, Željko</au><au>Laudani, Chiara Giulia</au><au>Habulin, Maja</au><au>Reverchon, Ernesto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Exploiting the pressure effect on lipase-catalyzed wax ester synthesis in dense carbon dioxide</atitle><jtitle>Biotechnology and bioengineering</jtitle><addtitle>Biotechnol. Bioeng</addtitle><date>2007-08-15</date><risdate>2007</risdate><volume>97</volume><issue>6</issue><spage>1366</spage><epage>1375</epage><pages>1366-1375</pages><issn>0006-3592</issn><eissn>1097-0290</eissn><coden>BIBIAU</coden><abstract>The present work focuses on the thermodynamic interpretation of the lauryl oleate biosynthesis in high‐pressure carbon dioxide. Lipase‐catalyzed lauryl oleate production by oleic acid esterification with 1‐dodecanol over immobilized lipase from Rhizomucor miehei (Lipozyme RM IM) was successfully performed in a sapphire window batch stirred tank reactor (BSTR) using dense CO2 as reaction medium. The experiments were planned to elucidate the pressure effect on the reaction performance. With increasing the pressure up to 10 MPa, the catalytic efficiency of the studied enzyme improved rising up to a maximum and decreased at higher pressure values. Kinetic observations, exhibiting that dense CO2 expanded reaction mixture in subcritical conditions led to higher performance than when diluted in a single supercritical phase, were elucidated by phase‐equilibrium arguments. The experimental results were justified with emphasis on thermodynamic interpretation of the studied system. Particularly, the different reaction performances obtained were related to the position of the operating point with respect to the location of liquid–vapor phase boundaries of the reactant fatty acid/alcohol/CO2 ternary system. The outlook for exploitation of CO2 expanded phase at lower pressure compared to supercritical phase, with heterogeneous system in which the solid catalyst particles are exposed to dense CO2 expanded reaction mixture, in developing new biotransformation schemes is promising. Biotechnol. Bioneg. 2007;97: 1366–1375. © 2007 Wiley Periodicals, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>17221889</pmid><doi>10.1002/bit.21331</doi><tpages>10</tpages></addata></record> |
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subjects | biocatalysis Biochemistry Biological and medical sciences Biotechnology Carbon dioxide Carbon Dioxide - chemistry Catalysis Chemical synthesis CO2 expanded reaction media Computer Simulation dense carbon dioxide Dodecanol - chemistry Enzyme Activation Enzymes Enzymes, Immobilized - chemistry Esterification Fundamental and applied biological sciences. Psychology Lipase - chemistry Lipozyme RM IM Models, Chemical Oleic Acid - chemistry Pressure Rhizomucor - enzymology Rhizomucor miehei Thermodynamics wax ester |
title | Exploiting the pressure effect on lipase-catalyzed wax ester synthesis in dense carbon dioxide |
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