Optimization of 1-glyceryl benzoate production by enzymatic transesterification in organic solvents
This work is focused on the evaluation of reaction parameters involved in the enzymatic production of 1-glyceryl benzoate, an intermediate substance to carvedilol and propranolol synthesis, catalyzed by Candida antarctica lipase in different organic solvents. To our knowledge, no related study on th...
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Veröffentlicht in: | Enzyme and microbial technology 2010-02, Vol.46 (2), p.107-112 |
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creator | Ceni, Giovana Lerin, Lindomar A. de Conto, Juliana Faccin Brancher, Cristiane Vendrusculo da Silva, Patrícia Costa Toniazzo, Geciane Treichel, Helen de Oliveira, Débora Oliveira, J. Vladimir Oestreicher, Enrique Guillermo Antunes, Octavio Augusto Ceva |
description | This work is focused on the evaluation of reaction parameters involved in the enzymatic production of 1-glyceryl benzoate, an intermediate substance to carvedilol and propranolol synthesis, catalyzed by
Candida antarctica lipase in different organic solvents. To our knowledge, no related study on this subject is available in the open literature. The main goals of the present investigation were to elucidate the relationship between relevant reaction variables and also to determine the optimum conditions for 1-glyceryl benzoate production. Results showed that the strategy adopted for the experimental design proved to be useful in maximizing the reaction conversion in 2-propanol as solvent with Novozym 435 as catalyst. The optimum conditions were found to be methyl benzoate to glycerol molar ratio of 1:1, stirring rate of 150
rpm, 50
°C, enzyme concentration of 10
wt% at 36
h of reaction, with a resulting conversion to 1-glyceryl benzoate of about 29%. Reaction kinetics of 1-glyceryl benzoate production demonstrated that very satisfactory conversions (∼40%) were achieved after 70
h of reaction. |
doi_str_mv | 10.1016/j.enzmictec.2009.09.011 |
format | Article |
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Candida antarctica lipase in different organic solvents. To our knowledge, no related study on this subject is available in the open literature. The main goals of the present investigation were to elucidate the relationship between relevant reaction variables and also to determine the optimum conditions for 1-glyceryl benzoate production. Results showed that the strategy adopted for the experimental design proved to be useful in maximizing the reaction conversion in 2-propanol as solvent with Novozym 435 as catalyst. The optimum conditions were found to be methyl benzoate to glycerol molar ratio of 1:1, stirring rate of 150
rpm, 50
°C, enzyme concentration of 10
wt% at 36
h of reaction, with a resulting conversion to 1-glyceryl benzoate of about 29%. Reaction kinetics of 1-glyceryl benzoate production demonstrated that very satisfactory conversions (∼40%) were achieved after 70
h of reaction.</description><identifier>ISSN: 0141-0229</identifier><identifier>EISSN: 1879-0909</identifier><identifier>DOI: 10.1016/j.enzmictec.2009.09.011</identifier><identifier>CODEN: EMTED2</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>1-Glyceryl benzoate ; Biological and medical sciences ; Biotechnology ; Candida antarctica ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Transesterification</subject><ispartof>Enzyme and microbial technology, 2010-02, Vol.46 (2), p.107-112</ispartof><rights>2009 Elsevier Inc.</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c376t-3c8c21338fc0118b2dfe1236073ac8c78c50ccdf2561a5650f3b6d33ad448d8a3</citedby><cites>FETCH-LOGICAL-c376t-3c8c21338fc0118b2dfe1236073ac8c78c50ccdf2561a5650f3b6d33ad448d8a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.enzmictec.2009.09.011$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22295653$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Ceni, Giovana</creatorcontrib><creatorcontrib>Lerin, Lindomar A.</creatorcontrib><creatorcontrib>de Conto, Juliana Faccin</creatorcontrib><creatorcontrib>Brancher, Cristiane Vendrusculo</creatorcontrib><creatorcontrib>da Silva, Patrícia Costa</creatorcontrib><creatorcontrib>Toniazzo, Geciane</creatorcontrib><creatorcontrib>Treichel, Helen</creatorcontrib><creatorcontrib>de Oliveira, Débora</creatorcontrib><creatorcontrib>Oliveira, J. Vladimir</creatorcontrib><creatorcontrib>Oestreicher, Enrique Guillermo</creatorcontrib><creatorcontrib>Antunes, Octavio Augusto Ceva</creatorcontrib><title>Optimization of 1-glyceryl benzoate production by enzymatic transesterification in organic solvents</title><title>Enzyme and microbial technology</title><description>This work is focused on the evaluation of reaction parameters involved in the enzymatic production of 1-glyceryl benzoate, an intermediate substance to carvedilol and propranolol synthesis, catalyzed by
Candida antarctica lipase in different organic solvents. To our knowledge, no related study on this subject is available in the open literature. The main goals of the present investigation were to elucidate the relationship between relevant reaction variables and also to determine the optimum conditions for 1-glyceryl benzoate production. Results showed that the strategy adopted for the experimental design proved to be useful in maximizing the reaction conversion in 2-propanol as solvent with Novozym 435 as catalyst. The optimum conditions were found to be methyl benzoate to glycerol molar ratio of 1:1, stirring rate of 150
rpm, 50
°C, enzyme concentration of 10
wt% at 36
h of reaction, with a resulting conversion to 1-glyceryl benzoate of about 29%. Reaction kinetics of 1-glyceryl benzoate production demonstrated that very satisfactory conversions (∼40%) were achieved after 70
h of reaction.</description><subject>1-Glyceryl benzoate</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Candida antarctica</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Transesterification</subject><issn>0141-0229</issn><issn>1879-0909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNqFkElLBDEQhYMoOC6_wb7orcdU0utRxA0EL3oOmeqKZOhlTDJC--utccSrUBCo-urVyxPiAuQSJFTX6yWNX4PHRLhUUrbLXQEciAU0dZvLVraHYiGhgFwq1R6LkxjXUnKjkAuBL5vkB_9lk5_GbHIZ5O_9jBTmPlux8GQTZZswdVv8IVZzxt15YB6zFOwYKSYK3nncS3hWCe925HGc-k8aUzwTR872kc5_31Pxdn_3evuYP788PN3ePOeo6yrlGhtUoHXjkP03K9U5AqUrWWvLo7rBUiJ2TpUV2LIqpdOrqtPadkXRdI3Vp-Jqr8t-P7bsyww-IvW9HWnaRqMAikqWBYP1HsQwxRjImU3wgw2zAWl2oZq1-QvV7EI1uwLgzcvfEzai7R0HgD7-rSsOmJ1p5m72HPF_Pz0FE9HTiNT5QJhMN_l_b30DxyGUMw</recordid><startdate>20100205</startdate><enddate>20100205</enddate><creator>Ceni, Giovana</creator><creator>Lerin, Lindomar A.</creator><creator>de Conto, Juliana Faccin</creator><creator>Brancher, Cristiane Vendrusculo</creator><creator>da Silva, Patrícia Costa</creator><creator>Toniazzo, Geciane</creator><creator>Treichel, Helen</creator><creator>de Oliveira, Débora</creator><creator>Oliveira, J. Vladimir</creator><creator>Oestreicher, Enrique Guillermo</creator><creator>Antunes, Octavio Augusto Ceva</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20100205</creationdate><title>Optimization of 1-glyceryl benzoate production by enzymatic transesterification in organic solvents</title><author>Ceni, Giovana ; Lerin, Lindomar A. ; de Conto, Juliana Faccin ; Brancher, Cristiane Vendrusculo ; da Silva, Patrícia Costa ; Toniazzo, Geciane ; Treichel, Helen ; de Oliveira, Débora ; Oliveira, J. Vladimir ; Oestreicher, Enrique Guillermo ; Antunes, Octavio Augusto Ceva</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c376t-3c8c21338fc0118b2dfe1236073ac8c78c50ccdf2561a5650f3b6d33ad448d8a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>1-Glyceryl benzoate</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Candida antarctica</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Transesterification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ceni, Giovana</creatorcontrib><creatorcontrib>Lerin, Lindomar A.</creatorcontrib><creatorcontrib>de Conto, Juliana Faccin</creatorcontrib><creatorcontrib>Brancher, Cristiane Vendrusculo</creatorcontrib><creatorcontrib>da Silva, Patrícia Costa</creatorcontrib><creatorcontrib>Toniazzo, Geciane</creatorcontrib><creatorcontrib>Treichel, Helen</creatorcontrib><creatorcontrib>de Oliveira, Débora</creatorcontrib><creatorcontrib>Oliveira, J. Vladimir</creatorcontrib><creatorcontrib>Oestreicher, Enrique Guillermo</creatorcontrib><creatorcontrib>Antunes, Octavio Augusto Ceva</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Enzyme and microbial technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ceni, Giovana</au><au>Lerin, Lindomar A.</au><au>de Conto, Juliana Faccin</au><au>Brancher, Cristiane Vendrusculo</au><au>da Silva, Patrícia Costa</au><au>Toniazzo, Geciane</au><au>Treichel, Helen</au><au>de Oliveira, Débora</au><au>Oliveira, J. Vladimir</au><au>Oestreicher, Enrique Guillermo</au><au>Antunes, Octavio Augusto Ceva</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Optimization of 1-glyceryl benzoate production by enzymatic transesterification in organic solvents</atitle><jtitle>Enzyme and microbial technology</jtitle><date>2010-02-05</date><risdate>2010</risdate><volume>46</volume><issue>2</issue><spage>107</spage><epage>112</epage><pages>107-112</pages><issn>0141-0229</issn><eissn>1879-0909</eissn><coden>EMTED2</coden><abstract>This work is focused on the evaluation of reaction parameters involved in the enzymatic production of 1-glyceryl benzoate, an intermediate substance to carvedilol and propranolol synthesis, catalyzed by
Candida antarctica lipase in different organic solvents. To our knowledge, no related study on this subject is available in the open literature. The main goals of the present investigation were to elucidate the relationship between relevant reaction variables and also to determine the optimum conditions for 1-glyceryl benzoate production. Results showed that the strategy adopted for the experimental design proved to be useful in maximizing the reaction conversion in 2-propanol as solvent with Novozym 435 as catalyst. The optimum conditions were found to be methyl benzoate to glycerol molar ratio of 1:1, stirring rate of 150
rpm, 50
°C, enzyme concentration of 10
wt% at 36
h of reaction, with a resulting conversion to 1-glyceryl benzoate of about 29%. Reaction kinetics of 1-glyceryl benzoate production demonstrated that very satisfactory conversions (∼40%) were achieved after 70
h of reaction.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><doi>10.1016/j.enzmictec.2009.09.011</doi><tpages>6</tpages></addata></record> |
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subjects | 1-Glyceryl benzoate Biological and medical sciences Biotechnology Candida antarctica Fundamental and applied biological sciences. Psychology Kinetics Transesterification |
title | Optimization of 1-glyceryl benzoate production by enzymatic transesterification in organic solvents |
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