Enzymatic Acylation of Flavonoids: Effect of the Nature of the Substrate, Origin of Lipase, and Operating Conditions on Conversion Yield and Regioselectivity
The conversion yield at equilibrium, the initial rate, and the regioselectivity of the enzymatic acetylation of aglycone flavonoids (quercetin, naringenin, hesperetin, and chrysin) were investigated and compared to those obtained with a glycosylated one (isoquercitrin). The effects of a wide range o...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2007-11, Vol.55 (23), p.9496-9502 |
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| creator | Chebil, Latifa Anthoni, Julie Humeau, Catherine Gerardin, Christine Engasser, Jean-Marc Ghoul, Mohamed |
| description | The conversion yield at equilibrium, the initial rate, and the regioselectivity of the enzymatic acetylation of aglycone flavonoids (quercetin, naringenin, hesperetin, and chrysin) were investigated and compared to those obtained with a glycosylated one (isoquercitrin). The effects of a wide range of operating conditions were quantified. Fourier transform infrared spectrometry (FT-IR), NMR, and high performance liquid chromatography electrospray ionization mass spectrometry (HPLC–ESI–MS) analyses showed that for glycosylated flavonoids, in the presence of Candida antarctica (CAL-B), the acetylation occurred on the 2″-OH, 3″-OH, and 6″-OH of the glucose part, while with Pseudomonas cepacea lipase (PSL-C) acetylation takes place on 6″-OH of the sugar and 4′-OH of the B-ring. For aglycone flavonoids, the acetylation occurred only with PSL-C on 4′-OH, 3′-OH, and 7-OH hydroxyls. The conversion yield and the number and the relative proportions of the synthesized products were found dependent on the nature of the enzyme, the molar ratio, and the flavonoid structure. The initial rate was affected only by the origin of the enzyme. |
| doi_str_mv | 10.1021/jf071943j |
| format | Article |
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The effects of a wide range of operating conditions were quantified. Fourier transform infrared spectrometry (FT-IR), NMR, and high performance liquid chromatography electrospray ionization mass spectrometry (HPLC–ESI–MS) analyses showed that for glycosylated flavonoids, in the presence of Candida antarctica (CAL-B), the acetylation occurred on the 2″-OH, 3″-OH, and 6″-OH of the glucose part, while with Pseudomonas cepacea lipase (PSL-C) acetylation takes place on 6″-OH of the sugar and 4′-OH of the B-ring. For aglycone flavonoids, the acetylation occurred only with PSL-C on 4′-OH, 3′-OH, and 7-OH hydroxyls. The conversion yield and the number and the relative proportions of the synthesized products were found dependent on the nature of the enzyme, the molar ratio, and the flavonoid structure. The initial rate was affected only by the origin of the enzyme.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf071943j</identifier><identifier>PMID: 17937478</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>acetylation ; Acylation ; Biological and medical sciences ; Biotechnology ; Burkholderia cepacia ; Burkholderia cepacia - enzymology ; Candida antarctica ; Candida antarcticalipase B ; Chemical and Process Engineering ; chemical structure ; chrysin ; Engineering Sciences ; enzyme activity ; Flavonoid ; flavonoids ; Flavonoids - chemistry ; Flavonoids - metabolism ; Food industries ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins ; Glycosylation ; hesperetin ; isoquercitrin ; Lipase - metabolism ; naringenin ; Pseudomonas ; Pseudomonas cepacialipase C ; regioselectivity ; Solvents ; Substrate Specificity ; triacylglycerol lipase</subject><ispartof>Journal of agricultural and food chemistry, 2007-11, Vol.55 (23), p.9496-9502</ispartof><rights>Copyright © 2007 American Chemical Society</rights><rights>2007 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a470t-70c85b74cc3f1b83140f8617b034e187999c3315a9509d911f0651dddf02ca8d3</citedby><cites>FETCH-LOGICAL-a470t-70c85b74cc3f1b83140f8617b034e187999c3315a9509d911f0651dddf02ca8d3</cites><orcidid>0000-0002-1089-201X ; 0000-0002-0133-5166</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf071943j$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf071943j$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,315,781,785,886,2766,27081,27929,27930,56743,56793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19241246$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17937478$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03535584$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Chebil, Latifa</creatorcontrib><creatorcontrib>Anthoni, Julie</creatorcontrib><creatorcontrib>Humeau, Catherine</creatorcontrib><creatorcontrib>Gerardin, Christine</creatorcontrib><creatorcontrib>Engasser, Jean-Marc</creatorcontrib><creatorcontrib>Ghoul, Mohamed</creatorcontrib><title>Enzymatic Acylation of Flavonoids: Effect of the Nature of the Substrate, Origin of Lipase, and Operating Conditions on Conversion Yield and Regioselectivity</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>The conversion yield at equilibrium, the initial rate, and the regioselectivity of the enzymatic acetylation of aglycone flavonoids (quercetin, naringenin, hesperetin, and chrysin) were investigated and compared to those obtained with a glycosylated one (isoquercitrin). The effects of a wide range of operating conditions were quantified. Fourier transform infrared spectrometry (FT-IR), NMR, and high performance liquid chromatography electrospray ionization mass spectrometry (HPLC–ESI–MS) analyses showed that for glycosylated flavonoids, in the presence of Candida antarctica (CAL-B), the acetylation occurred on the 2″-OH, 3″-OH, and 6″-OH of the glucose part, while with Pseudomonas cepacea lipase (PSL-C) acetylation takes place on 6″-OH of the sugar and 4′-OH of the B-ring. For aglycone flavonoids, the acetylation occurred only with PSL-C on 4′-OH, 3′-OH, and 7-OH hydroxyls. The conversion yield and the number and the relative proportions of the synthesized products were found dependent on the nature of the enzyme, the molar ratio, and the flavonoid structure. The initial rate was affected only by the origin of the enzyme.</description><subject>acetylation</subject><subject>Acylation</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Burkholderia cepacia</subject><subject>Burkholderia cepacia - enzymology</subject><subject>Candida antarctica</subject><subject>Candida antarcticalipase B</subject><subject>Chemical and Process Engineering</subject><subject>chemical structure</subject><subject>chrysin</subject><subject>Engineering Sciences</subject><subject>enzyme activity</subject><subject>Flavonoid</subject><subject>flavonoids</subject><subject>Flavonoids - chemistry</subject><subject>Flavonoids - metabolism</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins</subject><subject>Glycosylation</subject><subject>hesperetin</subject><subject>isoquercitrin</subject><subject>Lipase - metabolism</subject><subject>naringenin</subject><subject>Pseudomonas</subject><subject>Pseudomonas cepacialipase C</subject><subject>regioselectivity</subject><subject>Solvents</subject><subject>Substrate Specificity</subject><subject>triacylglycerol lipase</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFksGO0zAURSMEYsrAgh-AbEBCIuAXx7E9u6p0ZpAiiugMEivLdeyOSxoXO6ko_8K_4kxLu0FiZfu943tt3ZckzwG9A5TD-5VBFHiBVw-SEZAcZQSAPUxGKDYzRko4S56EsEIIMULR4-QMKMe0oGyU_J62v3Zr2VmVjtWuiRvXps6kl43cutbZOlykU2O06oZqd6fTT7Lrvf57mveL0HnZ6bfpzNulvb9c2Y0MsSLbOp1tdGzbdplOXFvbQT-k0SOettqHwe6b1U19D3_RS-uCbqKd3dpu9zR5ZGQT9LPDep7cXk5vJtdZNbv6OBlXmSwo6jKKFCMLWiiFDSwYhgIZVgJdIFxoYJRzrjAGIjlBvOYABpUE6ro2KFeS1fg8ebPXvZON2Hi7ln4nnLTielyJoYYwwYSwYguRfb1nN9796HXoxNoGpZtGttr1QZSsoJRF_n8gcMZxwdnJXXkXgtfm-ARAYghYHAOO7IuDaL9Y6_pEHhKNwKsDIIOSjfGyVTacOJ4XkBdl5LI9Z0Onfx770n8XJcWUiJvPc4HY1ytUTYj4EPmXe95IJ-TSR83beY4AD0MVxw2dnKUKYuV638bI_vGFP5s_0U8</recordid><startdate>20071114</startdate><enddate>20071114</enddate><creator>Chebil, Latifa</creator><creator>Anthoni, Julie</creator><creator>Humeau, Catherine</creator><creator>Gerardin, Christine</creator><creator>Engasser, Jean-Marc</creator><creator>Ghoul, Mohamed</creator><general>American Chemical Society</general><scope>FBQ</scope><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>7QL</scope><scope>C1K</scope><scope>M7N</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-1089-201X</orcidid><orcidid>https://orcid.org/0000-0002-0133-5166</orcidid></search><sort><creationdate>20071114</creationdate><title>Enzymatic Acylation of Flavonoids: Effect of the Nature of the Substrate, Origin of Lipase, and Operating Conditions on Conversion Yield and Regioselectivity</title><author>Chebil, Latifa ; Anthoni, Julie ; Humeau, Catherine ; Gerardin, Christine ; Engasser, Jean-Marc ; Ghoul, Mohamed</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a470t-70c85b74cc3f1b83140f8617b034e187999c3315a9509d911f0651dddf02ca8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>acetylation</topic><topic>Acylation</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Burkholderia cepacia</topic><topic>Burkholderia cepacia - enzymology</topic><topic>Candida antarctica</topic><topic>Candida antarcticalipase B</topic><topic>Chemical and Process Engineering</topic><topic>chemical structure</topic><topic>chrysin</topic><topic>Engineering Sciences</topic><topic>enzyme activity</topic><topic>Flavonoid</topic><topic>flavonoids</topic><topic>Flavonoids - chemistry</topic><topic>Flavonoids - metabolism</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins</topic><topic>Glycosylation</topic><topic>hesperetin</topic><topic>isoquercitrin</topic><topic>Lipase - metabolism</topic><topic>naringenin</topic><topic>Pseudomonas</topic><topic>Pseudomonas cepacialipase C</topic><topic>regioselectivity</topic><topic>Solvents</topic><topic>Substrate Specificity</topic><topic>triacylglycerol lipase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chebil, Latifa</creatorcontrib><creatorcontrib>Anthoni, Julie</creatorcontrib><creatorcontrib>Humeau, Catherine</creatorcontrib><creatorcontrib>Gerardin, Christine</creatorcontrib><creatorcontrib>Engasser, Jean-Marc</creatorcontrib><creatorcontrib>Ghoul, Mohamed</creatorcontrib><collection>AGRIS</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chebil, Latifa</au><au>Anthoni, Julie</au><au>Humeau, Catherine</au><au>Gerardin, Christine</au><au>Engasser, Jean-Marc</au><au>Ghoul, Mohamed</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymatic Acylation of Flavonoids: Effect of the Nature of the Substrate, Origin of Lipase, and Operating Conditions on Conversion Yield and Regioselectivity</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2007-11-14</date><risdate>2007</risdate><volume>55</volume><issue>23</issue><spage>9496</spage><epage>9502</epage><pages>9496-9502</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The conversion yield at equilibrium, the initial rate, and the regioselectivity of the enzymatic acetylation of aglycone flavonoids (quercetin, naringenin, hesperetin, and chrysin) were investigated and compared to those obtained with a glycosylated one (isoquercitrin). The effects of a wide range of operating conditions were quantified. Fourier transform infrared spectrometry (FT-IR), NMR, and high performance liquid chromatography electrospray ionization mass spectrometry (HPLC–ESI–MS) analyses showed that for glycosylated flavonoids, in the presence of Candida antarctica (CAL-B), the acetylation occurred on the 2″-OH, 3″-OH, and 6″-OH of the glucose part, while with Pseudomonas cepacea lipase (PSL-C) acetylation takes place on 6″-OH of the sugar and 4′-OH of the B-ring. For aglycone flavonoids, the acetylation occurred only with PSL-C on 4′-OH, 3′-OH, and 7-OH hydroxyls. The conversion yield and the number and the relative proportions of the synthesized products were found dependent on the nature of the enzyme, the molar ratio, and the flavonoid structure. The initial rate was affected only by the origin of the enzyme.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>17937478</pmid><doi>10.1021/jf071943j</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-1089-201X</orcidid><orcidid>https://orcid.org/0000-0002-0133-5166</orcidid></addata></record> |
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| subjects | acetylation Acylation Biological and medical sciences Biotechnology Burkholderia cepacia Burkholderia cepacia - enzymology Candida antarctica Candida antarcticalipase B Chemical and Process Engineering chemical structure chrysin Engineering Sciences enzyme activity Flavonoid flavonoids Flavonoids - chemistry Flavonoids - metabolism Food industries Fundamental and applied biological sciences. Psychology Fungal Proteins Glycosylation hesperetin isoquercitrin Lipase - metabolism naringenin Pseudomonas Pseudomonas cepacialipase C regioselectivity Solvents Substrate Specificity triacylglycerol lipase |
| title | Enzymatic Acylation of Flavonoids: Effect of the Nature of the Substrate, Origin of Lipase, and Operating Conditions on Conversion Yield and Regioselectivity |
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