Purification and characterization of a p-coumarate decarboxylase and a vinylphenol reductase from Brettanomyces bruxellensis
The presence of Brettanomyces bruxellensis has been correlated with an increase of phenolic aromas in wine. The production of these aromas results from the metabolization of cinnamic acids, present in the wine, to their ethyl derivatives. Hence, the participation of two enzymes has been proposed: a...
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| Veröffentlicht in: | International journal of food microbiology 2008-09, Vol.127 (1), p.6-11 |
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| container_title | International journal of food microbiology |
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| creator | Godoy, Liliana Martínez, Claudio Carrasco, Nelson Ganga, María Angélica |
| description | The presence of
Brettanomyces bruxellensis has been correlated with an increase of phenolic aromas in wine. The production of these aromas results from the metabolization of cinnamic acids, present in the wine, to their ethyl derivatives. Hence, the participation of two enzymes has been proposed: a
p-coumarate decarboxylase (CD) and a vinylphenol reductase (VR). Both enzymes were purified and characterized from
B. bruxellensis. In denaturing conditions, the CD enzyme had a molecular mass of 21 kDa, while in native conditions its mass was 41 kDa. The optimal activity was obtained at a temperature of 40 °C and a pH of 6.0. For
p-coumaric acid, the
K
m value and
V
max were 1.22
±
0.08 mM and 98
±
0.15 µmol/min mg, respectively. The VR enzyme had a molecular mass of 37 kDa in SDS-PAGE, while in natural conditions its mass was 118 kDa. The
K
m value was >
3.37
±
2.05 mM and its
V
max was 107.62
±
50.38 µmol/min mg for NADPH used as a cofactor. Both enzymatic activities were stable at pH 3.4, but in the presence of ethanol the CD activity decreased drastically while the VR activity was more stable. This is the first report that shows the presence of a CD and a VR enzyme in
B. bruxellensis. |
| doi_str_mv | 10.1016/j.ijfoodmicro.2008.05.011 |
| format | Article |
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Brettanomyces bruxellensis has been correlated with an increase of phenolic aromas in wine. The production of these aromas results from the metabolization of cinnamic acids, present in the wine, to their ethyl derivatives. Hence, the participation of two enzymes has been proposed: a
p-coumarate decarboxylase (CD) and a vinylphenol reductase (VR). Both enzymes were purified and characterized from
B. bruxellensis. In denaturing conditions, the CD enzyme had a molecular mass of 21 kDa, while in native conditions its mass was 41 kDa. The optimal activity was obtained at a temperature of 40 °C and a pH of 6.0. For
p-coumaric acid, the
K
m value and
V
max were 1.22
±
0.08 mM and 98
±
0.15 µmol/min mg, respectively. The VR enzyme had a molecular mass of 37 kDa in SDS-PAGE, while in natural conditions its mass was 118 kDa. The
K
m value was >
3.37
±
2.05 mM and its
V
max was 107.62
±
50.38 µmol/min mg for NADPH used as a cofactor. Both enzymatic activities were stable at pH 3.4, but in the presence of ethanol the CD activity decreased drastically while the VR activity was more stable. This is the first report that shows the presence of a CD and a VR enzyme in
B. bruxellensis.</description><identifier>ISSN: 0168-1605</identifier><identifier>EISSN: 1879-3460</identifier><identifier>DOI: 10.1016/j.ijfoodmicro.2008.05.011</identifier><identifier>PMID: 18571756</identifier><identifier>CODEN: IJFMDD</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Biological and medical sciences ; Brettanomyces ; Brettanomyces - enzymology ; Brettanomyces sp ; Carboxy-Lyases - isolation & purification ; Carboxy-Lyases - metabolism ; cinnamic acid ; Coumarate decarboxylase ; Electrophoresis, Polyacrylamide Gel ; enzyme activity ; enzymes ; Ethanol - pharmacology ; Fermented food industries ; flavor compounds ; flor yeasts ; Food industries ; Food Microbiology ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Kinetics ; Molecular Weight ; odor compounds ; Oxidoreductases - isolation & purification ; Oxidoreductases - metabolism ; p-coumaric acid ; phenolic acids ; Temperature ; Vinylphenol reductase ; Vitaceae ; volatile organic compounds ; Volatile phenols ; Wine ; Wine - microbiology ; wine quality ; winemaking ; wines ; Wines and vinegars</subject><ispartof>International journal of food microbiology, 2008-09, Vol.127 (1), p.6-11</ispartof><rights>2008 Elsevier B.V.</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-e1a93d95d7cca4da8f329aa2559c7d81eb0bb46de3c16de9679458812ccd0dd73</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0168160508002584$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20679417$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18571756$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Godoy, Liliana</creatorcontrib><creatorcontrib>Martínez, Claudio</creatorcontrib><creatorcontrib>Carrasco, Nelson</creatorcontrib><creatorcontrib>Ganga, María Angélica</creatorcontrib><title>Purification and characterization of a p-coumarate decarboxylase and a vinylphenol reductase from Brettanomyces bruxellensis</title><title>International journal of food microbiology</title><addtitle>Int J Food Microbiol</addtitle><description>The presence of
Brettanomyces bruxellensis has been correlated with an increase of phenolic aromas in wine. The production of these aromas results from the metabolization of cinnamic acids, present in the wine, to their ethyl derivatives. Hence, the participation of two enzymes has been proposed: a
p-coumarate decarboxylase (CD) and a vinylphenol reductase (VR). Both enzymes were purified and characterized from
B. bruxellensis. In denaturing conditions, the CD enzyme had a molecular mass of 21 kDa, while in native conditions its mass was 41 kDa. The optimal activity was obtained at a temperature of 40 °C and a pH of 6.0. For
p-coumaric acid, the
K
m value and
V
max were 1.22
±
0.08 mM and 98
±
0.15 µmol/min mg, respectively. The VR enzyme had a molecular mass of 37 kDa in SDS-PAGE, while in natural conditions its mass was 118 kDa. The
K
m value was >
3.37
±
2.05 mM and its
V
max was 107.62
±
50.38 µmol/min mg for NADPH used as a cofactor. Both enzymatic activities were stable at pH 3.4, but in the presence of ethanol the CD activity decreased drastically while the VR activity was more stable. This is the first report that shows the presence of a CD and a VR enzyme in
B. bruxellensis.</description><subject>Biological and medical sciences</subject><subject>Brettanomyces</subject><subject>Brettanomyces - enzymology</subject><subject>Brettanomyces sp</subject><subject>Carboxy-Lyases - isolation & purification</subject><subject>Carboxy-Lyases - metabolism</subject><subject>cinnamic acid</subject><subject>Coumarate decarboxylase</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>enzyme activity</subject><subject>enzymes</subject><subject>Ethanol - pharmacology</subject><subject>Fermented food industries</subject><subject>flavor compounds</subject><subject>flor yeasts</subject><subject>Food industries</subject><subject>Food Microbiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Molecular Weight</subject><subject>odor compounds</subject><subject>Oxidoreductases - isolation & purification</subject><subject>Oxidoreductases - metabolism</subject><subject>p-coumaric acid</subject><subject>phenolic acids</subject><subject>Temperature</subject><subject>Vinylphenol reductase</subject><subject>Vitaceae</subject><subject>volatile organic compounds</subject><subject>Volatile phenols</subject><subject>Wine</subject><subject>Wine - microbiology</subject><subject>wine quality</subject><subject>winemaking</subject><subject>wines</subject><subject>Wines and vinegars</subject><issn>0168-1605</issn><issn>1879-3460</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1v1DAQhi1ERZfCX4BwgFvCOFnn4wgrvqRKIEHP1mQ8oV4l8WInVbfix9chK8qRiy15ntd-_QjxSkImQZZv95ndd86ZwZJ3WQ5QZ6AykPKR2Mi6atJiW8JjsYlsncoS1Ll4GsIeAFRRwBNxLmtVyUqVG_H72-xtZwkn68YER5PQNXqkib29Ww9dl2BySMnNQ5xMnBgm9K27PfYY-E8Gkxs7HvvDNY-uTzybmaZl1nk3JO89TxOObjgSh6T18y33PY_BhmfirMM-8PPTfiGuPn74sfucXn799GX37jIllZdTyhKbwjTKVES4NVh3Rd4g5ko1VJlacgttuy0NFyTj2pRVs1V1LXMiA8ZUxYV4s9578O7XzGHSgw0UW-DIbg46l1ACyCaCzQpGryF47vTB2_jro5agF_V6r_9Rrxf1GpSO6mP2xemRuR3YPCRPriPw-gRgIOw7jyPZ8JfLYektl7YvV65Dp_Gnj8zV9xxkAVIVlapUJHYrwVHajWWvA1keiY31TJM2zv5H4XuVr7V1</recordid><startdate>20080930</startdate><enddate>20080930</enddate><creator>Godoy, Liliana</creator><creator>Martínez, Claudio</creator><creator>Carrasco, Nelson</creator><creator>Ganga, María Angélica</creator><general>Elsevier B.V</general><general>[Amsterdam; New York, NY]: Elsevier Science</general><general>Elsevier</general><scope>FBQ</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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20080930</creationdate><title>Purification and characterization of a p-coumarate decarboxylase and a vinylphenol reductase from Brettanomyces bruxellensis</title><author>Godoy, Liliana ; Martínez, Claudio ; Carrasco, Nelson ; Ganga, María Angélica</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-e1a93d95d7cca4da8f329aa2559c7d81eb0bb46de3c16de9679458812ccd0dd73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Biological and medical sciences</topic><topic>Brettanomyces</topic><topic>Brettanomyces - enzymology</topic><topic>Brettanomyces sp</topic><topic>Carboxy-Lyases - isolation & purification</topic><topic>Carboxy-Lyases - metabolism</topic><topic>cinnamic acid</topic><topic>Coumarate decarboxylase</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>enzyme activity</topic><topic>enzymes</topic><topic>Ethanol - pharmacology</topic><topic>Fermented food industries</topic><topic>flavor compounds</topic><topic>flor yeasts</topic><topic>Food industries</topic><topic>Food Microbiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Molecular Weight</topic><topic>odor compounds</topic><topic>Oxidoreductases - isolation & purification</topic><topic>Oxidoreductases - metabolism</topic><topic>p-coumaric acid</topic><topic>phenolic acids</topic><topic>Temperature</topic><topic>Vinylphenol reductase</topic><topic>Vitaceae</topic><topic>volatile organic compounds</topic><topic>Volatile phenols</topic><topic>Wine</topic><topic>Wine - microbiology</topic><topic>wine quality</topic><topic>winemaking</topic><topic>wines</topic><topic>Wines and vinegars</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Godoy, Liliana</creatorcontrib><creatorcontrib>Martínez, Claudio</creatorcontrib><creatorcontrib>Carrasco, Nelson</creatorcontrib><creatorcontrib>Ganga, María Angélica</creatorcontrib><collection>AGRIS</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>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>International journal of food microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Godoy, Liliana</au><au>Martínez, Claudio</au><au>Carrasco, Nelson</au><au>Ganga, María Angélica</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of a p-coumarate decarboxylase and a vinylphenol reductase from Brettanomyces bruxellensis</atitle><jtitle>International journal of food microbiology</jtitle><addtitle>Int J Food Microbiol</addtitle><date>2008-09-30</date><risdate>2008</risdate><volume>127</volume><issue>1</issue><spage>6</spage><epage>11</epage><pages>6-11</pages><issn>0168-1605</issn><eissn>1879-3460</eissn><coden>IJFMDD</coden><abstract>The presence of
Brettanomyces bruxellensis has been correlated with an increase of phenolic aromas in wine. The production of these aromas results from the metabolization of cinnamic acids, present in the wine, to their ethyl derivatives. Hence, the participation of two enzymes has been proposed: a
p-coumarate decarboxylase (CD) and a vinylphenol reductase (VR). Both enzymes were purified and characterized from
B. bruxellensis. In denaturing conditions, the CD enzyme had a molecular mass of 21 kDa, while in native conditions its mass was 41 kDa. The optimal activity was obtained at a temperature of 40 °C and a pH of 6.0. For
p-coumaric acid, the
K
m value and
V
max were 1.22
±
0.08 mM and 98
±
0.15 µmol/min mg, respectively. The VR enzyme had a molecular mass of 37 kDa in SDS-PAGE, while in natural conditions its mass was 118 kDa. The
K
m value was >
3.37
±
2.05 mM and its
V
max was 107.62
±
50.38 µmol/min mg for NADPH used as a cofactor. Both enzymatic activities were stable at pH 3.4, but in the presence of ethanol the CD activity decreased drastically while the VR activity was more stable. This is the first report that shows the presence of a CD and a VR enzyme in
B. bruxellensis.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>18571756</pmid><doi>10.1016/j.ijfoodmicro.2008.05.011</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0168-1605 |
| ispartof | International journal of food microbiology, 2008-09, Vol.127 (1), p.6-11 |
| issn | 0168-1605 1879-3460 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Biological and medical sciences Brettanomyces Brettanomyces - enzymology Brettanomyces sp Carboxy-Lyases - isolation & purification Carboxy-Lyases - metabolism cinnamic acid Coumarate decarboxylase Electrophoresis, Polyacrylamide Gel enzyme activity enzymes Ethanol - pharmacology Fermented food industries flavor compounds flor yeasts Food industries Food Microbiology Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Kinetics Molecular Weight odor compounds Oxidoreductases - isolation & purification Oxidoreductases - metabolism p-coumaric acid phenolic acids Temperature Vinylphenol reductase Vitaceae volatile organic compounds Volatile phenols Wine Wine - microbiology wine quality winemaking wines Wines and vinegars |
| title | Purification and characterization of a p-coumarate decarboxylase and a vinylphenol reductase from Brettanomyces bruxellensis |
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