Heterologous production of the Piromyces equi cinnamoyl esterase in Trichoderma reesei for biotechnological applications
Aims: The objective of the study was to produce and characterize the cinnamoyl esterase EstA from the anaerobic fungus Piromyces equi for potential industrial applications. Methods and Results: The catalytic domain EstA was produced in Trichoderma reesei. Because the two fungi displayed different...
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| Veröffentlicht in: | Letters in applied microbiology 2009-12, Vol.49 (6), p.673-678 |
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| creator | Poidevin, L. Levasseur, A. Paës, G. Navarro, D. Heiss‐Blanquet, S. Asther, M. Record, E. |
| description | Aims: The objective of the study was to produce and characterize the cinnamoyl esterase EstA from the anaerobic fungus Piromyces equi for potential industrial applications.
Methods and Results: The catalytic domain EstA was produced in Trichoderma reesei. Because the two fungi displayed different genome features, including different codon usage and GC content, a synthetic gene was designed and expressed, leading to the production of the corresponding protein at around 33 mg per litre in the T. reesei culture medium. After the recombinant protein was purified, biochemical characterization showed that EstA presents peak activity at pH 6·5 and at 50–60°C. Furthermore, EstA remained stable at pH 6–8 and below 50°C. EstA was compared to cinnamoyl esterases FaeA and FaeB from Aspergillus niger in terms of ferulic acid (FA) release from wheat bran (WB), maize bran (MB) and sugar beet pulp (SBP).
Conclusion: The synthetic gene was successfully cloned and overexpressed in T. reesei. EstA from P. equi was demonstrated to efficiently release FA from various natural substrates.
Significance and Impact of the Study: Recombinant EstA produced in an industrial enzyme producer, T. reesei, was biochemically characterized, and its capacity to release an aromatic compound (FA) for biotechnological applications was demonstrated. |
| doi_str_mv | 10.1111/j.1472-765X.2009.02734.x |
| format | Article |
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Methods and Results: The catalytic domain EstA was produced in Trichoderma reesei. Because the two fungi displayed different genome features, including different codon usage and GC content, a synthetic gene was designed and expressed, leading to the production of the corresponding protein at around 33 mg per litre in the T. reesei culture medium. After the recombinant protein was purified, biochemical characterization showed that EstA presents peak activity at pH 6·5 and at 50–60°C. Furthermore, EstA remained stable at pH 6–8 and below 50°C. EstA was compared to cinnamoyl esterases FaeA and FaeB from Aspergillus niger in terms of ferulic acid (FA) release from wheat bran (WB), maize bran (MB) and sugar beet pulp (SBP).
Conclusion: The synthetic gene was successfully cloned and overexpressed in T. reesei. EstA from P. equi was demonstrated to efficiently release FA from various natural substrates.
Significance and Impact of the Study: Recombinant EstA produced in an industrial enzyme producer, T. reesei, was biochemically characterized, and its capacity to release an aromatic compound (FA) for biotechnological applications was demonstrated.</description><identifier>ISSN: 0266-8254</identifier><identifier>EISSN: 1472-765X</identifier><identifier>DOI: 10.1111/j.1472-765X.2009.02734.x</identifier><identifier>PMID: 19780949</identifier><identifier>CODEN: LAMIE7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Aspergillus niger - enzymology ; Biological and medical sciences ; biotechnology ; Carboxylic Ester Hydrolases - genetics ; Carboxylic Ester Hydrolases - metabolism ; cinnamoyl esterase ; Cloning, Molecular ; Coumaric Acids - metabolism ; ferulic acid ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; heterologous production ; Hydrogen-Ion Concentration ; Industrial Microbiology ; Life Sciences ; Microbiology ; Microbiology and Parasitology ; Piromyces - enzymology ; Piromyces - genetics ; Piromyces equi ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Substrate Specificity ; Temperature ; Trichoderma - genetics ; Trichoderma - metabolism ; Trichoderma reesei</subject><ispartof>Letters in applied microbiology, 2009-12, Vol.49 (6), p.673-678</ispartof><rights>2009 The Authors. Journal compilation © 2009 The Society for Applied Microbiology</rights><rights>2015 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-c3834-18fd4181d1b8811dbc704b3a343784d491e8cfa7029e23a89d9c00e74cc4a643</citedby><orcidid>0000-0002-3266-8270 ; 0000-0002-7545-9997 ; 0000-0003-0239-9716</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1472-765X.2009.02734.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1472-765X.2009.02734.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,776,780,881,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22137053$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19780949$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02668642$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Poidevin, L.</creatorcontrib><creatorcontrib>Levasseur, A.</creatorcontrib><creatorcontrib>Paës, G.</creatorcontrib><creatorcontrib>Navarro, D.</creatorcontrib><creatorcontrib>Heiss‐Blanquet, S.</creatorcontrib><creatorcontrib>Asther, M.</creatorcontrib><creatorcontrib>Record, E.</creatorcontrib><title>Heterologous production of the Piromyces equi cinnamoyl esterase in Trichoderma reesei for biotechnological applications</title><title>Letters in applied microbiology</title><addtitle>Lett Appl Microbiol</addtitle><description>Aims: The objective of the study was to produce and characterize the cinnamoyl esterase EstA from the anaerobic fungus Piromyces equi for potential industrial applications.
Methods and Results: The catalytic domain EstA was produced in Trichoderma reesei. Because the two fungi displayed different genome features, including different codon usage and GC content, a synthetic gene was designed and expressed, leading to the production of the corresponding protein at around 33 mg per litre in the T. reesei culture medium. After the recombinant protein was purified, biochemical characterization showed that EstA presents peak activity at pH 6·5 and at 50–60°C. Furthermore, EstA remained stable at pH 6–8 and below 50°C. EstA was compared to cinnamoyl esterases FaeA and FaeB from Aspergillus niger in terms of ferulic acid (FA) release from wheat bran (WB), maize bran (MB) and sugar beet pulp (SBP).
Conclusion: The synthetic gene was successfully cloned and overexpressed in T. reesei. EstA from P. equi was demonstrated to efficiently release FA from various natural substrates.
Significance and Impact of the Study: Recombinant EstA produced in an industrial enzyme producer, T. reesei, was biochemically characterized, and its capacity to release an aromatic compound (FA) for biotechnological applications was demonstrated.</description><subject>Aspergillus niger - enzymology</subject><subject>Biological and medical sciences</subject><subject>biotechnology</subject><subject>Carboxylic Ester Hydrolases - genetics</subject><subject>Carboxylic Ester Hydrolases - metabolism</subject><subject>cinnamoyl esterase</subject><subject>Cloning, Molecular</subject><subject>Coumaric Acids - metabolism</subject><subject>ferulic acid</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>heterologous production</subject><subject>Hydrogen-Ion Concentration</subject><subject>Industrial Microbiology</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Microbiology and Parasitology</subject><subject>Piromyces - enzymology</subject><subject>Piromyces - genetics</subject><subject>Piromyces equi</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><subject>Trichoderma - genetics</subject><subject>Trichoderma - metabolism</subject><subject>Trichoderma reesei</subject><issn>0266-8254</issn><issn>1472-765X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkc2u0zAQhS0E4pYLr4C8QYhFgv8a2wsW1RVQpCJYdMHOcpwJdZXEvXYD7dtj01K8mZHn85HnHIQwJTXN5_2-pkKySjbLHzUjRNeESS7q0xO0uA2eogVhTVMpthR36EVKe0KIokw_R3dUS0W00At0WsMRYhjCzzAnfIihm93RhwmHHh93gL_7GMazg4ThcfbY-WmyYzgPGFJ-ZxNgP-Ft9G4XOoijxREggcd9iLj14QhuNxV17-yA7eEw5Kbop5foWW-HBK-u9R5tP33cPqyrzbfPXx5Wm8pxxUVFVd8JqmhHW6Uo7VoniWi55YJLJTqhKSjXW0mYBsat0p12hIAUzgnbCH6P3l1kd3Ywh-hHG88mWG_Wq40pd8Uj1Qj2i2b27YXNNjzOeUEz-uRgGOwE2R0jef6SpEpl8vWVnNsRupvwP18z8OYK2JQ376OdnE83jjHKJVnyzH24cL_9AOf_OsSUnM3elDhNidOUnM3fnM3JbFZfS8f_ADi_nOk</recordid><startdate>200912</startdate><enddate>200912</enddate><creator>Poidevin, L.</creator><creator>Levasseur, A.</creator><creator>Paës, G.</creator><creator>Navarro, D.</creator><creator>Heiss‐Blanquet, S.</creator><creator>Asther, M.</creator><creator>Record, E.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-3266-8270</orcidid><orcidid>https://orcid.org/0000-0002-7545-9997</orcidid><orcidid>https://orcid.org/0000-0003-0239-9716</orcidid></search><sort><creationdate>200912</creationdate><title>Heterologous production of the Piromyces equi cinnamoyl esterase in Trichoderma reesei for biotechnological applications</title><author>Poidevin, L. ; Levasseur, A. ; Paës, G. ; Navarro, D. ; Heiss‐Blanquet, S. ; Asther, M. ; Record, E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3834-18fd4181d1b8811dbc704b3a343784d491e8cfa7029e23a89d9c00e74cc4a643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Aspergillus niger - enzymology</topic><topic>Biological and medical sciences</topic><topic>biotechnology</topic><topic>Carboxylic Ester Hydrolases - genetics</topic><topic>Carboxylic Ester Hydrolases - metabolism</topic><topic>cinnamoyl esterase</topic><topic>Cloning, Molecular</topic><topic>Coumaric Acids - metabolism</topic><topic>ferulic acid</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>heterologous production</topic><topic>Hydrogen-Ion Concentration</topic><topic>Industrial Microbiology</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Microbiology and Parasitology</topic><topic>Piromyces - enzymology</topic><topic>Piromyces - genetics</topic><topic>Piromyces equi</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><topic>Trichoderma - genetics</topic><topic>Trichoderma - metabolism</topic><topic>Trichoderma reesei</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Poidevin, L.</creatorcontrib><creatorcontrib>Levasseur, A.</creatorcontrib><creatorcontrib>Paës, G.</creatorcontrib><creatorcontrib>Navarro, D.</creatorcontrib><creatorcontrib>Heiss‐Blanquet, S.</creatorcontrib><creatorcontrib>Asther, M.</creatorcontrib><creatorcontrib>Record, E.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Letters in applied microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Poidevin, L.</au><au>Levasseur, A.</au><au>Paës, G.</au><au>Navarro, D.</au><au>Heiss‐Blanquet, S.</au><au>Asther, M.</au><au>Record, E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heterologous production of the Piromyces equi cinnamoyl esterase in Trichoderma reesei for biotechnological applications</atitle><jtitle>Letters in applied microbiology</jtitle><addtitle>Lett Appl Microbiol</addtitle><date>2009-12</date><risdate>2009</risdate><volume>49</volume><issue>6</issue><spage>673</spage><epage>678</epage><pages>673-678</pages><issn>0266-8254</issn><eissn>1472-765X</eissn><coden>LAMIE7</coden><abstract>Aims: The objective of the study was to produce and characterize the cinnamoyl esterase EstA from the anaerobic fungus Piromyces equi for potential industrial applications.
Methods and Results: The catalytic domain EstA was produced in Trichoderma reesei. Because the two fungi displayed different genome features, including different codon usage and GC content, a synthetic gene was designed and expressed, leading to the production of the corresponding protein at around 33 mg per litre in the T. reesei culture medium. After the recombinant protein was purified, biochemical characterization showed that EstA presents peak activity at pH 6·5 and at 50–60°C. Furthermore, EstA remained stable at pH 6–8 and below 50°C. EstA was compared to cinnamoyl esterases FaeA and FaeB from Aspergillus niger in terms of ferulic acid (FA) release from wheat bran (WB), maize bran (MB) and sugar beet pulp (SBP).
Conclusion: The synthetic gene was successfully cloned and overexpressed in T. reesei. EstA from P. equi was demonstrated to efficiently release FA from various natural substrates.
Significance and Impact of the Study: Recombinant EstA produced in an industrial enzyme producer, T. reesei, was biochemically characterized, and its capacity to release an aromatic compound (FA) for biotechnological applications was demonstrated.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>19780949</pmid><doi>10.1111/j.1472-765X.2009.02734.x</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0002-3266-8270</orcidid><orcidid>https://orcid.org/0000-0002-7545-9997</orcidid><orcidid>https://orcid.org/0000-0003-0239-9716</orcidid></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Aspergillus niger - enzymology Biological and medical sciences biotechnology Carboxylic Ester Hydrolases - genetics Carboxylic Ester Hydrolases - metabolism cinnamoyl esterase Cloning, Molecular Coumaric Acids - metabolism ferulic acid Fundamental and applied biological sciences. Psychology Fungal Proteins - genetics Fungal Proteins - metabolism heterologous production Hydrogen-Ion Concentration Industrial Microbiology Life Sciences Microbiology Microbiology and Parasitology Piromyces - enzymology Piromyces - genetics Piromyces equi Recombinant Proteins - genetics Recombinant Proteins - metabolism Substrate Specificity Temperature Trichoderma - genetics Trichoderma - metabolism Trichoderma reesei |
| title | Heterologous production of the Piromyces equi cinnamoyl esterase in Trichoderma reesei for biotechnological applications |
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