Engineering Saccharomyces cerevisiae to produce feruloyl esterase for the release of ferulic acid from switchgrass
The Aspergillus niger feruloyl esterase gene (faeA) was cloned into Saccharomyces cerevisiae via a yeast expression vector, resulting in efficient expression and secretion of the enzyme in the medium with a yield of ~2 mg/l. The recombinant enzyme was purified to homogeneity by anion-exchange and hy...
Gespeichert in:
Veröffentlicht in: | Journal of industrial microbiology & biotechnology 2011-12, Vol.38 (12), p.1961-1967 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1967 |
---|---|
container_issue | 12 |
container_start_page | 1961 |
container_title | Journal of industrial microbiology & biotechnology |
container_volume | 38 |
creator | Wong, Dominic W. S Chan, Victor J Batt, Sarah B Sarath, Gautam Liao, Hans |
description | The Aspergillus niger feruloyl esterase gene (faeA) was cloned into Saccharomyces cerevisiae via a yeast expression vector, resulting in efficient expression and secretion of the enzyme in the medium with a yield of ~2 mg/l. The recombinant enzyme was purified to homogeneity by anion-exchange and hydrophobic interaction chromatography. The specific activity was determined to be 8,200 U/μg (pH 6.5, 20°C, 3.5 mM 4-nitrophenyl ferulate). The protein had a correct N-terminal sequence of ASTQGISEDLY, indicating that the signal peptide was properly processed. The FAE exhibited an optimum pH of 6–7 and operated optimally at 50°C using ground switchgrass as the substrate. The yeast clone was demonstrated to catalyze the release of ferulic acid continuously from switchgrass in YNB medium at 30°C. This work represents the first report on engineering yeast for the breakdown of ferulic acid crosslink to facilitate consolidated bioprocessing. |
doi_str_mv | 10.1007/s10295-011-0985-9 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_926903374</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>926903374</sourcerecordid><originalsourceid>FETCH-LOGICAL-c499t-c978f70b505c73256aac9a38563cb25510efb695fbc101dda8fee6a205487503</originalsourceid><addsrcrecordid>eNqFkktv1DAUhSMEoqXwA9iAhYRYBa7tXDteoqo8pEosWtaR41zPuMrEgz0Bzb_HIQOVWMDKD33n3GMdV9VzDm85gH6XOQiDNXBeg2mxNg-qc95oVSNKfFj2UukaG4ln1ZOc7wAAtRaPqzPBlVAC2vMqXU2bMBGlMG3YjXVua1PcHR1l5ijR95CDJXaIbJ_iMDtintI8xuPIKB8o2VxuYmKHLbFEIy3n6FcoOGZdGJgvhiz_CAe33RRBflo98nbM9Oy0XlS3H65uLz_V118-fr58f127xphD7YxuvYYeAZ2WApW1zljZopKuF4gcyPfKoO8dBz4MtvVEygrAptUI8qJ6s9qW5N_mkrbbhexoHO1Ecc6dEcqAlLr5PwnYag6_PF_9Rd7FOU3lFQskhGn4AvEVcinmnMh3-xR2Nh07Dt3SW7f21pXeuqW3zhTNi5Px3O9o-KP4XVQBXp8Am50dfbKTC_mew4KhVIUTK5f3S6WU7hP-a_rLVeRt7OwmFeOvNwJ4s_wYCbyVPwErhrmH</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>905229410</pqid></control><display><type>article</type><title>Engineering Saccharomyces cerevisiae to produce feruloyl esterase for the release of ferulic acid from switchgrass</title><source>MEDLINE</source><source>Access via Oxford University Press (Open Access Collection)</source><source>SpringerNature Journals</source><creator>Wong, Dominic W. S ; Chan, Victor J ; Batt, Sarah B ; Sarath, Gautam ; Liao, Hans</creator><creatorcontrib>Wong, Dominic W. S ; Chan, Victor J ; Batt, Sarah B ; Sarath, Gautam ; Liao, Hans</creatorcontrib><description>The Aspergillus niger feruloyl esterase gene (faeA) was cloned into Saccharomyces cerevisiae via a yeast expression vector, resulting in efficient expression and secretion of the enzyme in the medium with a yield of ~2 mg/l. The recombinant enzyme was purified to homogeneity by anion-exchange and hydrophobic interaction chromatography. The specific activity was determined to be 8,200 U/μg (pH 6.5, 20°C, 3.5 mM 4-nitrophenyl ferulate). The protein had a correct N-terminal sequence of ASTQGISEDLY, indicating that the signal peptide was properly processed. The FAE exhibited an optimum pH of 6–7 and operated optimally at 50°C using ground switchgrass as the substrate. The yeast clone was demonstrated to catalyze the release of ferulic acid continuously from switchgrass in YNB medium at 30°C. This work represents the first report on engineering yeast for the breakdown of ferulic acid crosslink to facilitate consolidated bioprocessing.</description><identifier>ISSN: 1367-5435</identifier><identifier>EISSN: 1476-5535</identifier><identifier>DOI: 10.1007/s10295-011-0985-9</identifier><identifier>PMID: 21626208</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>anion exchange ; Aspergillus niger ; Aspergillus niger - enzymology ; Aspergillus niger - genetics ; Biochemistry ; Bioinformatics ; Biological and medical sciences ; Biomass ; Biomedical and Life Sciences ; bioprocessing ; Biotechnology ; Carboxylic Ester Hydrolases - metabolism ; Catalysis ; chromatography ; Cloning ; Coumaric Acids - isolation & purification ; Engineering ; Enzyme kinetics ; Enzymes ; ferulic acid ; Fundamental and applied biological sciences. Psychology ; genes ; Genetic Engineering ; Glycerol ; Grasses ; hydrophobic bonding ; Inorganic Chemistry ; Kinases ; Life Sciences ; Lignin ; Microbiology ; Nitro Compounds ; Original Paper ; Panicum - chemistry ; Panicum virgatum ; Proteins ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; secretion ; signal peptide ; Studies ; Yeast ; Yeasts</subject><ispartof>Journal of industrial microbiology & biotechnology, 2011-12, Vol.38 (12), p.1961-1967</ispartof><rights>Springer-Verlag (outside the USA) 2011</rights><rights>2015 INIST-CNRS</rights><rights>Society for Industrial Microbiology and Biotechnology 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-c978f70b505c73256aac9a38563cb25510efb695fbc101dda8fee6a205487503</citedby><cites>FETCH-LOGICAL-c499t-c978f70b505c73256aac9a38563cb25510efb695fbc101dda8fee6a205487503</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10295-011-0985-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10295-011-0985-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>315,781,785,27929,27930,41493,42562,51324</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25262536$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21626208$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wong, Dominic W. S</creatorcontrib><creatorcontrib>Chan, Victor J</creatorcontrib><creatorcontrib>Batt, Sarah B</creatorcontrib><creatorcontrib>Sarath, Gautam</creatorcontrib><creatorcontrib>Liao, Hans</creatorcontrib><title>Engineering Saccharomyces cerevisiae to produce feruloyl esterase for the release of ferulic acid from switchgrass</title><title>Journal of industrial microbiology & biotechnology</title><addtitle>J Ind Microbiol Biotechnol</addtitle><addtitle>J Ind Microbiol Biotechnol</addtitle><description>The Aspergillus niger feruloyl esterase gene (faeA) was cloned into Saccharomyces cerevisiae via a yeast expression vector, resulting in efficient expression and secretion of the enzyme in the medium with a yield of ~2 mg/l. The recombinant enzyme was purified to homogeneity by anion-exchange and hydrophobic interaction chromatography. The specific activity was determined to be 8,200 U/μg (pH 6.5, 20°C, 3.5 mM 4-nitrophenyl ferulate). The protein had a correct N-terminal sequence of ASTQGISEDLY, indicating that the signal peptide was properly processed. The FAE exhibited an optimum pH of 6–7 and operated optimally at 50°C using ground switchgrass as the substrate. The yeast clone was demonstrated to catalyze the release of ferulic acid continuously from switchgrass in YNB medium at 30°C. This work represents the first report on engineering yeast for the breakdown of ferulic acid crosslink to facilitate consolidated bioprocessing.</description><subject>anion exchange</subject><subject>Aspergillus niger</subject><subject>Aspergillus niger - enzymology</subject><subject>Aspergillus niger - genetics</subject><subject>Biochemistry</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biomass</subject><subject>Biomedical and Life Sciences</subject><subject>bioprocessing</subject><subject>Biotechnology</subject><subject>Carboxylic Ester Hydrolases - metabolism</subject><subject>Catalysis</subject><subject>chromatography</subject><subject>Cloning</subject><subject>Coumaric Acids - isolation & purification</subject><subject>Engineering</subject><subject>Enzyme kinetics</subject><subject>Enzymes</subject><subject>ferulic acid</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Genetic Engineering</subject><subject>Glycerol</subject><subject>Grasses</subject><subject>hydrophobic bonding</subject><subject>Inorganic Chemistry</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>Lignin</subject><subject>Microbiology</subject><subject>Nitro Compounds</subject><subject>Original Paper</subject><subject>Panicum - chemistry</subject><subject>Panicum virgatum</subject><subject>Proteins</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>secretion</subject><subject>signal peptide</subject><subject>Studies</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>1367-5435</issn><issn>1476-5535</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkktv1DAUhSMEoqXwA9iAhYRYBa7tXDteoqo8pEosWtaR41zPuMrEgz0Bzb_HIQOVWMDKD33n3GMdV9VzDm85gH6XOQiDNXBeg2mxNg-qc95oVSNKfFj2UukaG4ln1ZOc7wAAtRaPqzPBlVAC2vMqXU2bMBGlMG3YjXVua1PcHR1l5ijR95CDJXaIbJ_iMDtintI8xuPIKB8o2VxuYmKHLbFEIy3n6FcoOGZdGJgvhiz_CAe33RRBflo98nbM9Oy0XlS3H65uLz_V118-fr58f127xphD7YxuvYYeAZ2WApW1zljZopKuF4gcyPfKoO8dBz4MtvVEygrAptUI8qJ6s9qW5N_mkrbbhexoHO1Ecc6dEcqAlLr5PwnYag6_PF_9Rd7FOU3lFQskhGn4AvEVcinmnMh3-xR2Nh07Dt3SW7f21pXeuqW3zhTNi5Px3O9o-KP4XVQBXp8Am50dfbKTC_mew4KhVIUTK5f3S6WU7hP-a_rLVeRt7OwmFeOvNwJ4s_wYCbyVPwErhrmH</recordid><startdate>20111201</startdate><enddate>20111201</enddate><creator>Wong, Dominic W. S</creator><creator>Chan, Victor J</creator><creator>Batt, Sarah B</creator><creator>Sarath, Gautam</creator><creator>Liao, Hans</creator><general>Springer-Verlag</general><general>Springer</general><general>Oxford University Press</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>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QO</scope></search><sort><creationdate>20111201</creationdate><title>Engineering Saccharomyces cerevisiae to produce feruloyl esterase for the release of ferulic acid from switchgrass</title><author>Wong, Dominic W. S ; Chan, Victor J ; Batt, Sarah B ; Sarath, Gautam ; Liao, Hans</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c499t-c978f70b505c73256aac9a38563cb25510efb695fbc101dda8fee6a205487503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>anion exchange</topic><topic>Aspergillus niger</topic><topic>Aspergillus niger - enzymology</topic><topic>Aspergillus niger - genetics</topic><topic>Biochemistry</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biomass</topic><topic>Biomedical and Life Sciences</topic><topic>bioprocessing</topic><topic>Biotechnology</topic><topic>Carboxylic Ester Hydrolases - metabolism</topic><topic>Catalysis</topic><topic>chromatography</topic><topic>Cloning</topic><topic>Coumaric Acids - isolation & purification</topic><topic>Engineering</topic><topic>Enzyme kinetics</topic><topic>Enzymes</topic><topic>ferulic acid</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Genetic Engineering</topic><topic>Glycerol</topic><topic>Grasses</topic><topic>hydrophobic bonding</topic><topic>Inorganic Chemistry</topic><topic>Kinases</topic><topic>Life Sciences</topic><topic>Lignin</topic><topic>Microbiology</topic><topic>Nitro Compounds</topic><topic>Original Paper</topic><topic>Panicum - chemistry</topic><topic>Panicum virgatum</topic><topic>Proteins</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>secretion</topic><topic>signal peptide</topic><topic>Studies</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wong, Dominic W. S</creatorcontrib><creatorcontrib>Chan, Victor J</creatorcontrib><creatorcontrib>Batt, Sarah B</creatorcontrib><creatorcontrib>Sarath, Gautam</creatorcontrib><creatorcontrib>Liao, Hans</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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Access via ABI/INFORM (ProQuest)</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection (Alumni Edition)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>Proquest Central</collection><collection>Business Premium Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database (ProQuest)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Journal of industrial microbiology & biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wong, Dominic W. S</au><au>Chan, Victor J</au><au>Batt, Sarah B</au><au>Sarath, Gautam</au><au>Liao, Hans</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Engineering Saccharomyces cerevisiae to produce feruloyl esterase for the release of ferulic acid from switchgrass</atitle><jtitle>Journal of industrial microbiology & biotechnology</jtitle><stitle>J Ind Microbiol Biotechnol</stitle><addtitle>J Ind Microbiol Biotechnol</addtitle><date>2011-12-01</date><risdate>2011</risdate><volume>38</volume><issue>12</issue><spage>1961</spage><epage>1967</epage><pages>1961-1967</pages><issn>1367-5435</issn><eissn>1476-5535</eissn><abstract>The Aspergillus niger feruloyl esterase gene (faeA) was cloned into Saccharomyces cerevisiae via a yeast expression vector, resulting in efficient expression and secretion of the enzyme in the medium with a yield of ~2 mg/l. The recombinant enzyme was purified to homogeneity by anion-exchange and hydrophobic interaction chromatography. The specific activity was determined to be 8,200 U/μg (pH 6.5, 20°C, 3.5 mM 4-nitrophenyl ferulate). The protein had a correct N-terminal sequence of ASTQGISEDLY, indicating that the signal peptide was properly processed. The FAE exhibited an optimum pH of 6–7 and operated optimally at 50°C using ground switchgrass as the substrate. The yeast clone was demonstrated to catalyze the release of ferulic acid continuously from switchgrass in YNB medium at 30°C. This work represents the first report on engineering yeast for the breakdown of ferulic acid crosslink to facilitate consolidated bioprocessing.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>21626208</pmid><doi>10.1007/s10295-011-0985-9</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1367-5435 |
ispartof | Journal of industrial microbiology & biotechnology, 2011-12, Vol.38 (12), p.1961-1967 |
issn | 1367-5435 1476-5535 |
language | eng |
recordid | cdi_proquest_miscellaneous_926903374 |
source | MEDLINE; Access via Oxford University Press (Open Access Collection); SpringerNature Journals |
subjects | anion exchange Aspergillus niger Aspergillus niger - enzymology Aspergillus niger - genetics Biochemistry Bioinformatics Biological and medical sciences Biomass Biomedical and Life Sciences bioprocessing Biotechnology Carboxylic Ester Hydrolases - metabolism Catalysis chromatography Cloning Coumaric Acids - isolation & purification Engineering Enzyme kinetics Enzymes ferulic acid Fundamental and applied biological sciences. Psychology genes Genetic Engineering Glycerol Grasses hydrophobic bonding Inorganic Chemistry Kinases Life Sciences Lignin Microbiology Nitro Compounds Original Paper Panicum - chemistry Panicum virgatum Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics secretion signal peptide Studies Yeast Yeasts |
title | Engineering Saccharomyces cerevisiae to produce feruloyl esterase for the release of ferulic acid from switchgrass |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-12T12%3A52%3A44IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Engineering%20Saccharomyces%20cerevisiae%20to%20produce%20feruloyl%20esterase%20for%20the%20release%20of%20ferulic%20acid%20from%20switchgrass&rft.jtitle=Journal%20of%20industrial%20microbiology%20&%20biotechnology&rft.au=Wong,%20Dominic%20W.%20S&rft.date=2011-12-01&rft.volume=38&rft.issue=12&rft.spage=1961&rft.epage=1967&rft.pages=1961-1967&rft.issn=1367-5435&rft.eissn=1476-5535&rft_id=info:doi/10.1007/s10295-011-0985-9&rft_dat=%3Cproquest_cross%3E926903374%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=905229410&rft_id=info:pmid/21626208&rfr_iscdi=true |