Expression and evaluation of enzymes required for the hydrolysis of galactomannan
The cost-effective production of bioethanol from lignocellulose requires the complete conversion of plant biomass, which contains up to 30 % mannan. To ensure utilisation of galactomannan during consolidated bioprocessing, heterologous production of mannan-degrading enzymes in fungal hosts was explo...
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| Veröffentlicht in: | Journal of industrial microbiology & biotechnology 2014-08, Vol.41 (8), p.1201-1209 |
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| creator | Malherbe, A. R Rose, S. H Viljoen-Bloom, M van Zyl, W. H |
| description | The cost-effective production of bioethanol from lignocellulose requires the complete conversion of plant biomass, which contains up to 30 % mannan. To ensure utilisation of galactomannan during consolidated bioprocessing, heterologous production of mannan-degrading enzymes in fungal hosts was explored. The Aspergillus aculeatus endo-β-mannanase (Man1) and Talaromyces emersonii α-galactosidase (Agal) genes were expressed in Saccharomyces cerevisiae Y294, and the Aspergillus niger β-mannosidase (cMndA) and synthetic Cellvibrio mixtus β-mannosidase (Man5A) genes in A. niger. Maximum enzyme activity for Man1 (374 nkat ml⁻¹, pH 5.47), Agal (135 nkat ml⁻¹, pH 2.37), cMndA (12 nkat ml⁻¹, pH 3.40) and Man5A (8 nkat ml⁻¹, pH 3.40) was observed between 60 and 70 °C. Co-expression of the Man1 and Agal genes in S. cerevisiae Y294[Agal-Man1] reduced the extracellular activity relative to individual expression of the respective genes. However, the combined action of crude Man1, Agal and Man5A enzyme preparations significantly decreased the viscosity of galactomannan in locust bean gum, confirming hydrolysis thereof. Furthermore, when complemented with exogenous Man5A, S. cerevisiae Y294[Agal-Man1] produced 56 % of the theoretical ethanol yield, corresponding to a 66 % carbohydrate conversion, on 5 g l⁻¹ mannose and 10 g l⁻¹ locust bean gum. |
| doi_str_mv | 10.1007/s10295-014-1459-7 |
| format | Article |
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R ; Rose, S. H ; Viljoen-Bloom, M ; van Zyl, W. H</creator><creatorcontrib>Malherbe, A. R ; Rose, S. H ; Viljoen-Bloom, M ; van Zyl, W. H</creatorcontrib><description>The cost-effective production of bioethanol from lignocellulose requires the complete conversion of plant biomass, which contains up to 30 % mannan. To ensure utilisation of galactomannan during consolidated bioprocessing, heterologous production of mannan-degrading enzymes in fungal hosts was explored. The Aspergillus aculeatus endo-β-mannanase (Man1) and Talaromyces emersonii α-galactosidase (Agal) genes were expressed in Saccharomyces cerevisiae Y294, and the Aspergillus niger β-mannosidase (cMndA) and synthetic Cellvibrio mixtus β-mannosidase (Man5A) genes in A. niger. Maximum enzyme activity for Man1 (374 nkat ml⁻¹, pH 5.47), Agal (135 nkat ml⁻¹, pH 2.37), cMndA (12 nkat ml⁻¹, pH 3.40) and Man5A (8 nkat ml⁻¹, pH 3.40) was observed between 60 and 70 °C. Co-expression of the Man1 and Agal genes in S. cerevisiae Y294[Agal-Man1] reduced the extracellular activity relative to individual expression of the respective genes. However, the combined action of crude Man1, Agal and Man5A enzyme preparations significantly decreased the viscosity of galactomannan in locust bean gum, confirming hydrolysis thereof. Furthermore, when complemented with exogenous Man5A, S. cerevisiae Y294[Agal-Man1] produced 56 % of the theoretical ethanol yield, corresponding to a 66 % carbohydrate conversion, on 5 g l⁻¹ mannose and 10 g l⁻¹ locust bean gum.</description><identifier>ISSN: 1367-5435</identifier><identifier>EISSN: 1476-5535</identifier><identifier>DOI: 10.1007/s10295-014-1459-7</identifier><identifier>PMID: 24888762</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>alpha-galactosidase ; alpha-Galactosidase - metabolism ; Amino acids ; Aspergillus - enzymology ; Aspergillus aculeatus ; Aspergillus niger ; beta-mannosidase ; beta-Mannosidase - genetics ; Biochemistry ; Biodiesel fuels ; Bioenergy/Biofuels/Biochemicals ; Biofuels ; Bioinformatics ; Biological and medical sciences ; Biomass ; Biomedical and Life Sciences ; bioprocessing ; Bioreactors ; Biotechnology ; Cellvibrio - enzymology ; Cellvibrio mixtus ; Cloning ; cost effectiveness ; Enzymatic activity ; enzyme activity ; Enzymes ; Ethanol ; ethanol production ; Fundamental and applied biological sciences. Psychology ; Fungi ; Galactans ; galactomannans ; Genes ; Genetic Engineering ; Glucose ; hosts ; Hydrolysis ; Industrial Microbiology - methods ; Inorganic Chemistry ; Kinetics ; Laboratories ; Life Sciences ; Lignin - metabolism ; Lignocellulose ; locust bean gum ; Mannans - metabolism ; mannose ; Microbiology ; Plant biomass ; Plant Gums ; Plasmids ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Studies ; Talaromyces ; Talaromyces - enzymology ; Talaromyces emersonii ; Viscosity ; Yeast</subject><ispartof>Journal of industrial microbiology & biotechnology, 2014-08, Vol.41 (8), p.1201-1209</ispartof><rights>Society for Industrial Microbiology and Biotechnology 2014</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c595t-72df824dd8d1ff1b5a01665099144d1b38d2c037d921015e767f2946a18b0d63</citedby><cites>FETCH-LOGICAL-c595t-72df824dd8d1ff1b5a01665099144d1b38d2c037d921015e767f2946a18b0d63</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/s10295-014-1459-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10295-014-1459-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28612395$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24888762$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Malherbe, A. R</creatorcontrib><creatorcontrib>Rose, S. H</creatorcontrib><creatorcontrib>Viljoen-Bloom, M</creatorcontrib><creatorcontrib>van Zyl, W. H</creatorcontrib><title>Expression and evaluation of enzymes required for the hydrolysis of galactomannan</title><title>Journal of industrial microbiology & biotechnology</title><addtitle>J Ind Microbiol Biotechnol</addtitle><addtitle>J Ind Microbiol Biotechnol</addtitle><description>The cost-effective production of bioethanol from lignocellulose requires the complete conversion of plant biomass, which contains up to 30 % mannan. To ensure utilisation of galactomannan during consolidated bioprocessing, heterologous production of mannan-degrading enzymes in fungal hosts was explored. The Aspergillus aculeatus endo-β-mannanase (Man1) and Talaromyces emersonii α-galactosidase (Agal) genes were expressed in Saccharomyces cerevisiae Y294, and the Aspergillus niger β-mannosidase (cMndA) and synthetic Cellvibrio mixtus β-mannosidase (Man5A) genes in A. niger. Maximum enzyme activity for Man1 (374 nkat ml⁻¹, pH 5.47), Agal (135 nkat ml⁻¹, pH 2.37), cMndA (12 nkat ml⁻¹, pH 3.40) and Man5A (8 nkat ml⁻¹, pH 3.40) was observed between 60 and 70 °C. Co-expression of the Man1 and Agal genes in S. cerevisiae Y294[Agal-Man1] reduced the extracellular activity relative to individual expression of the respective genes. However, the combined action of crude Man1, Agal and Man5A enzyme preparations significantly decreased the viscosity of galactomannan in locust bean gum, confirming hydrolysis thereof. Furthermore, when complemented with exogenous Man5A, S. cerevisiae Y294[Agal-Man1] produced 56 % of the theoretical ethanol yield, corresponding to a 66 % carbohydrate conversion, on 5 g l⁻¹ mannose and 10 g l⁻¹ locust bean gum.</description><subject>alpha-galactosidase</subject><subject>alpha-Galactosidase - metabolism</subject><subject>Amino acids</subject><subject>Aspergillus - enzymology</subject><subject>Aspergillus aculeatus</subject><subject>Aspergillus niger</subject><subject>beta-mannosidase</subject><subject>beta-Mannosidase - genetics</subject><subject>Biochemistry</subject><subject>Biodiesel fuels</subject><subject>Bioenergy/Biofuels/Biochemicals</subject><subject>Biofuels</subject><subject>Bioinformatics</subject><subject>Biological and medical sciences</subject><subject>Biomass</subject><subject>Biomedical and Life Sciences</subject><subject>bioprocessing</subject><subject>Bioreactors</subject><subject>Biotechnology</subject><subject>Cellvibrio - enzymology</subject><subject>Cellvibrio mixtus</subject><subject>Cloning</subject><subject>cost effectiveness</subject><subject>Enzymatic activity</subject><subject>enzyme activity</subject><subject>Enzymes</subject><subject>Ethanol</subject><subject>ethanol production</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungi</subject><subject>Galactans</subject><subject>galactomannans</subject><subject>Genes</subject><subject>Genetic Engineering</subject><subject>Glucose</subject><subject>hosts</subject><subject>Hydrolysis</subject><subject>Industrial Microbiology - methods</subject><subject>Inorganic Chemistry</subject><subject>Kinetics</subject><subject>Laboratories</subject><subject>Life Sciences</subject><subject>Lignin - metabolism</subject><subject>Lignocellulose</subject><subject>locust bean gum</subject><subject>Mannans - metabolism</subject><subject>mannose</subject><subject>Microbiology</subject><subject>Plant biomass</subject><subject>Plant Gums</subject><subject>Plasmids</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Studies</subject><subject>Talaromyces</subject><subject>Talaromyces - enzymology</subject><subject>Talaromyces emersonii</subject><subject>Viscosity</subject><subject>Yeast</subject><issn>1367-5435</issn><issn>1476-5535</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</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>eNqNkk1LHTEUhoMo1dr-ADd1oBS6Gc3J52RZxH6AUES7DrmT5Doyk1yTmdLbX99M57aVLsRVEs7zvsk5bxA6AXwGGMvzDJgoXmNgNTCuarmHjoBJUXNO-X7ZUyFrzig_RC9zvscYcynJC3RIWNM0UpAjdH35Y5Nczl0MlQm2ct9NP5lxPkZfufBzO7hcJfcwdcnZysdUjXeuutvaFPtt7vKMrU1v2jEOJgQTXqEDb_rsXu_WY3T78fL24nN99fXTl4sPV3XLFR9rSaxvCLO2seA9rLjBIATHSgFjFla0saTFVFpFAAN3UkhPFBMGmhW2gh6j94vtJsWHyeVRD11uXd-b4OKUNXDOMRBFnoMyJhmhRBb07X_ofZxSKH38piiQMsJCwUK1KeacnNeb1A0mbTVgPSejl2R0SUbPyehZ82bnPK0GZ_8q_kRRgHc7wOTW9D6Z0Hb5H9cIIFTxwpGFy6UU1i49euITt58uIm-iNutUjL_dkDLX8icwkyDpL25-rS4</recordid><startdate>20140801</startdate><enddate>20140801</enddate><creator>Malherbe, A. 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R ; Rose, S. H ; Viljoen-Bloom, M ; van Zyl, W. H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c595t-72df824dd8d1ff1b5a01665099144d1b38d2c037d921015e767f2946a18b0d63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>alpha-galactosidase</topic><topic>alpha-Galactosidase - metabolism</topic><topic>Amino acids</topic><topic>Aspergillus - enzymology</topic><topic>Aspergillus aculeatus</topic><topic>Aspergillus niger</topic><topic>beta-mannosidase</topic><topic>beta-Mannosidase - genetics</topic><topic>Biochemistry</topic><topic>Biodiesel fuels</topic><topic>Bioenergy/Biofuels/Biochemicals</topic><topic>Biofuels</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biomass</topic><topic>Biomedical and Life Sciences</topic><topic>bioprocessing</topic><topic>Bioreactors</topic><topic>Biotechnology</topic><topic>Cellvibrio - enzymology</topic><topic>Cellvibrio mixtus</topic><topic>Cloning</topic><topic>cost effectiveness</topic><topic>Enzymatic activity</topic><topic>enzyme activity</topic><topic>Enzymes</topic><topic>Ethanol</topic><topic>ethanol production</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungi</topic><topic>Galactans</topic><topic>galactomannans</topic><topic>Genes</topic><topic>Genetic Engineering</topic><topic>Glucose</topic><topic>hosts</topic><topic>Hydrolysis</topic><topic>Industrial Microbiology - methods</topic><topic>Inorganic Chemistry</topic><topic>Kinetics</topic><topic>Laboratories</topic><topic>Life Sciences</topic><topic>Lignin - metabolism</topic><topic>Lignocellulose</topic><topic>locust bean gum</topic><topic>Mannans - metabolism</topic><topic>mannose</topic><topic>Microbiology</topic><topic>Plant biomass</topic><topic>Plant Gums</topic><topic>Plasmids</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Studies</topic><topic>Talaromyces</topic><topic>Talaromyces - enzymology</topic><topic>Talaromyces emersonii</topic><topic>Viscosity</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Malherbe, A. 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R</au><au>Rose, S. H</au><au>Viljoen-Bloom, M</au><au>van Zyl, W. H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression and evaluation of enzymes required for the hydrolysis of galactomannan</atitle><jtitle>Journal of industrial microbiology & biotechnology</jtitle><stitle>J Ind Microbiol Biotechnol</stitle><addtitle>J Ind Microbiol Biotechnol</addtitle><date>2014-08-01</date><risdate>2014</risdate><volume>41</volume><issue>8</issue><spage>1201</spage><epage>1209</epage><pages>1201-1209</pages><issn>1367-5435</issn><eissn>1476-5535</eissn><abstract>The cost-effective production of bioethanol from lignocellulose requires the complete conversion of plant biomass, which contains up to 30 % mannan. To ensure utilisation of galactomannan during consolidated bioprocessing, heterologous production of mannan-degrading enzymes in fungal hosts was explored. The Aspergillus aculeatus endo-β-mannanase (Man1) and Talaromyces emersonii α-galactosidase (Agal) genes were expressed in Saccharomyces cerevisiae Y294, and the Aspergillus niger β-mannosidase (cMndA) and synthetic Cellvibrio mixtus β-mannosidase (Man5A) genes in A. niger. Maximum enzyme activity for Man1 (374 nkat ml⁻¹, pH 5.47), Agal (135 nkat ml⁻¹, pH 2.37), cMndA (12 nkat ml⁻¹, pH 3.40) and Man5A (8 nkat ml⁻¹, pH 3.40) was observed between 60 and 70 °C. Co-expression of the Man1 and Agal genes in S. cerevisiae Y294[Agal-Man1] reduced the extracellular activity relative to individual expression of the respective genes. However, the combined action of crude Man1, Agal and Man5A enzyme preparations significantly decreased the viscosity of galactomannan in locust bean gum, confirming hydrolysis thereof. Furthermore, when complemented with exogenous Man5A, S. cerevisiae Y294[Agal-Man1] produced 56 % of the theoretical ethanol yield, corresponding to a 66 % carbohydrate conversion, on 5 g l⁻¹ mannose and 10 g l⁻¹ locust bean gum.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>24888762</pmid><doi>10.1007/s10295-014-1459-7</doi><tpages>9</tpages></addata></record> |
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| ispartof | Journal of industrial microbiology & biotechnology, 2014-08, Vol.41 (8), p.1201-1209 |
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| subjects | alpha-galactosidase alpha-Galactosidase - metabolism Amino acids Aspergillus - enzymology Aspergillus aculeatus Aspergillus niger beta-mannosidase beta-Mannosidase - genetics Biochemistry Biodiesel fuels Bioenergy/Biofuels/Biochemicals Biofuels Bioinformatics Biological and medical sciences Biomass Biomedical and Life Sciences bioprocessing Bioreactors Biotechnology Cellvibrio - enzymology Cellvibrio mixtus Cloning cost effectiveness Enzymatic activity enzyme activity Enzymes Ethanol ethanol production Fundamental and applied biological sciences. Psychology Fungi Galactans galactomannans Genes Genetic Engineering Glucose hosts Hydrolysis Industrial Microbiology - methods Inorganic Chemistry Kinetics Laboratories Life Sciences Lignin - metabolism Lignocellulose locust bean gum Mannans - metabolism mannose Microbiology Plant biomass Plant Gums Plasmids Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Studies Talaromyces Talaromyces - enzymology Talaromyces emersonii Viscosity Yeast |
| title | Expression and evaluation of enzymes required for the hydrolysis of galactomannan |
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