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Table 1: List of Trichoderma enzymes industrially produced in Trichoderma sp. (AMFEP, 2009).
Host organismEnzymeT. reesei or longibrachiatumCellulaseGlucanase (beta)GlucoamylaseGlucosyltransferaseHemicellulaseMannanase (endo-1.4-beta)PentosanaseProteaseXylanaseT. harzianumGlucanase (beta)Glucosidase (exo-1.3-beta)T. virideCellulaseXylanase
Table 2: List of non-Trichoderma enzymes industrially produced in Trichoderma sp. (AMFEP, 2009).
Host organismEnzymeDonor organismT. reesei or longibrachiatumAminopeptidaseAspergillus sp.Amylase (alpha)Aspergillus sp.LaccaseThielavia sp.Pectin lyaseAspergillus sp.Pectin methylesteraseAspergillus sp.Phospholipase AAspergillus sp.Phospholipase AThermomyces sp.Phospholipase BAspergillus sp.PhytaseAspergillus sp.PhytaseButtiauxella sp.PolygalacturonaseAspergillus sp.PullulanaseHormoconis sp.XylanaseActinomadura sp.

Table 3: Enzymes heterologously produced in Trichoderma in laboratory scale.
EnzymeYield [gl-1]Donor organismReferenceAcid phosphatase0.5 (shake flask)Aspergillus niger ADDIN EN.CITE <EndNote><Cite><Author>Miettinen-Oinonen</Author><Year>1997</Year><RecNum>218</RecNum><DisplayText>[40]</DisplayText><record><rec-number>218</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">218</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Miettinen-Oinonen, A.</author><author>Torkkeli, T.</author><author>Paloheimo, M.</author><author>Nevalainen, H.</author></authors></contributors><auth-address>Primalco Ltd Biotec, Rajamaki, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Overexpression of the </style><style face="italic" font="default" size="100%">Aspergillus niger</style><style face="normal" font="default" size="100%"> pH 2.5 acid phosphatase gene in a heterologous host </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Journal of biotechnology</secondary-title><alt-title>J Biotechnol</alt-title></titles><periodical><full-title>Journal of biotechnology</full-title><abbr-1>J Biotechnol</abbr-1></periodical><alt-periodical><full-title>Journal of biotechnology</full-title><abbr-1>J Biotechnol</abbr-1></alt-periodical><pages>13-20</pages><volume>58</volume><number>1</number><edition>1997/10/23</edition><keywords><keyword>Acid Phosphatase/biosynthesis/*genetics</keyword><keyword>Aspergillus niger/enzymology/*genetics</keyword><keyword>Gene Expression Regulation, Enzymologic</keyword><keyword>Hydrogen-Ion Concentration</keyword><keyword>Recombinant Proteins/biosynthesis</keyword><keyword>Trichoderma/*genetics</keyword></keywords><dates><year>1997</year><pub-dates><date>Oct 2</date></pub-dates></dates><isbn>0168-1656 (Print)&#xD;0168-1656 (Linking)</isbn><accession-num>9335175</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/9335175</url></related-urls></urls><language>eng</language></record></Cite></EndNote>[40]Fab antibody fragments0.15 (small-scale fermentor)Murine ADDIN EN.CITE  ADDIN EN.CITE.DATA [22]Glucosidase (beta)0.0027 (shake flask)Talaromyces emersonii ADDIN EN.CITE  ADDIN EN.CITE.DATA [41]Chymosin0.1 (shake flask)Calf ADDIN EN.CITE  ADDIN EN.CITE.DATA [19, 20]Cinnamoyl esterase EstA0.033 (shake flask)Piromyces equi ADDIN EN.CITE  ADDIN EN.CITE.DATA [42]Cutinase1.4 (small-scale fermentor)Coprinopsis cinerea ADDIN EN.CITE  ADDIN EN.CITE.DATA [43]DewA0.033 (small-scale fermentor)Aspergillus nidulans ADDIN EN.CITE  ADDIN EN.CITE.DATA [44]Endochitinase.13 (shake flask)Trichoderma harzianum ADDIN EN.CITE  ADDIN EN.CITE.DATA [45]Endopeptidase B0.5 (small-scale fermentor)Barley ADDIN EN.CITE <EndNote><Cite><Author>Saarelainen</Author><Year>1997</Year><RecNum>223</RecNum><DisplayText>[46]</DisplayText><record><rec-number>223</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">223</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Saarelainen, R.</author><author>Mantyla, A.</author><author>Nevalainen, H.</author><author>Suominen, P.</author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Expression of Barley Endopeptidase B in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Applied and environmental microbiology</secondary-title><alt-title>Appl Environ Microbiol</alt-title></titles><periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></periodical><alt-periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></alt-periodical><pages>4938-40</pages><volume>63</volume><number>12</number><edition>2006/03/15</edition><dates><year>1997</year><pub-dates><date>Dec</date></pub-dates></dates><isbn>0099-2240 (Print)&#xD;0099-2240 (Linking)</isbn><accession-num>16535756</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/16535756</url></related-urls></urls><custom2>1389312</custom2><language>eng</language></record></Cite></EndNote>[46]Glucoamylase P0.7 (shake flask)Hormoconis resinae ADDIN EN.CITE  ADDIN EN.CITE.DATA [47, 48]Laccase0.02 (small-scale fermentor)Phlebia radiate ADDIN EN.CITE <EndNote><Cite><Author>Saloheimo</Author><Year>1991</Year><RecNum>230</RecNum><DisplayText>[49]</DisplayText><record><rec-number>230</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">230</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Saloheimo, M.</author><author>Niku-Paavola, M.-L.</author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Heterologous production of a ligninolytic enzyme: expression of the </style><style face="italic" font="default" size="100%">Phlebia radiata</style><style face="normal" font="default" size="100%"> laccase gene in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Bio/technology</secondary-title></titles><periodical><full-title>Bio/technology</full-title><abbr-1>Biotechnology (N Y)</abbr-1></periodical><pages>987-990</pages><volume>9</volume><number>10</number><dates><year>1991</year></dates><urls></urls></record></Cite></EndNote>[49]Laccase0.23 (small-scale fermentor)Melanocarpus albomyces ADDIN EN.CITE  ADDIN EN.CITE.DATA [50]Steryl esterase0.076 (shake flask)Melanocarpus albomyces ADDIN EN.CITE  ADDIN EN.CITE.DATA [51, 52]Xylanase II0.5 (small-scale fermentor)Humicola grisea ADDIN EN.CITE <EndNote><Cite><Author>De Faria</Author><Year>2002</Year><RecNum>239</RecNum><DisplayText>[53]</DisplayText><record><rec-number>239</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">239</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>De Faria, F. P.</author><author>Te&apos;O, V. S. J.</author><author>Bergquist, P. L.</author><author>Azevedo, M. O.</author><author>Nevalainen, K. M. H.</author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Expression and processing of a major xylanase (XYN2) from the thermophilic fungus </style><style face="italic" font="default" size="100%">Humicola grisea var. thermoidea</style><style face="normal" font="default" size="100%"> in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Letters in applied microbiology</secondary-title></titles><periodical><full-title>Letters in applied microbiology</full-title><abbr-1>Lett Appl Microbiol</abbr-1></periodical><pages>119-123</pages><volume>34</volume><number>2</number><dates><year>2002</year></dates><publisher>Blackwell Science Ltd</publisher><isbn>1472-765X</isbn><urls><related-urls><url>http://dx.doi.org/10.1046/j.1472-765x.2002.01057.x</url></related-urls></urls><electronic-resource-num>10.1046/j.1472-765x.2002.01057.x</electronic-resource-num></record></Cite></EndNote>[53]Xyn VI0.172 (shake flask)Acrophialophora nainiana ADDIN EN.CITE  ADDIN EN.CITE.DATA [54]Xyn11A0.82 (small-scale fermentor)Nonomuraea flexuosa ADDIN EN.CITE  ADDIN EN.CITE.DATA [55]
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Fa�7p�(��������X	D<EndNote><Cite><Author>Nyyssönen</Author><Year>1993</Year><RecNum>216</RecNum><DisplayText>[22]</DisplayText><record><rec-number>216</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">216</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Nyyssönen, E.</author><author>Penttilä, M.</author><author>Harkki, A.</author><author>Saloheimo, A.</author><author>Knowles, J. K.</author><author>Keränen, S.</author></authors></contributors><auth-address>VTT Biotechnical Laboratory, Espoo, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Efficient production of antibody fragments by the filamentous fungus </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Bio/technology</secondary-title><alt-title>Biotechnology (N Y)</alt-title></titles><periodical><full-title>Bio/technology</full-title><abbr-1>Biotechnology (N Y)</abbr-1></periodical><alt-periodical><full-title>Bio/technology</full-title><abbr-1>Biotechnology (N Y)</abbr-1></alt-periodical><pages>591-5</pages><volume>11</volume><number>5</number><edition>1993/05/01</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Animals</keyword><keyword>Base Sequence</keyword><keyword>Blotting, Western</keyword><keyword>Cellulase/genetics</keyword><keyword>Endopeptidases/metabolism</keyword><keyword>Genetic Engineering</keyword><keyword>Genetic Vectors</keyword><keyword>Immunoglobulin Fab Fragments/*biosynthesis/chemistry/genetics</keyword><keyword>Immunoglobulin G/biosynthesis/chemistry/genetics</keyword><keyword>Mice</keyword><keyword>Molecular Sequence Data</keyword><keyword>Oxazolone/analogs &amp; derivatives/immunology</keyword><keyword>Plasmids</keyword><keyword>Recombinant Fusion Proteins/biosynthesis</keyword><keyword>Transfection</keyword><keyword>Trichoderma/*genetics/immunology</keyword></keywords><dates><year>1993</year><pub-dates><date>May</date></pub-dates></dates><isbn>0733-222X (Print)&#xD;0733-222X (Linking)</isbn><accession-num>7763606</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/7763606</url></related-urls></urls><language>eng</language></record></Cite></EndNote>X	D<EndNote><Cite><Author>Nyyssönen</Author><Year>1993</Year><RecNum>216</RecNum><DisplayText>[22]</DisplayText><record><rec-number>216</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">216</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Nyyssönen, E.</author><author>Penttilä, M.</author><author>Harkki, A.</author><author>Saloheimo, A.</author><author>Knowles, J. K.</author><author>Keränen, S.</author></authors></contributors><auth-address>VTT Biotechnical Laboratory, Espoo, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Efficient production of antibody fragments by the filamentous fungus </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Bio/technology</secondary-title><alt-title>Biotechnology (N Y)</alt-title></titles><periodical><full-title>Bio/technology</full-title><abbr-1>Biotechnology (N Y)</abbr-1></periodical><alt-periodical><full-title>Bio/technology</full-title><abbr-1>Biotechnology (N Y)</abbr-1></alt-periodical><pages>591-5</pages><volume>11</volume><number>5</number><edition>1993/05/01</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Animals</keyword><keyword>Base Sequence</keyword><keyword>Blotting, Western</keyword><keyword>Cellulase/genetics</keyword><keyword>Endopeptidases/metabolism</keyword><keyword>Genetic Engineering</keyword><keyword>Genetic Vectors</keyword><keyword>Immunoglobulin Fab Fragments/*biosynthesis/chemistry/genetics</keyword><keyword>Immunoglobulin G/biosynthesis/chemistry/genetics</keyword><keyword>Mice</keyword><keyword>Molecular Sequence Data</keyword><keyword>Oxazolone/analogs &amp; derivatives/immunology</keyword><keyword>Plasmids</keyword><keyword>Recombinant Fusion Proteins/biosynthesis</keyword><keyword>Transfection</keyword><keyword>Trichoderma/*genetics/immunology</keyword></keywords><dates><year>1993</year><pub-dates><date>May</date></pub-dates></dates><isbn>0733-222X (Print)&#xD;0733-222X (Linking)</isbn><accession-num>7763606</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/7763606</url></related-urls></urls><language>eng</language></record></Cite></EndNote>$$If�7!vh5��5�r
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D<EndNote><Cite><Author>Murray</Author><Year>2004</Year><RecNum>81</RecNum><DisplayText>[41]</DisplayText><record><rec-number>81</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">81</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Murray, P.</author><author>Aro, N.</author><author>Collins, C.</author><author>Grassick, A.</author><author>Penttilä, M.</author><author>Saloheimo, M.</author><author>Tuohy, M.</author></authors></contributors><auth-address>Molecular Glycobiotechnology Group, Department of Biochemistry, National University of Ireland, Galway, Ireland.</auth-address><titles><title><style face="normal" font="default" size="100%">Expression in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> and characterisation of a thermostable family 3 beta-glucosidase from the moderately thermophilic fungus </style><style face="italic" font="default" size="100%">Talaromyces emersonii</style></title><secondary-title>Protein expression and purification</secondary-title><alt-title>Protein Expr Purif</alt-title></titles><periodical><full-title>Protein expression and purification</full-title><abbr-1>Protein Expr Purif</abbr-1></periodical><alt-periodical><full-title>Protein expression and purification</full-title><abbr-1>Protein Expr Purif</abbr-1></alt-periodical><pages>248-57</pages><volume>38</volume><number>2</number><edition>2004/11/24</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Cloning, Molecular</keyword><keyword>Enzyme Stability/physiology</keyword><keyword>*Gene Expression Regulation, Enzymologic</keyword><keyword>Genetic Vectors/genetics</keyword><keyword>Molecular Sequence Data</keyword><keyword>Molecular Weight</keyword><keyword>Recombinant Fusion Proteins/chemistry/genetics/isolation &amp; purification</keyword><keyword>Sequence Alignment</keyword><keyword>Sequence Homology, Amino Acid</keyword><keyword>Talaromyces/*enzymology/genetics/growth &amp; development</keyword><keyword>*Temperature</keyword><keyword>Trichoderma/*genetics</keyword><keyword>beta-Glucosidase/*chemistry/*genetics/isolation &amp; purification</keyword></keywords><dates><year>2004</year><pub-dates><date>Dec</date></pub-dates></dates><isbn>1046-5928 (Print)&#xD;1046-5928 (Linking)</isbn><accession-num>15555940</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/15555940</url></related-urls></urls><electronic-resource-num>10.1016/j.pep.2004.08.006</electronic-resource-num><language>eng</language></record></Cite></EndNote>�
D<EndNote><Cite><Author>Murray</Author><Year>2004</Year><RecNum>81</RecNum><DisplayText>[41]</DisplayText><record><rec-number>81</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">81</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Murray, P.</author><author>Aro, N.</author><author>Collins, C.</author><author>Grassick, A.</author><author>Penttilä, M.</author><author>Saloheimo, M.</author><author>Tuohy, M.</author></authors></contributors><auth-address>Molecular Glycobiotechnology Group, Department of Biochemistry, National University of Ireland, Galway, Ireland.</auth-address><titles><title><style face="normal" font="default" size="100%">Expression in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> and characterisation of a thermostable family 3 beta-glucosidase from the moderately thermophilic fungus </style><style face="italic" font="default" size="100%">Talaromyces emersonii</style></title><secondary-title>Protein expression and purification</secondary-title><alt-title>Protein Expr Purif</alt-title></titles><periodical><full-title>Protein expression and purification</full-title><abbr-1>Protein Expr Purif</abbr-1></periodical><alt-periodical><full-title>Protein expression and purification</full-title><abbr-1>Protein Expr Purif</abbr-1></alt-periodical><pages>248-57</pages><volume>38</volume><number>2</number><edition>2004/11/24</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Cloning, Molecular</keyword><keyword>Enzyme Stability/physiology</keyword><keyword>*Gene Expression Regulation, Enzymologic</keyword><keyword>Genetic Vectors/genetics</keyword><keyword>Molecular Sequence Data</keyword><keyword>Molecular Weight</keyword><keyword>Recombinant Fusion Proteins/chemistry/genetics/isolation &amp; purification</keyword><keyword>Sequence Alignment</keyword><keyword>Sequence Homology, Amino Acid</keyword><keyword>Talaromyces/*enzymology/genetics/growth &amp; development</keyword><keyword>*Temperature</keyword><keyword>Trichoderma/*genetics</keyword><keyword>beta-Glucosidase/*chemistry/*genetics/isolation &amp; purification</keyword></keywords><dates><year>2004</year><pub-dates><date>Dec</date></pub-dates></dates><isbn>1046-5928 (Print)&#xD;1046-5928 (Linking)</isbn><accession-num>15555940</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/15555940</url></related-urls></urls><electronic-resource-num>10.1016/j.pep.2004.08.006</electronic-resource-num><language>eng</language></record></Cite></EndNote>$$If�7!vh5��5�r
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Fa�7p�(��������RD<EndNote><Cite><Author>Harkki</Author><Year>1989</Year><RecNum>207</RecNum><DisplayText>[19, 20]</DisplayText><record><rec-number>207</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">207</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Harkki, A.</author><author>Uusitalo, J.</author><author>Bailey, M.</author><author>Penttilä, M.</author><author>Knowles, J.K.C.</author></authors></contributors><titles><title><style face="normal" font="default" size="100%">A novel fungal expression system: secretion of active calf chymosin from the filamentous fungus </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Bio/technology</secondary-title></titles><periodical><full-title>Bio/technology</full-title><abbr-1>Biotechnology (N Y)</abbr-1></periodical><pages>596-603</pages><volume>7</volume><dates><year>1989</year></dates><urls></urls></record></Cite><Cite><Author>Uusitalo</Author><Year>1991</Year><RecNum>206</RecNum><record><rec-number>206</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">206</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Uusitalo, J. 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M.</author><author>Nevalainen, K. M.</author><author>Harkki, A. M.</author><author>Knowles, J. K.</author><author>Penttilä, M. 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D<EndNote><Cite><Author>Poidevin</Author><Year>2009</Year><RecNum>220</RecNum><DisplayText>[42]</DisplayText><record><rec-number>220</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">220</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Poidevin, L.</author><author>Levasseur, A.</author><author>Paes, G.</author><author>Navarro, D.</author><author>Heiss-Blanquet, S.</author><author>Asther, M.</author><author>Record, E.</author></authors></contributors><auth-address>IFP, Institut Francais du Petrole, Rueil-Malmaison, France. laetitia.poidevin@esil.univmed.fr</auth-address><titles><title><style face="normal" font="default" size="100%">Heterologous production of the </style><style face="italic" font="default" size="100%">Piromyces equi</style><style face="normal" font="default" size="100%"> cinnamoyl esterase in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> for biotechnological applications</style></title><secondary-title>Letters in applied microbiology</secondary-title><alt-title>Lett Appl Microbiol</alt-title></titles><periodical><full-title>Letters in applied microbiology</full-title><abbr-1>Lett Appl Microbiol</abbr-1></periodical><alt-periodical><full-title>Letters in applied microbiology</full-title><abbr-1>Lett Appl Microbiol</abbr-1></alt-periodical><pages>673-8</pages><volume>49</volume><number>6</number><edition>2009/09/29</edition><keywords><keyword>Aspergillus niger/enzymology</keyword><keyword>Carboxylic Ester Hydrolases/genetics/*metabolism</keyword><keyword>Cloning, Molecular</keyword><keyword>Coumaric Acids/metabolism</keyword><keyword>Fungal Proteins/genetics/*metabolism</keyword><keyword>Hydrogen-Ion Concentration</keyword><keyword>*Industrial Microbiology</keyword><keyword>Piromyces/*enzymology/genetics</keyword><keyword>Recombinant Proteins/genetics/metabolism</keyword><keyword>Substrate Specificity</keyword><keyword>Temperature</keyword><keyword>Trichoderma/genetics/*metabolism</keyword></keywords><dates><year>2009</year><pub-dates><date>Dec</date></pub-dates></dates><isbn>1472-765X (Electronic)&#xD;0266-8254 (Linking)</isbn><accession-num>19780949</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/19780949</url></related-urls></urls><electronic-resource-num>10.1111/j.1472-765X.2009.02734.x</electronic-resource-num><language>eng</language></record></Cite></EndNote>P
D<EndNote><Cite><Author>Poidevin</Author><Year>2009</Year><RecNum>220</RecNum><DisplayText>[42]</DisplayText><record><rec-number>220</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">220</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Poidevin, L.</author><author>Levasseur, A.</author><author>Paes, G.</author><author>Navarro, D.</author><author>Heiss-Blanquet, S.</author><author>Asther, M.</author><author>Record, E.</author></authors></contributors><auth-address>IFP, Institut Francais du Petrole, Rueil-Malmaison, France. laetitia.poidevin@esil.univmed.fr</auth-address><titles><title><style face="normal" font="default" size="100%">Heterologous production of the </style><style face="italic" font="default" size="100%">Piromyces equi</style><style face="normal" font="default" size="100%"> cinnamoyl esterase in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> for biotechnological applications</style></title><secondary-title>Letters in applied microbiology</secondary-title><alt-title>Lett Appl Microbiol</alt-title></titles><periodical><full-title>Letters in applied microbiology</full-title><abbr-1>Lett Appl Microbiol</abbr-1></periodical><alt-periodical><full-title>Letters in applied microbiology</full-title><abbr-1>Lett Appl Microbiol</abbr-1></alt-periodical><pages>673-8</pages><volume>49</volume><number>6</number><edition>2009/09/29</edition><keywords><keyword>Aspergillus niger/enzymology</keyword><keyword>Carboxylic Ester Hydrolases/genetics/*metabolism</keyword><keyword>Cloning, Molecular</keyword><keyword>Coumaric Acids/metabolism</keyword><keyword>Fungal Proteins/genetics/*metabolism</keyword><keyword>Hydrogen-Ion Concentration</keyword><keyword>*Industrial Microbiology</keyword><keyword>Piromyces/*enzymology/genetics</keyword><keyword>Recombinant Proteins/genetics/metabolism</keyword><keyword>Substrate Specificity</keyword><keyword>Temperature</keyword><keyword>Trichoderma/genetics/*metabolism</keyword></keywords><dates><year>2009</year><pub-dates><date>Dec</date></pub-dates></dates><isbn>1472-765X (Electronic)&#xD;0266-8254 (Linking)</isbn><accession-num>19780949</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/19780949</url></related-urls></urls><electronic-resource-num>10.1111/j.1472-765X.2009.02734.x</electronic-resource-num><language>eng</language></record></Cite></EndNote>$$If�7!vh5��5�r
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D<EndNote><Cite><Author>Kontkanen</Author><Year>2009</Year><RecNum>298</RecNum><DisplayText>[43]</DisplayText><record><rec-number>298</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">298</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kontkanen, H.</author><author>Westerholm-Parvinen, A.</author><author>Saloheimo, M.</author><author>Bailey, M.</author><author>Rättö, M.</author><author>Mattila, I.</author><author>Mohsina, M.</author><author>Kalkkinen, N.</author><author>Nakari-Setälä, T.</author><author>Buchert, J.</author></authors></contributors><auth-address>VTT, P.O. Box 1000, FI-02044 Espoo, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Novel </style><style face="italic" font="default" size="100%">Coprinopsis cinerea</style><style face="normal" font="default" size="100%"> polyesterase that hydrolyzes cutin and suberin</style></title><secondary-title>Applied and environmental microbiology</secondary-title><alt-title>Appl Environ Microbiol</alt-title></titles><periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></periodical><alt-periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></alt-periodical><pages>2148-57</pages><volume>75</volume><number>7</number><edition>2009/02/10</edition><keywords><keyword>Agaricales/*enzymology/*genetics</keyword><keyword>Butyrates/metabolism</keyword><keyword>Chromatography, Affinity</keyword><keyword>Cloning, Molecular</keyword><keyword>DNA, Fungal/chemistry/genetics</keyword><keyword>Enzyme Stability</keyword><keyword>Gene Expression</keyword><keyword>Hydrogen-Ion Concentration</keyword><keyword>Hydrolases/chemistry/*genetics/isolation &amp; purification/*metabolism</keyword><keyword>Kinetics</keyword><keyword>*Lipids</keyword><keyword>Membrane Lipids/*metabolism</keyword><keyword>Molecular Sequence Data</keyword><keyword>Molecular Weight</keyword><keyword>Sequence Analysis, DNA</keyword><keyword>Substrate Specificity</keyword><keyword>Temperature</keyword><keyword>Trichoderma/genetics</keyword></keywords><dates><year>2009</year><pub-dates><date>Apr</date></pub-dates></dates><isbn>1098-5336 (Electronic)&#xD;0099-2240 (Linking)</isbn><accession-num>19201950</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/19201950</url></related-urls></urls><custom2>2663218</custom2><electronic-resource-num>10.1128/AEM.02103-08</electronic-resource-num><language>eng</language></record></Cite></EndNote>�
D<EndNote><Cite><Author>Kontkanen</Author><Year>2009</Year><RecNum>298</RecNum><DisplayText>[43]</DisplayText><record><rec-number>298</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">298</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kontkanen, H.</author><author>Westerholm-Parvinen, A.</author><author>Saloheimo, M.</author><author>Bailey, M.</author><author>Rättö, M.</author><author>Mattila, I.</author><author>Mohsina, M.</author><author>Kalkkinen, N.</author><author>Nakari-Setälä, T.</author><author>Buchert, J.</author></authors></contributors><auth-address>VTT, P.O. Box 1000, FI-02044 Espoo, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Novel </style><style face="italic" font="default" size="100%">Coprinopsis cinerea</style><style face="normal" font="default" size="100%"> polyesterase that hydrolyzes cutin and suberin</style></title><secondary-title>Applied and environmental microbiology</secondary-title><alt-title>Appl Environ Microbiol</alt-title></titles><periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></periodical><alt-periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></alt-periodical><pages>2148-57</pages><volume>75</volume><number>7</number><edition>2009/02/10</edition><keywords><keyword>Agaricales/*enzymology/*genetics</keyword><keyword>Butyrates/metabolism</keyword><keyword>Chromatography, Affinity</keyword><keyword>Cloning, Molecular</keyword><keyword>DNA, Fungal/chemistry/genetics</keyword><keyword>Enzyme Stability</keyword><keyword>Gene Expression</keyword><keyword>Hydrogen-Ion Concentration</keyword><keyword>Hydrolases/chemistry/*genetics/isolation &amp; purification/*metabolism</keyword><keyword>Kinetics</keyword><keyword>*Lipids</keyword><keyword>Membrane Lipids/*metabolism</keyword><keyword>Molecular Sequence Data</keyword><keyword>Molecular Weight</keyword><keyword>Sequence Analysis, DNA</keyword><keyword>Substrate Specificity</keyword><keyword>Temperature</keyword><keyword>Trichoderma/genetics</keyword></keywords><dates><year>2009</year><pub-dates><date>Apr</date></pub-dates></dates><isbn>1098-5336 (Electronic)&#xD;0099-2240 (Linking)</isbn><accession-num>19201950</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/19201950</url></related-urls></urls><custom2>2663218</custom2><electronic-resource-num>10.1128/AEM.02103-08</electronic-resource-num><language>eng</language></record></Cite></EndNote>$$If�7!vh5��5�r
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D<EndNote><Cite><Author>Schmoll</Author><Year>2010</Year><RecNum>129</RecNum><DisplayText>[44]</DisplayText><record><rec-number>129</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">129</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Schmoll, M.</author><author>Seibel, C.</author><author>Kotlowski, C.</author><author>Wollert Genannt Vendt, F.</author><author>Liebmann, B.</author><author>Kubicek, C. P.</author></authors></contributors><auth-address>Research Area Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, 1060, Wien, Austria. mschmoll@mail.zserv.tuwien.ac.at</auth-address><titles><title><style face="normal" font="default" size="100%">Recombinant production of an </style><style face="italic" font="default" size="100%">Aspergillus nidulans</style><style face="normal" font="default" size="100%"> class I hydrophobin (DewA) in </style><style face="italic" font="default" size="100%">Hypocrea jecorina</style><style face="normal" font="default" size="100%"> (</style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%">) is promoter-dependent</style></title><secondary-title>Applied microbiology and biotechnology</secondary-title><alt-title>Appl Microbiol Biotechnol</alt-title></titles><periodical><full-title>Applied microbiology and biotechnology</full-title><abbr-1>Appl Microbiol Biotechnol</abbr-1></periodical><alt-periodical><full-title>Applied microbiology and biotechnology</full-title><abbr-1>Appl Microbiol Biotechnol</abbr-1></alt-periodical><pages>95-103</pages><volume>88</volume><number>1</number><edition>2010/06/23</edition><keywords><keyword>Aspergillus nidulans/*genetics</keyword><keyword>Carbon/metabolism</keyword><keyword>Culture Media/chemistry</keyword><keyword>Fungal Proteins/*biosynthesis/genetics</keyword><keyword>*Gene Expression</keyword><keyword>Lactose/metabolism</keyword><keyword>*Promoter Regions, Genetic</keyword><keyword>Recombinant Proteins/genetics/metabolism</keyword><keyword>Sequence Analysis, Protein</keyword><keyword>Trichoderma/genetics/*metabolism</keyword></keywords><dates><year>2010</year><pub-dates><date>Sep</date></pub-dates></dates><isbn>1432-0614 (Electronic)&#xD;0175-7598 (Linking)</isbn><accession-num>20567818</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/20567818</url></related-urls></urls><electronic-resource-num>10.1007/s00253-010-2710-4</electronic-resource-num><language>eng</language></record></Cite></EndNote>�
D<EndNote><Cite><Author>Schmoll</Author><Year>2010</Year><RecNum>129</RecNum><DisplayText>[44]</DisplayText><record><rec-number>129</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">129</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Schmoll, M.</author><author>Seibel, C.</author><author>Kotlowski, C.</author><author>Wollert Genannt Vendt, F.</author><author>Liebmann, B.</author><author>Kubicek, C. P.</author></authors></contributors><auth-address>Research Area Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, 1060, Wien, Austria. mschmoll@mail.zserv.tuwien.ac.at</auth-address><titles><title><style face="normal" font="default" size="100%">Recombinant production of an </style><style face="italic" font="default" size="100%">Aspergillus nidulans</style><style face="normal" font="default" size="100%"> class I hydrophobin (DewA) in </style><style face="italic" font="default" size="100%">Hypocrea jecorina</style><style face="normal" font="default" size="100%"> (</style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%">) is promoter-dependent</style></title><secondary-title>Applied microbiology and biotechnology</secondary-title><alt-title>Appl Microbiol Biotechnol</alt-title></titles><periodical><full-title>Applied microbiology and biotechnology</full-title><abbr-1>Appl Microbiol Biotechnol</abbr-1></periodical><alt-periodical><full-title>Applied microbiology and biotechnology</full-title><abbr-1>Appl Microbiol Biotechnol</abbr-1></alt-periodical><pages>95-103</pages><volume>88</volume><number>1</number><edition>2010/06/23</edition><keywords><keyword>Aspergillus nidulans/*genetics</keyword><keyword>Carbon/metabolism</keyword><keyword>Culture Media/chemistry</keyword><keyword>Fungal Proteins/*biosynthesis/genetics</keyword><keyword>*Gene Expression</keyword><keyword>Lactose/metabolism</keyword><keyword>*Promoter Regions, Genetic</keyword><keyword>Recombinant Proteins/genetics/metabolism</keyword><keyword>Sequence Analysis, Protein</keyword><keyword>Trichoderma/genetics/*metabolism</keyword></keywords><dates><year>2010</year><pub-dates><date>Sep</date></pub-dates></dates><isbn>1432-0614 (Electronic)&#xD;0175-7598 (Linking)</isbn><accession-num>20567818</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/20567818</url></related-urls></urls><electronic-resource-num>10.1007/s00253-010-2710-4</electronic-resource-num><language>eng</language></record></Cite></EndNote>$$If�7!vh5��5�r
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Fa�7p�(���������	D<EndNote><Cite><Author>Margolles-Clark</Author><Year>1996</Year><RecNum>222</RecNum><DisplayText>[45]</DisplayText><record><rec-number>222</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">222</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Margolles-Clark, E.</author><author>Hayes, C. K.</author><author>Harman, G. E.</author><author>Penttilä, M.</author></authors></contributors><auth-address>VTT Biotechnology and Food Research, Espoo, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Improved production of </style><style face="italic" font="default" size="100%">Trichoderma harzianum</style><style face="normal" font="default" size="100%"> endochitinase by expression in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Applied and environmental microbiology</secondary-title><alt-title>Appl Environ Microbiol</alt-title></titles><periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></periodical><alt-periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></alt-periodical><pages>2145-51</pages><volume>62</volume><number>6</number><edition>1996/06/01</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Base Sequence</keyword><keyword>Chitinase/*biosynthesis/genetics/metabolism</keyword><keyword>Culture Media</keyword><keyword>DNA Primers/genetics</keyword><keyword>DNA, Fungal/genetics</keyword><keyword>Enzyme Stability</keyword><keyword>Gene Expression</keyword><keyword>Genes, Fungal</keyword><keyword>Molecular Sequence Data</keyword><keyword>Promoter Regions, Genetic</keyword><keyword>Protein Processing, Post-Translational</keyword><keyword>Protein Sorting Signals/genetics</keyword><keyword>Transformation, Genetic</keyword><keyword>Trichoderma/*enzymology/genetics/growth &amp; development</keyword></keywords><dates><year>1996</year><pub-dates><date>Jun</date></pub-dates></dates><isbn>0099-2240 (Print)&#xD;0099-2240 (Linking)</isbn><accession-num>8787411</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/8787411</url></related-urls></urls><custom2>167992</custom2><language>eng</language></record></Cite></EndNote>�	D<EndNote><Cite><Author>Margolles-Clark</Author><Year>1996</Year><RecNum>222</RecNum><DisplayText>[45]</DisplayText><record><rec-number>222</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">222</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Margolles-Clark, E.</author><author>Hayes, C. K.</author><author>Harman, G. E.</author><author>Penttilä, M.</author></authors></contributors><auth-address>VTT Biotechnology and Food Research, Espoo, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Improved production of </style><style face="italic" font="default" size="100%">Trichoderma harzianum</style><style face="normal" font="default" size="100%"> endochitinase by expression in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Applied and environmental microbiology</secondary-title><alt-title>Appl Environ Microbiol</alt-title></titles><periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></periodical><alt-periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></alt-periodical><pages>2145-51</pages><volume>62</volume><number>6</number><edition>1996/06/01</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Base Sequence</keyword><keyword>Chitinase/*biosynthesis/genetics/metabolism</keyword><keyword>Culture Media</keyword><keyword>DNA Primers/genetics</keyword><keyword>DNA, Fungal/genetics</keyword><keyword>Enzyme Stability</keyword><keyword>Gene Expression</keyword><keyword>Genes, Fungal</keyword><keyword>Molecular Sequence Data</keyword><keyword>Promoter Regions, Genetic</keyword><keyword>Protein Processing, Post-Translational</keyword><keyword>Protein Sorting Signals/genetics</keyword><keyword>Transformation, Genetic</keyword><keyword>Trichoderma/*enzymology/genetics/growth &amp; development</keyword></keywords><dates><year>1996</year><pub-dates><date>Jun</date></pub-dates></dates><isbn>0099-2240 (Print)&#xD;0099-2240 (Linking)</isbn><accession-num>8787411</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/8787411</url></related-urls></urls><custom2>167992</custom2><language>eng</language></record></Cite></EndNote>$$If�7!vh5��5�r
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Fa�7p�(���������D<EndNote><Cite><Author>Joutsjoki</Author><Year>1993</Year><RecNum>226</RecNum><DisplayText>[47, 48]</DisplayText><record><rec-number>226</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">226</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Joutsjoki, V. V.</author><author>Torkkeli, T. K.</author><author>Nevalainen, K. M.</author></authors></contributors><auth-address>Research Laboratories, Alko Ltd., Helsinki, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Transformation of </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> with the </style><style face="italic" font="default" size="100%">Hormoconis resinae</style><style face="normal" font="default" size="100%"> glucoamylase P (</style><style face="italic" font="default" size="100%">gamP</style><style face="normal" font="default" size="100%">) gene: production of a heterologous glucoamylase by </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Current genetics</secondary-title><alt-title>Curr Genet</alt-title></titles><periodical><full-title>Current genetics</full-title><abbr-1>Curr Genet</abbr-1></periodical><alt-periodical><full-title>Current genetics</full-title><abbr-1>Curr Genet</abbr-1></alt-periodical><pages>223-8</pages><volume>24</volume><number>3</number><edition>1993/09/01</edition><keywords><keyword>Blotting, Northern</keyword><keyword>Blotting, Southern</keyword><keyword>Blotting, Western</keyword><keyword>Cloning, Molecular</keyword><keyword>Glucan 1,4-alpha-Glucosidase/biosynthesis/*genetics</keyword><keyword>Kinetics</keyword><keyword>Mitosporic Fungi/enzymology/*genetics</keyword><keyword>Promoter Regions, Genetic</keyword><keyword>Terminator Regions, Genetic</keyword><keyword>*Transformation, Genetic</keyword><keyword>Trichoderma/*genetics</keyword></keywords><dates><year>1993</year><pub-dates><date>Sep</date></pub-dates></dates><isbn>0172-8083 (Print)&#xD;0172-8083 (Linking)</isbn><accession-num>8221931</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/8221931</url></related-urls></urls><language>eng</language></record></Cite><Cite><Author>Joutsjoki</Author><Year>1993</Year><RecNum>225</RecNum><record><rec-number>225</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">225</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Joutsjoki, V. V.</author><author>Kuittinen, M.</author><author>Torkkeli, T. K.</author><author>Suominen, P. L.</author></authors></contributors><auth-address>Research Laboratories, Alko Ltd., Helsinki, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Secretion of the </style><style face="italic" font="default" size="100%">Hormoconis resinae</style><style face="normal" font="default" size="100%"> glucoamylase P enzyme from </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> directed by the natural and the </style><style face="italic" font="default" size="100%">cbh1</style><style face="normal" font="default" size="100%"> gene secretion signal</style></title><secondary-title>FEMS microbiology letters</secondary-title><alt-title>FEMS Microbiol Lett</alt-title></titles><periodical><full-title>FEMS microbiology letters</full-title><abbr-1>FEMS Microbiol Lett</abbr-1></periodical><alt-periodical><full-title>FEMS microbiology letters</full-title><abbr-1>FEMS Microbiol Lett</abbr-1></alt-periodical><pages>281-6</pages><volume>112</volume><number>3</number><edition>1993/09/15</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Base Sequence</keyword><keyword>Biological Transport</keyword><keyword>Cellulose 1,4-beta-Cellobiosidase</keyword><keyword>Glucan 1,4-alpha-Glucosidase/genetics/*secretion</keyword><keyword>Glycoside Hydrolases/*genetics</keyword><keyword>Mitosporic Fungi/*genetics</keyword><keyword>Molecular Sequence Data</keyword><keyword>Protein Sorting Signals/*genetics</keyword><keyword>Recombinant Fusion Proteins/secretion</keyword><keyword>Trichoderma/genetics</keyword></keywords><dates><year>1993</year><pub-dates><date>Sep 15</date></pub-dates></dates><isbn>0378-1097 (Print)&#xD;0378-1097 (Linking)</isbn><accession-num>8224791</accession-num><work-type>Comparative Study</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/8224791</url></related-urls></urls><language>eng</language></record></Cite></EndNote>�D<EndNote><Cite><Author>Joutsjoki</Author><Year>1993</Year><RecNum>226</RecNum><DisplayText>[47, 48]</DisplayText><record><rec-number>226</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">226</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Joutsjoki, V. V.</author><author>Torkkeli, T. K.</author><author>Nevalainen, K. M.</author></authors></contributors><auth-address>Research Laboratories, Alko Ltd., Helsinki, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Transformation of </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> with the </style><style face="italic" font="default" size="100%">Hormoconis resinae</style><style face="normal" font="default" size="100%"> glucoamylase P (</style><style face="italic" font="default" size="100%">gamP</style><style face="normal" font="default" size="100%">) gene: production of a heterologous glucoamylase by </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Current genetics</secondary-title><alt-title>Curr Genet</alt-title></titles><periodical><full-title>Current genetics</full-title><abbr-1>Curr Genet</abbr-1></periodical><alt-periodical><full-title>Current genetics</full-title><abbr-1>Curr Genet</abbr-1></alt-periodical><pages>223-8</pages><volume>24</volume><number>3</number><edition>1993/09/01</edition><keywords><keyword>Blotting, Northern</keyword><keyword>Blotting, Southern</keyword><keyword>Blotting, Western</keyword><keyword>Cloning, Molecular</keyword><keyword>Glucan 1,4-alpha-Glucosidase/biosynthesis/*genetics</keyword><keyword>Kinetics</keyword><keyword>Mitosporic Fungi/enzymology/*genetics</keyword><keyword>Promoter Regions, Genetic</keyword><keyword>Terminator Regions, Genetic</keyword><keyword>*Transformation, Genetic</keyword><keyword>Trichoderma/*genetics</keyword></keywords><dates><year>1993</year><pub-dates><date>Sep</date></pub-dates></dates><isbn>0172-8083 (Print)&#xD;0172-8083 (Linking)</isbn><accession-num>8221931</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/8221931</url></related-urls></urls><language>eng</language></record></Cite><Cite><Author>Joutsjoki</Author><Year>1993</Year><RecNum>225</RecNum><record><rec-number>225</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">225</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Joutsjoki, V. V.</author><author>Kuittinen, M.</author><author>Torkkeli, T. K.</author><author>Suominen, P. L.</author></authors></contributors><auth-address>Research Laboratories, Alko Ltd., Helsinki, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Secretion of the </style><style face="italic" font="default" size="100%">Hormoconis resinae</style><style face="normal" font="default" size="100%"> glucoamylase P enzyme from </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> directed by the natural and the </style><style face="italic" font="default" size="100%">cbh1</style><style face="normal" font="default" size="100%"> gene secretion signal</style></title><secondary-title>FEMS microbiology letters</secondary-title><alt-title>FEMS Microbiol Lett</alt-title></titles><periodical><full-title>FEMS microbiology letters</full-title><abbr-1>FEMS Microbiol Lett</abbr-1></periodical><alt-periodical><full-title>FEMS microbiology letters</full-title><abbr-1>FEMS Microbiol Lett</abbr-1></alt-periodical><pages>281-6</pages><volume>112</volume><number>3</number><edition>1993/09/15</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Base Sequence</keyword><keyword>Biological Transport</keyword><keyword>Cellulose 1,4-beta-Cellobiosidase</keyword><keyword>Glucan 1,4-alpha-Glucosidase/genetics/*secretion</keyword><keyword>Glycoside Hydrolases/*genetics</keyword><keyword>Mitosporic Fungi/*genetics</keyword><keyword>Molecular Sequence Data</keyword><keyword>Protein Sorting Signals/*genetics</keyword><keyword>Recombinant Fusion Proteins/secretion</keyword><keyword>Trichoderma/genetics</keyword></keywords><dates><year>1993</year><pub-dates><date>Sep 15</date></pub-dates></dates><isbn>0378-1097 (Print)&#xD;0378-1097 (Linking)</isbn><accession-num>8224791</accession-num><work-type>Comparative Study</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/8224791</url></related-urls></urls><language>eng</language></record></Cite></EndNote>$$If�7!vh5��5�r
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Fa�7p�(��������zD<EndNote><Cite><Author>Kiiskinen</Author><Year>2004</Year><RecNum>79</RecNum><DisplayText>[50]</DisplayText><record><rec-number>79</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">79</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kiiskinen, L. L.</author><author>Kruus, K.</author><author>Bailey, M.</author><author>Ylösmäki, E.</author><author>Siika-Aho, M.</author><author>Saloheimo, M.</author></authors></contributors><auth-address>VTT Biotechnology, PO Box 1500, Fin-02044 VTT, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Expression of </style><style face="italic" font="default" size="100%">Melanocarpus albomyces</style><style face="normal" font="default" size="100%"> laccase in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> and characterization of the purified enzyme</style></title><secondary-title>Microbiology</secondary-title><alt-title>Microbiology</alt-title></titles><periodical><full-title>Microbiology</full-title><abbr-1>Microbiology</abbr-1></periodical><alt-periodical><full-title>Microbiology</full-title><abbr-1>Microbiology</abbr-1></alt-periodical><pages>3065-74</pages><volume>150</volume><number>Pt 9</number><edition>2004/09/07</edition><keywords><keyword>Cellulose 1,4-beta-Cellobiosidase/metabolism</keyword><keyword>Cloning, Molecular</keyword><keyword>Culture Media/chemistry</keyword><keyword>Enzyme Stability</keyword><keyword>Fermentation</keyword><keyword>Fungal Proteins/genetics/metabolism</keyword><keyword>Gene Expression</keyword><keyword>Hydrogen-Ion Concentration</keyword><keyword>Laccase/genetics/*isolation &amp; purification/*metabolism</keyword><keyword>Molecular Weight</keyword><keyword>Papain/metabolism</keyword><keyword>Promoter Regions, Genetic</keyword><keyword>RNA, Fungal/analysis/isolation &amp; purification</keyword><keyword>RNA, Messenger/analysis/isolation &amp; purification</keyword><keyword>Recombinant Fusion Proteins/genetics/isolation &amp; purification/metabolism</keyword><keyword>Recombinant Proteins/genetics/isolation &amp; purification/metabolism</keyword><keyword>Sordariales/*enzymology/genetics</keyword><keyword>Substrate Specificity</keyword><keyword>Temperature</keyword><keyword>Trichoderma/*genetics/metabolism</keyword></keywords><dates><year>2004</year><pub-dates><date>Sep</date></pub-dates></dates><isbn>1350-0872 (Print)&#xD;1350-0872 (Linking)</isbn><accession-num>15347764</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/15347764</url></related-urls></urls><electronic-resource-num>10.1099/mic.0.27147-0</electronic-resource-num><language>eng</language></record></Cite></EndNote>zD<EndNote><Cite><Author>Kiiskinen</Author><Year>2004</Year><RecNum>79</RecNum><DisplayText>[50]</DisplayText><record><rec-number>79</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">79</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kiiskinen, L. 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Fa�7p�(��������4D<EndNote><Cite><Author>Kontkanen</Author><Year>2006</Year><RecNum>136</RecNum><DisplayText>[51, 52]</DisplayText><record><rec-number>136</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">136</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kontkanen, H.</author><author>Reinikainen, T.</author><author>Saloheimo, M.</author></authors></contributors><auth-address>VTT, P.O. Box 1000, FIN-02044 VTT, Finland. hanna.kontkanen@vtt.fi</auth-address><titles><title><style face="normal" font="default" size="100%">Cloning and expression of a </style><style face="italic" font="default" size="100%">Melanocarpus albomyces</style><style face="normal" font="default" size="100%"> steryl esterase gene in </style><style face="italic" font="default" size="100%">Pichia pastoris</style><style face="normal" font="default" size="100%"> and </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Biotechnology and bioengineering</secondary-title><alt-title>Biotechnol Bioeng</alt-title></titles><periodical><full-title>Biotechnology and bioengineering</full-title><abbr-1>Biotechnol Bioeng</abbr-1></periodical><alt-periodical><full-title>Biotechnology and bioengineering</full-title><abbr-1>Biotechnol Bioeng</abbr-1></alt-periodical><pages>407-15</pages><volume>94</volume><number>3</number><edition>2006/04/15</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Cloning, Molecular</keyword><keyword>Cytoplasm/enzymology/genetics</keyword><keyword>Esterases/biosynthesis/chemistry/*genetics</keyword><keyword>Fungal Proteins/biosynthesis/chemistry/*genetics</keyword><keyword>*Gene Expression</keyword><keyword>Molecular Sequence Data</keyword><keyword>Pichia/enzymology/*genetics</keyword><keyword>Protein Precursors/biosynthesis/chemistry/*genetics</keyword><keyword>Protein Sorting Signals/genetics</keyword><keyword>Recombinant Proteins/biosynthesis/genetics</keyword><keyword>Trichoderma/enzymology/*genetics</keyword></keywords><dates><year>2006</year><pub-dates><date>Jun 20</date></pub-dates></dates><isbn>0006-3592 (Print)&#xD;0006-3592 (Linking)</isbn><accession-num>16615142</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/16615142</url></related-urls></urls><electronic-resource-num>10.1002/bit.20686</electronic-resource-num><language>eng</language></record></Cite><Cite><Author>Kontkanen</Author><Year>2006</Year><RecNum>137</RecNum><record><rec-number>137</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">137</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kontkanen, H.</author><author>Saloheimo, M.</author><author>Pere, J.</author><author>Miettinen-Oinonen, A.</author><author>Reinikainen, T.</author></authors></contributors><auth-address>VTT Biotechnology, PO Box 1500, 02044 VTT, Espoo, Finland. hanna.kontkanen@vtt.fi</auth-address><titles><title><style face="normal" font="default" size="100%">Characterization of </style><style face="italic" font="default" size="100%">Melanocarpus albomyces</style><style face="normal" font="default" size="100%"> steryl esterase produced in </style><style face="italic" font="default" size="100%">Trichoderma reesei </style><style face="normal" font="default" size="100%">and modification of fibre products with the enzyme</style></title><secondary-title>Applied microbiology and biotechnology</secondary-title><alt-title>Appl Microbiol Biotechnol</alt-title></titles><periodical><full-title>Applied microbiology and biotechnology</full-title><abbr-1>Appl Microbiol Biotechnol</abbr-1></periodical><alt-periodical><full-title>Applied microbiology and biotechnology</full-title><abbr-1>Appl Microbiol Biotechnol</abbr-1></alt-periodical><pages>696-704</pages><volume>72</volume><number>4</number><edition>2006/02/14</edition><keywords><keyword>Cloning, Molecular</keyword><keyword>Esterases/chemistry/genetics/*metabolism</keyword><keyword>Fungal Proteins/biosynthesis/chemistry/*genetics</keyword><keyword>Polyesters/*metabolism</keyword><keyword>Recombinant Fusion Proteins/genetics/isolation &amp; purification/metabolism</keyword><keyword>Sordariales/*enzymology/genetics</keyword><keyword>Trichoderma/genetics</keyword></keywords><dates><year>2006</year><pub-dates><date>Oct</date></pub-dates></dates><isbn>0175-7598 (Print)&#xD;0175-7598 (Linking)</isbn><accession-num>16470365</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/16470365</url></related-urls></urls><electronic-resource-num>10.1007/s00253-006-0321-x</electronic-resource-num><language>eng</language></record></Cite></EndNote>4D<EndNote><Cite><Author>Kontkanen</Author><Year>2006</Year><RecNum>136</RecNum><DisplayText>[51, 52]</DisplayText><record><rec-number>136</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">136</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kontkanen, H.</author><author>Reinikainen, T.</author><author>Saloheimo, M.</author></authors></contributors><auth-address>VTT, P.O. 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Fa�7p�(���������D<EndNote><Cite><Author>Salles</Author><Year>2007</Year><RecNum>240</RecNum><DisplayText>[54]</DisplayText><record><rec-number>240</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">240</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Salles, B. C.</author><author>Te&apos;o, V. S.</author><author>Gibbs, M. D.</author><author>Bergquist, P. L.</author><author>Filho, E. X.</author><author>Ximenes, E. A.</author><author>Nevalainen, K. M.</author></authors></contributors><auth-address>Laboratorio de Enzimologia, Departamento de Biologia Celular, Universidade de Brasilia, Brasilia, Brazil. cobucci@stanford.edu</auth-address><titles><title><style face="normal" font="default" size="100%">Identification of two novel xylanase-encoding genes (</style><style face="italic" font="default" size="100%">xyn5</style><style face="normal" font="default" size="100%"> and </style><style face="italic" font="default" size="100%">xyn6</style><style face="normal" font="default" size="100%">) from </style><style face="italic" font="default" size="100%">Acrophialophora nainiana</style><style face="normal" font="default" size="100%"> and heterologous expression of </style><style face="italic" font="default" size="100%">xyn6</style><style face="normal" font="default" size="100%"> in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Biotechnology letters</secondary-title><alt-title>Biotechnol Lett</alt-title></titles><periodical><full-title>Biotechnology letters</full-title><abbr-1>Biotechnol Lett</abbr-1></periodical><alt-periodical><full-title>Biotechnology letters</full-title><abbr-1>Biotechnol Lett</abbr-1></alt-periodical><pages>1195-201</pages><volume>29</volume><number>8</number><edition>2007/05/10</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Ascomycota/*metabolism</keyword><keyword>Binding Sites</keyword><keyword>Cloning, Molecular</keyword><keyword>Densitometry/methods</keyword><keyword>Endo-1,4-beta Xylanases/*chemistry/metabolism</keyword><keyword>Escherichia coli/metabolism</keyword><keyword>*Gene Expression Regulation, Enzymologic</keyword><keyword>*Gene Expression Regulation, Fungal</keyword><keyword>Introns</keyword><keyword>Molecular Sequence Data</keyword><keyword>Mutagenesis, Site-Directed</keyword><keyword>Oligonucleotides/chemistry</keyword><keyword>Open Reading Frames</keyword><keyword>Trichoderma/*enzymology/metabolism</keyword></keywords><dates><year>2007</year><pub-dates><date>Aug</date></pub-dates></dates><isbn>0141-5492 (Print)&#xD;0141-5492 (Linking)</isbn><accession-num>17487548</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/17487548</url></related-urls></urls><electronic-resource-num>10.1007/s10529-007-9380-z</electronic-resource-num><language>eng</language></record></Cite></EndNote>�D<EndNote><Cite><Author>Salles</Author><Year>2007</Year><RecNum>240</RecNum><DisplayText>[54]</DisplayText><record><rec-number>240</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">240</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Salles, B. 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M.</author></authors></contributors><auth-address>Laboratorio de Enzimologia, Departamento de Biologia Celular, Universidade de Brasilia, Brasilia, Brazil. cobucci@stanford.edu</auth-address><titles><title><style face="normal" font="default" size="100%">Identification of two novel xylanase-encoding genes (</style><style face="italic" font="default" size="100%">xyn5</style><style face="normal" font="default" size="100%"> and </style><style face="italic" font="default" size="100%">xyn6</style><style face="normal" font="default" size="100%">) from </style><style face="italic" font="default" size="100%">Acrophialophora nainiana</style><style face="normal" font="default" size="100%"> and heterologous expression of </style><style face="italic" font="default" size="100%">xyn6</style><style face="normal" font="default" size="100%"> in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Biotechnology letters</secondary-title><alt-title>Biotechnol Lett</alt-title></titles><periodical><full-title>Biotechnology letters</full-title><abbr-1>Biotechnol Lett</abbr-1></periodical><alt-periodical><full-title>Biotechnology letters</full-title><abbr-1>Biotechnol Lett</abbr-1></alt-periodical><pages>1195-201</pages><volume>29</volume><number>8</number><edition>2007/05/10</edition><keywords><keyword>Amino Acid Sequence</keyword><keyword>Ascomycota/*metabolism</keyword><keyword>Binding Sites</keyword><keyword>Cloning, Molecular</keyword><keyword>Densitometry/methods</keyword><keyword>Endo-1,4-beta Xylanases/*chemistry/metabolism</keyword><keyword>Escherichia coli/metabolism</keyword><keyword>*Gene Expression Regulation, Enzymologic</keyword><keyword>*Gene Expression Regulation, Fungal</keyword><keyword>Introns</keyword><keyword>Molecular Sequence Data</keyword><keyword>Mutagenesis, Site-Directed</keyword><keyword>Oligonucleotides/chemistry</keyword><keyword>Open Reading Frames</keyword><keyword>Trichoderma/*enzymology/metabolism</keyword></keywords><dates><year>2007</year><pub-dates><date>Aug</date></pub-dates></dates><isbn>0141-5492 (Print)&#xD;0141-5492 (Linking)</isbn><accession-num>17487548</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/17487548</url></related-urls></urls><electronic-resource-num>10.1007/s10529-007-9380-z</electronic-resource-num><language>eng</language></record></Cite></EndNote>�$$If�7!vh5��5�r
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Fa�7p�(��������<	D<EndNote><Cite><Author>Paloheimo</Author><Year>2003</Year><RecNum>241</RecNum><DisplayText>[55]</DisplayText><record><rec-number>241</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">241</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Paloheimo, M.</author><author>Mäntylä, A.</author><author>Kallio, J.</author><author>Suominen, P.</author></authors></contributors><auth-address>Roal Oy, FIN-05201 Rajamaki, Finland. marja.paloheimo@roal.fi</auth-address><titles><title><style face="normal" font="default" size="100%">High-yield production of a bacterial xylanase in the filamentous fungus </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> requires a carrier polypeptide with an intact domain structure</style></title><secondary-title>Applied and environmental microbiology</secondary-title><alt-title>Appl Environ Microbiol</alt-title></titles><periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></periodical><alt-periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></alt-periodical><pages>7073-82</pages><volume>69</volume><number>12</number><edition>2003/12/09</edition><keywords><keyword>Actinomycetales/*enzymology/genetics</keyword><keyword>Biotechnology/methods</keyword><keyword>Cellulose 1,4-beta-Cellobiosidase/chemistry/genetics/*metabolism</keyword><keyword>Endo-1,4-beta Xylanases/genetics/*metabolism</keyword><keyword>Gene Expression Regulation, Fungal</keyword><keyword>Peptides/chemistry/genetics/*metabolism</keyword><keyword>Recombinant Fusion Proteins/genetics/metabolism</keyword><keyword>Trichoderma/*enzymology/genetics</keyword><keyword>beta-Mannosidase/chemistry/genetics/*metabolism</keyword></keywords><dates><year>2003</year><pub-dates><date>Dec</date></pub-dates></dates><isbn>0099-2240 (Print)&#xD;0099-2240 (Linking)</isbn><accession-num>14660351</accession-num><work-type>Evaluation Studies</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/14660351</url></related-urls></urls><custom2>309970</custom2><language>eng</language></record></Cite></EndNote><	D<EndNote><Cite><Author>Paloheimo</Author><Year>2003</Year><RecNum>241</RecNum><DisplayText>[55]</DisplayText><record><rec-number>241</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">241</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Paloheimo, M.</author><author>Mäntylä, A.</author><author>Kallio, J.</author><author>Suominen, P.</author></authors></contributors><auth-address>Roal Oy, FIN-05201 Rajamaki, Finland. marja.paloheimo@roal.fi</auth-address><titles><title><style face="normal" font="default" size="100%">High-yield production of a bacterial xylanase in the filamentous fungus </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> requires a carrier polypeptide with an intact domain structure</style></title><secondary-title>Applied and environmental microbiology</secondary-title><alt-title>Appl Environ Microbiol</alt-title></titles><periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></periodical><alt-periodical><full-title>Applied and environmental microbiology</full-title><abbr-1>Appl Environ Microbiol</abbr-1></alt-periodical><pages>7073-82</pages><volume>69</volume><number>12</number><edition>2003/12/09</edition><keywords><keyword>Actinomycetales/*enzymology/genetics</keyword><keyword>Biotechnology/methods</keyword><keyword>Cellulose 1,4-beta-Cellobiosidase/chemistry/genetics/*metabolism</keyword><keyword>Endo-1,4-beta Xylanases/genetics/*metabolism</keyword><keyword>Gene Expression Regulation, Fungal</keyword><keyword>Peptides/chemistry/genetics/*metabolism</keyword><keyword>Recombinant Fusion Proteins/genetics/metabolism</keyword><keyword>Trichoderma/*enzymology/genetics</keyword><keyword>beta-Mannosidase/chemistry/genetics/*metabolism</keyword></keywords><dates><year>2003</year><pub-dates><date>Dec</date></pub-dates></dates><isbn>0099-2240 (Print)&#xD;0099-2240 (Linking)</isbn><accession-num>14660351</accession-num><work-type>Evaluation Studies</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/14660351</url></related-urls></urls><custom2>309970</custom2><language>eng</language></record></Cite></EndNote>$$If�7!vh5��5�r
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