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Trichoderma as whole-cell catalyst and recombinant protein production host

Rita Gorsche, Robert L. Mach, Astrid R. Mach-Aigner*

Department for Biotechnology and Microbiology, Institute of Chemical Engineering, Vienna University of Technology, Gumpendorfer Str. 1a, A-1060 Wien, Austria

* Corresponding author: 	Tel.: +43 1 58801 166558
	Fax: +43 1 58801 17299
	E-mail: HYPERLINK "mailto:astrid.mach-aigner@tuwien.ac.at"astrid.mach-aigner@tuwien.ac.at
Abstract
Due to their ability to secrete vast amounts of plant cell wall degrading enzymes, Trichoderma strains have been used successfully for the industrial production of both homologous and heterologous enzymes. Extensive research on the optimization of the production process has yielded a number of versatile tools necessary to utilize Trichoderma�s protein secretion capacity to produce a wide variety of heterologous proteins. This article will address the use of Trichoderma reesei as a protein production host, as well as recent efforts towards its application as a whole-cell catalyst. The latter brings together the saprophytic activity of Trichoderma with metabolic engineering approaches for production of valuable chemical compounds from sustainable feedstock.

Keywords
Trichoderma, Hypocrea, protein production, whole-cell catalysis, host organism
Introduction
Trichoderma reesei (anamorph of Hypocrea jecorina) ADDIN EN.CITE  ADDIN EN.CITE.DATA [1] has been used for a number of years in industry for the production of hydrolyzing enzymes such as cellulases and hemicellulases. As a result of extensive programs in mutation and strain improvement the industrial strains used today can reach protein production and secretion on a scale of 100 g/l, of which up to 60% consists of the major cellulase cellobiohydrolase I (CBHI)  ADDIN EN.CITE <EndNote><Cite><Author>Schuster</Author><Year>2010</Year><RecNum>291</RecNum><DisplayText>[2]</DisplayText><record><rec-number>291</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">291</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Schuster, A.</author><author>Schmoll, M.</author></authors></contributors><auth-address>Research Area Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Getreidemarkt 9/166-5, 1060, Vienna, Austria. andre.schuster@tuwien.ac.at</auth-address><titles><title><style face="normal" font="default" size="100%">Biology and biotechnology of </style><style face="italic" font="default" size="100%">Trichoderma</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>787-99</pages><volume>87</volume><number>3</number><edition>2010/05/13</edition><keywords><keyword>Fungal Proteins/genetics/metabolism</keyword><keyword>Gene Expression Regulation, Fungal</keyword><keyword>*Industrial Microbiology</keyword><keyword>Trichoderma/classification/enzymology/*genetics/*metabolism</keyword></keywords><dates><year>2010</year><pub-dates><date>Jul</date></pub-dates></dates><isbn>1432-0614 (Electronic)&#xD;0175-7598 (Linking)</isbn><accession-num>20461510</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t&#xD;Review</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/20461510</url></related-urls></urls><custom2>2886115</custom2><electronic-resource-num>10.1007/s00253-010-2632-1</electronic-resource-num><language>eng</language></record></Cite></EndNote>[2], while growing on relatively cheap and simple media, such as mixtures of cellulose and xylan in plant materials from agricultural waste  ADDIN EN.CITE  ADDIN EN.CITE.DATA [3], or lactose, an industrial byproduct  ADDIN EN.CITE  ADDIN EN.CITE.DATA [4]. Furthermore, in contrast to most other industrial expression hosts, Trichoderma does not require any expensive additives, such as vitamins, amino acids or other supplements, in the growth medium, which makes T. reesei an interesting host organism for the production of heterologous proteins and has been studied in that respect for some time.
Moreover, following years of research toward improving hydrolytic enzyme production all essential tools needed for the expression of heterologous proteins using Trichoderma as host organism have been developed and tested extensively. In addition to the fact that there are numerous useful mutant strains available, from hypercellulolytic to cellulose-negative strains, and even some partially protease-deficient strains  ADDIN EN.CITE <EndNote><Cite><Author>Mantyla</Author><Year>1998</Year><RecNum>175</RecNum><DisplayText>[5]</DisplayText><record><rec-number>175</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">175</key></foreign-keys><ref-type name="Book Section">5</ref-type><contributors><authors><author>Mantyla, A.; Paloheimo M.; Suominen, P.</author></authors><secondary-authors><author>Harman, G.E.; Kubicek, C.P.</author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">Industrial mutants and recombinant strains of </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Trichoderma &amp; Gliocladium</secondary-title></titles><pages>291-309</pages><volume>2</volume><num-vols>2</num-vols><section>13</section><dates><year>1998</year></dates><pub-location>London</pub-location><publisher>Taylor &amp; Francis Ltd</publisher><isbn>0-7484-0805-3</isbn><urls></urls></record></Cite></EndNote>[5], Trichoderma can also be transformed with a number of different selection markers, from auxotrophic markers, such as pyr4  ADDIN EN.CITE  ADDIN EN.CITE.DATA [6], to resistance to hygromycin  ADDIN EN.CITE  ADDIN EN.CITE.DATA [7] or benomyl  ADDIN EN.CITE <EndNote><Cite><Author>Peterbauer</Author><Year>1992</Year><RecNum>184</RecNum><DisplayText>[8]</DisplayText><record><rec-number>184</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">184</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Peterbauer, Clemens K.</author><author>Heidenreich, Erich</author><author>Baker, Ralph T.</author><author>Kubicek, Christian P.</author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Effect of benomyl and benomyl resistance on cellulase formation by </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> and </style><style face="italic" font="default" size="100%">Trichoderma harzianum</style></title><secondary-title>Canadian journal of microbiology</secondary-title></titles><periodical><full-title>Canadian journal of microbiology</full-title><abbr-1>Can J Microbiol</abbr-1></periodical><pages>1292-1297</pages><volume>38</volume><number>12</number><dates><year>1992</year><pub-dates><date>1992/12/01</date></pub-dates></dates><publisher>NRC Research Press</publisher><isbn>0008-4166</isbn><urls><related-urls><url>http://dx.doi.org/10.1139/m92-213</url></related-urls></urls><electronic-resource-num>10.1139/m92-213</electronic-resource-num><access-date>2012/11/01</access-date></record></Cite></EndNote>[8], or even growth on acetamide as sole nitrogen source mediated through the A. nidulans amdS gene  ADDIN EN.CITE <EndNote><Cite><Author>Penttila</Author><Year>1987</Year><RecNum>177</RecNum><DisplayText>[9]</DisplayText><record><rec-number>177</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">177</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Penttil�, M.</author><author>Nevalainen, H.</author><author>Ratto, M.</author><author>Salminen, E.</author><author>Knowles, J.</author></authors></contributors><auth-address>VTT, Biotechnical Laboratory, Espoo, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">A versatile transformation system for the cellulolytic filamentous fungus </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Gene</secondary-title><alt-title>Gene</alt-title></titles><periodical><full-title>Gene</full-title><abbr-1>Gene</abbr-1></periodical><alt-periodical><full-title>Gene</full-title><abbr-1>Gene</abbr-1></alt-periodical><pages>155-64</pages><volume>61</volume><number>2</number><edition>1987/01/01</edition><keywords><keyword>Amidohydrolases/genetics</keyword><keyword>Arginine</keyword><keyword>Aspergillus nidulans/genetics</keyword><keyword>Genes, Dominant</keyword><keyword>Genes, Fungal</keyword><keyword>Genetic Complementation Test</keyword><keyword>Mitosporic Fungi/*genetics</keyword><keyword>Plasmids</keyword><keyword>Selection, Genetic</keyword><keyword>*Transformation, Genetic</keyword><keyword>Trichoderma/*genetics</keyword><keyword>beta-Galactosidase/genetics</keyword></keywords><dates><year>1987</year></dates><isbn>0378-1119 (Print)&#xD;0378-1119 (Linking)</isbn><accession-num>3127274</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/3127274</url></related-urls></urls><language>eng</language></record></Cite></EndNote>[9], most of which are recyclable. Finally, the recently developed Cre/loxP based transformation system allows bidirectional positive selection via hygromycin resistance or loss of sensitivity to fluoroacetamide, as well as excision of the marker gene allowing for multiple deletions and sequential transformations  ADDIN EN.CITE  ADDIN EN.CITE.DATA [10]. These characteristics of Trichoderma, together with investigations into the regulation of gene expression, protein production and protein secretion (reviewed in  ADDIN EN.CITE  ADDIN EN.CITE.DATA [11-14]), form a promising basis for research into improvement of heterologous protein production.

Recombinant proteins produced by Trichoderma sp.
While Trichoderma sp. are primarily used for the industrial production of their own hydrolytic enzymes (Table 1), thereby making perfect use of their excellent secretory capacity, a growing number of heterologous enzymes, mostly from closely related donor organisms, are also produced efficiently so as to make them competitive  ADDIN EN.CITE <EndNote><Cite ExcludeYear="1"><Author>AMFEP</Author><RecNum>287</RecNum><DisplayText>[15]</DisplayText><record><rec-number>287</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">287</key></foreign-keys><ref-type name="Web Page">12</ref-type><contributors><authors><author>AMFEP</author></authors></contributors><titles><title>List of commercial enzymes</title></titles><volume>2012</volume><number>05/11/2012</number><dates><year>2009</year></dates><urls><related-urls><url>http://www.amfep.org/content/list-enzymes</url></related-urls></urls></record></Cite></EndNote>[15] (Table 2).
Along with these examples of heterologous enzymes that are already produced on an industrial scale using Trichoderma as host organism, many other recombinant enzymes from more distantly related donor organisms have been successfully expressed in Trichoderma sp. in laboratory scale. Even though the protein yields obtained are still modest, there is much room for improvement through further engineering and optimization of production conditions (Table 2, adapted from  ADDIN EN.CITE  ADDIN EN.CITE.DATA [16-18]).
One example is the production of calf chymosin  ADDIN EN.CITE <EndNote><Cite><Author>Penttila</Author><Year>1998</Year><RecNum>168</RecNum><DisplayText>[17]</DisplayText><record><rec-number>168</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">168</key></foreign-keys><ref-type name="Book Section">5</ref-type><contributors><authors><author>Penttil�, M.</author></authors><secondary-authors><author>Harman, G.E.; Kubicek, C.P.</author></secondary-authors></contributors><titles><title><style face="normal" font="default" size="100%">Heterologous protein production in </style><style face="italic" font="default" size="100%">Trichoderma</style></title><secondary-title>Trichoderma &amp; Gliocladium</secondary-title></titles><pages>365-382</pages><volume>2</volume><num-vols>2</num-vols><section>17</section><dates><year>1998</year></dates><pub-location>London</pub-location><publisher>Taylor &amp; Francis Ltd</publisher><isbn>0-7484-0805-3</isbn><urls></urls></record></Cite></EndNote>[17], the first heterologous protein to be expressed in T. reesei Rut-C30 under the cbh1 promoter. The expression of a fusion protein of prochymosin with the CBHI core-linker region, which facilitated efficient translation, folding and secretion of the protein, the integration of the target gene into the highly expressed cbh1 locus and the optimisation of the culture conditions led to protein yields of over 100 mg/l of active chymosin in shake-flask cultures  ADDIN EN.CITE  ADDIN EN.CITE.DATA [19, 20]. 
Further efforts toward the expression of heterologous proteins in T. reesei resulted among others in the production of murine Fab antibody fragments by Nyyss�nen and co-workers  ADDIN EN.CITE  ADDIN EN.CITE.DATA [21, 22]. These molecules consist of the light chain and the Fd part of the heavy chain, connected by a disulphide bridge. The gene encoding the light chain was successfully expressed in T. reesei Rut-C30 and resulted in the production of 0.2 mg/l of product in shake-flask cultures. Following the subsequent expression of the gene encoding the heavy Fd chain fully functional antigen-binding Fab molecules were secreted into the culture medium on a scale of 1 mg/l in shake-flask culture. To further increase the protein yield the heavy Fd chain was expressed as a fusion protein with the CBHI core-linker region that resulted in protein yields of up to 40 mg/l in shake-flask cultures and 150 mg/l through cultivation in small-scale bioreactors  ADDIN EN.CITE  ADDIN EN.CITE.DATA [21, 22].

Strategies for improving protein production in Trichoderma sp.
In order to improve heterologous protein production in Trichoderma sp. a number of important factors, such as choice of promoter and signal sequences, control of glycosylation patterns, correct processing and successful secretion of the target protein have to be considered. 
Due to the fact that up to 60% of hydrolytic enzymes secreted by industrial T. reesei strains consist of CBHI  ADDIN EN.CITE <EndNote><Cite><Author>Schuster</Author><Year>2010</Year><RecNum>291</RecNum><DisplayText>[2]</DisplayText><record><rec-number>291</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">291</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Schuster, A.</author><author>Schmoll, M.</author></authors></contributors><auth-address>Research Area Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Getreidemarkt 9/166-5, 1060, Vienna, Austria. andre.schuster@tuwien.ac.at</auth-address><titles><title><style face="normal" font="default" size="100%">Biology and biotechnology of </style><style face="italic" font="default" size="100%">Trichoderma</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>787-99</pages><volume>87</volume><number>3</number><edition>2010/05/13</edition><keywords><keyword>Fungal Proteins/genetics/metabolism</keyword><keyword>Gene Expression Regulation, Fungal</keyword><keyword>*Industrial Microbiology</keyword><keyword>Trichoderma/classification/enzymology/*genetics/*metabolism</keyword></keywords><dates><year>2010</year><pub-dates><date>Jul</date></pub-dates></dates><isbn>1432-0614 (Electronic)&#xD;0175-7598 (Linking)</isbn><accession-num>20461510</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t&#xD;Review</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/20461510</url></related-urls></urls><custom2>2886115</custom2><electronic-resource-num>10.1007/s00253-010-2632-1</electronic-resource-num><language>eng</language></record></Cite></EndNote>[2], expressed from the single copy gene cbh1, its promoter, which can be strongly induced by growth on plant material, cellulose and especially sophorose, is often chosen for high-yield heterologous protein production  ADDIN EN.CITE <EndNote><Cite><Author>Keranen</Author><Year>1995</Year><RecNum>63</RecNum><DisplayText>[23]</DisplayText><record><rec-number>63</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">63</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Ker�nen, S.</author><author>Penttil�, M.</author></authors></contributors><auth-address>VTT Biotechnology and Food Research, Espoo, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Production of recombinant proteins in the filamentous fungus </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Current opinion in biotechnology</secondary-title><alt-title>Curr Opin Biotechnol</alt-title></titles><periodical><full-title>Current opinion in biotechnology</full-title><abbr-1>Curr Opin Biotechnol</abbr-1></periodical><alt-periodical><full-title>Current opinion in biotechnology</full-title><abbr-1>Curr Opin Biotechnol</abbr-1></alt-periodical><pages>534-7</pages><volume>6</volume><number>5</number><edition>1995/10/01</edition><keywords><keyword>Genetic Engineering</keyword><keyword>Recombinant Proteins/*biosynthesis</keyword><keyword>Trichoderma/*genetics/metabolism</keyword></keywords><dates><year>1995</year><pub-dates><date>Oct</date></pub-dates></dates><isbn>0958-1669 (Print)&#xD;0958-1669 (Linking)</isbn><accession-num>7579664</accession-num><work-type>Review</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/7579664</url></related-urls></urls><language>eng</language></record></Cite></EndNote>[23]. Nevertheless, owing to the characteristic carbon catabolite repression on glucose containing media and the inevitable co-regulation with most of the other native hydrolytic enzymes produced by T. reesei, which might impair the purification of the target protein, a number of other promoters might be considered for their use in heterologous protein production. For the expression on media containing glucose promoters regulating genes such as pgk1, encoding a phosphoglycerate kinase  ADDIN EN.CITE  ADDIN EN.CITE.DATA [24], pki, encoding a pyruvate kinase  ADDIN EN.CITE  ADDIN EN.CITE.DATA [25], tef1, encoding the translation elongation factor 1�, some as yet undefined genes as well as a glucose-derepressed version of the cbh1 promoter have been tested for their protein production capacity and can yield up to 50% of the total secreted protein on glucose  ADDIN EN.CITE  ADDIN EN.CITE.DATA [26, 27]. Moreover, the promoters of pdc, encoding a pyruvate decarboxylase, and eno, encoding an enolase, have been reported to yield up to 80% of total protein secreted  ADDIN EN.CITE <EndNote><Cite><Author>Li</Author><Year>2012</Year><RecNum>124</RecNum><DisplayText>[28]</DisplayText><record><rec-number>124</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">124</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Li, J.</author><author>Wang, J.</author><author>Wang, S.</author><author>Xing, M.</author><author>Yu, S.</author><author>Liu, G.</author></authors></contributors><auth-address>College of Life Science, Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen, 518060, China. zjuliug@szu.edu.cn.</auth-address><titles><title><style face="normal" font="default" size="100%">Achieving efficient protein expression in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> by using strong constitutive promoters</style></title><secondary-title>Microbial cell factories</secondary-title><alt-title>Microb Cell Fact</alt-title></titles><periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></periodical><alt-periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></alt-periodical><pages>84</pages><volume>11</volume><edition>2012/06/20</edition><dates><year>2012</year></dates><isbn>1475-2859 (Electronic)&#xD;1475-2859 (Linking)</isbn><accession-num>22709462</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/22709462</url></related-urls></urls><custom2>3439336</custom2><electronic-resource-num>10.1186/1475-2859-11-84</electronic-resource-num><language>eng</language></record></Cite></EndNote>[28]. 
In addition to the expression of high amounts of heterologous enzymes through the use of strongly inducible promoters, it is also crucial that these proteins are correctly folded and glycosylated to obtain them in their active form. This is especially important for the production of antibodies or other pharmaceutically active products, where differences in glycosylation have a considerable effect on the therapeutic activity of a heterologously produced component. Even though this requires a detailed understanding of the glycosylation pathways in Trichoderma, only very few enzymes involved in the N-glycosylation pathway have been isolated and characterized (reviewed by  ADDIN EN.CITE <EndNote><Cite><Author>Nevalainen</Author><Year>2005</Year><RecNum>60</RecNum><DisplayText>[29]</DisplayText><record><rec-number>60</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">60</key></foreign-keys><ref-type name="Book Section">5</ref-type><contributors><authors><author>Nevalainen, Helena</author><author>Te&apos;o, Valentino</author><author>Penttil�, Mer ja</author><author>Pakula, Tiina</author></authors><secondary-authors><author>Dilip, K. Arora</author><author>Randy, M. Berka</author></secondary-authors></contributors><titles><title>Heterologous gene expression in filamentous fungi: A holistic view</title><secondary-title>Applied Mycology and Biotechnology</secondary-title></titles><pages>211-237</pages><volume>Volume 5</volume><dates><year>2005</year></dates><publisher>Elsevier</publisher><isbn>1874-5334</isbn><urls><related-urls><url>http://www.sciencedirect.com/science/article/pii/S1874533405800115</url></related-urls></urls><electronic-resource-num>10.1016/s1874-5334(05)80011-5</electronic-resource-num></record></Cite></EndNote>[29]). One example is the �-1-2-mannosidase, which can cleave four 1,2-linked mannose sugars from Man9GlcNAc2. This activity points toward a Golgi-based mannosidases, but the exact location of this enzyme in the cell has not been found yet  ADDIN EN.CITE  ADDIN EN.CITE.DATA [30, 31]. At present altering the glycosylation patterns of proteins expressed in Trichoderma to yield mammalian-like glycan structures is achieved through in in vitro processing of the protein with mammalian enzymes  ADDIN EN.CITE  ADDIN EN.CITE.DATA [32], or through expression of mammalian genes, such as the human N-acetylglucosaminyltransferase I gene under the T. reesei cbh1 promoter, which results in the formation of GlcNAcMan5GlcNAc2  ADDIN EN.CITE  ADDIN EN.CITE.DATA [33]. Finally, overexpression of the T. reesei mannose-1-phosphate guanyltransferase leads to increased levels of GDP-mannose, which facilitates the formation of high-mannose glycan structures  ADDIN EN.CITE  ADDIN EN.CITE.DATA [34]. 
Notwithstanding the fact that the exceptionally high protein secretion capacity of T. reesei is usually decisive when choosing it as the host organism for heterologous protein production, in some cases an intracellular expression of the target proteins might be essential for protein yield and stability. Unfortunately this approach can have serious disadvantages, such as the possible toxicity of the heterologous protein to the host cell as well as a very problematic purification of the target protein. In order to overcome these limitations Mustalahti and co-workers proposed the use of hydrophobin fusions and protein body (PB) formation  ADDIN EN.CITE <EndNote><Cite><Author>Mustalahti</Author><Year>2011</Year><RecNum>65</RecNum><DisplayText>[35]</DisplayText><record><rec-number>65</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">65</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Mustalahti, E.</author><author>Saloheimo, M.</author><author>Joensuu, J. J.</author></authors></contributors><auth-address>VTT Biotechnology, VTT Technical Research Centre of Finland, Espoo 02044 VTT, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Intracellular protein production in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> (</style><style face="italic" font="default" size="100%">Hypocrea jecorina</style><style face="normal" font="default" size="100%">) with hydrophobin fusion technology</style></title><secondary-title>New biotechnology</secondary-title><alt-title>N Biotechnol</alt-title></titles><periodical><full-title>New biotechnology</full-title><abbr-1>N Biotechnol</abbr-1></periodical><alt-periodical><full-title>New biotechnology</full-title><abbr-1>N Biotechnol</abbr-1></alt-periodical><edition>2011/10/06</edition><dates><year>2011</year><pub-dates><date>Sep 28</date></pub-dates></dates><isbn>1876-4347 (Electronic)&#xD;1871-6784 (Linking)</isbn><accession-num>21971507</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/21971507</url></related-urls></urls><electronic-resource-num>10.1016/j.nbt.2011.09.006</electronic-resource-num><language>Eng</language></record></Cite></EndNote>[35]. They expressed the Green Fluorescent Protein (GFP) in T. reesei Rut-C30  ADDIN EN.CITE <EndNote><Cite><Author>Montenecourt</Author><Year>1979</Year><RecNum>317</RecNum><DisplayText>[36]</DisplayText><record><rec-number>317</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">317</key></foreign-keys><ref-type name="Book Section">5</ref-type><contributors><authors><author>Montenecourt, B. S.</author><author>Eveleigh, D. E.</author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Selective Screening Methods for the Isolation of High Yielding Cellulase Mutants of </style><style face="italic" font="default" size="100%">Trichoderma reesei</style></title><secondary-title>Hydrolysis of Cellulose: Mechanisms of Enzymatic and Acid Catalysis</secondary-title><tertiary-title>Advances in Chemistry</tertiary-title></titles><pages>289-301</pages><volume>181</volume><number>181</number><num-vols>0</num-vols><section>14</section><dates><year>1979</year></dates><publisher>AMERICAN CHEMICAL SOCIETY</publisher><isbn>0-8412-0460-8</isbn><urls><related-urls><url>http://dx.doi.org/10.1021/ba-1979-0181.ch014</url></related-urls></urls><electronic-resource-num>doi:10.1021/ba-1979-0181.ch014&#xD;10.1021/ba-1979-0181.ch014</electronic-resource-num><access-date>2012/11/09</access-date></record></Cite></EndNote>[36] as a fusion protein to the class II hydrophobin HBFI and the secretory signal peptide from CBHI, which was targeted to the ER and induced the formation of PB-like structures, similar to those that had already been observed using ZERA (a domain of maize �-zein) as fusion partner  ADDIN EN.CITE  ADDIN EN.CITE.DATA [37]. A further advantage of this approach is the resulting simple and inexpensive purification of the target protein using a surfactant in an aqueous two-phase system, which yields up to 62% of the target protein  ADDIN EN.CITE <EndNote><Cite><Author>Mustalahti</Author><Year>2011</Year><RecNum>65</RecNum><DisplayText>[35]</DisplayText><record><rec-number>65</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">65</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Mustalahti, E.</author><author>Saloheimo, M.</author><author>Joensuu, J. J.</author></authors></contributors><auth-address>VTT Biotechnology, VTT Technical Research Centre of Finland, Espoo 02044 VTT, Finland.</auth-address><titles><title><style face="normal" font="default" size="100%">Intracellular protein production in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> (</style><style face="italic" font="default" size="100%">Hypocrea jecorina</style><style face="normal" font="default" size="100%">) with hydrophobin fusion technology</style></title><secondary-title>New biotechnology</secondary-title><alt-title>N Biotechnol</alt-title></titles><periodical><full-title>New biotechnology</full-title><abbr-1>N Biotechnol</abbr-1></periodical><alt-periodical><full-title>New biotechnology</full-title><abbr-1>N Biotechnol</abbr-1></alt-periodical><edition>2011/10/06</edition><dates><year>2011</year><pub-dates><date>Sep 28</date></pub-dates></dates><isbn>1876-4347 (Electronic)&#xD;1871-6784 (Linking)</isbn><accession-num>21971507</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/21971507</url></related-urls></urls><electronic-resource-num>10.1016/j.nbt.2011.09.006</electronic-resource-num><language>Eng</language></record></Cite></EndNote>[35]. 

Trichoderma as whole-cell factory
Even though Trichoderma is mainly used for industrial enzyme production there have been attempts to use metabolic engineering and recombinant T. reesei strains for the production of valuable chemical components from diverse sustainable feed stock (see Figure 1). 
One example for the use of T. reesei as a whole-cell factory is the introduction of the ethylene-forming enzyme from Pseuomonas syringae into T. reesei QM9414 by a group at the Agricultural University in Bejing. The expression of this enzyme under the 3-phosphoglycerate kinase I (pgk1) promoter, the cbh1 promoter, and the glyceraldehyde-phosphate dehydrogenase (gpd) promoter from Aspergillus nidulans, resulted in a number of strains that produced up to 4 ml/h/l of ethylene on a number of different carbon sources, such as cellulose, CMC and wheat straw. Such efforts document the potential use of agricultural wastes and a recombinant T. reesei strain to produce an important building block for the chemical industry  ADDIN EN.CITE  ADDIN EN.CITE.DATA [38]. 
Only one year later Steiger and co-workers reported the use of a recombinant T. reesei strain to produce the antiviral drug precursor N-acetylneuraminic acid (NeuNAc) through cultivation on chitin, one of the most prominent renewable resources (109-1011 tons/year)  ADDIN EN.CITE  ADDIN EN.CITE.DATA [39]. The successful introduction of two recombinant enzymes, namely a GlcNAc-2-epimerase from Anabaena sp. CH1 and a NeuNAc synthase from Campylobacter jejuni complemented the native chitinolytic potential of T. reesei and resulted in the successful utilization of colloidal chitin as carbon source in a fermentation process and the biosynthesis of NeuNAc on a scale of several �g per g mycelium (dry weight)  ADDIN EN.CITE  ADDIN EN.CITE.DATA [39]. 
Undoubtedly these results do not constitute a competitive production process by far. Nevertheless, it was shown that it is possible to engineer a two-step bacterial enzyme cascade into a saprophytic fungus to yield a whole-cell catalyst for the production of a valuable chemical building block for the pharmaceutical industry from an abundant starting material using a simple and cheap cultivation method  ADDIN EN.CITE  ADDIN EN.CITE.DATA [39]. 

Conclusions
The use of recombinant Trichoderma strains for the industrial production of hydrolytic enzymes and the related research on gene regulation, protein processing and secretion aiming to increase the protein yield of industrial strains finally resulted in the development of all necessary tools that can now be applied in heterologous protein production. Consequently a number of foreign genes from distantly related organisms have been introduced into Trichoderma and the resulting proteins can be recovered in a correctly folded and fully functional form  ADDIN EN.CITE  ADDIN EN.CITE.DATA [2, 29]. Furthermore, efforts toward the use of the saprophyte Trichoderma as a whole-cell catalyst have shown that it is indeed possible to use cheap, renewable resources as growth medium for recombinant strains to produce valuable chemical building blocks  ADDIN EN.CITE  ADDIN EN.CITE.DATA [38, 39]. In combination with the extensive knowledge about cultivation conditions and improvement of protein yields available today, further research on Trichoderma-based whole-cell approaches for the production of value added chemicals from renewable biomass constitutes a promising endeavour. An important advantage of using Trichoderma as a whole-cell catalyst is the fact that the addition of expensive co-factors for enzyme reactions is not necessary, which partly facilitates the downstream process. Moreover the use of cheap, renewable resources and simultaneous absence of harsh chemicals are congruent with the general trend towards sustainable and environmentally friendly production processes.� 
References

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Figure legends

Figure 1: Schematic drawing of the use of Trichoderma as a whole-cell catalyst in recent approaches  ADDIN EN.CITE  ADDIN EN.CITE.DATA [38, 39]. Chitin or lignocellulose are used as renewable starting material for cultivation of engineered Trichoderma strains in a bioreactor. As a saprophyte Trichoderma natively is able to degrade biomass into the monomeric compounds, as N-acetylglucoseamine (GlcNAc) or pentose and hexose sugars, respectively. Depending on the introduced genes Trichoderma converts the monomers into the target compounds, N-acetylneuraminic acid (NeuNAc) or ethylene, respectively. ADDIN 








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�D���y������K����y������K�Nmailto:astrid.mach-aigner@tuwien.ac.at�	D<EndNote><Cite><Author>Kuhls</Author><Year>1996</Year><RecNum>355</RecNum><DisplayText>[1]</DisplayText><record><rec-number>355</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">355</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Kuhls, K.</author><author>Lieckfeldt, E.</author><author>Samuels, G. J.</author><author>Kovacs, W.</author><author>Meyer, W.</author><author>Petrini, O.</author><author>Gams, W.</author><author>Borner, T.</author><author>Kubicek, C. P.</author></authors></contributors><auth-address>Institut fur Biologie, Humboldt-Universitat zu Berlin, Germany.</auth-address><titles><title>Molecular evidence that the asexual industrial fungus Trichoderma reesei is a clonal derivative of the ascomycete Hypocrea jecorina</title><secondary-title>Proceedings of the National Academy of Sciences of the United States of America</secondary-title><alt-title>Proc Natl Acad Sci U S A</alt-title></titles><periodical><full-title>Proceedings of the National Academy of Sciences of the United States of America</full-title><abbr-1>Proc Natl Acad Sci U S A</abbr-1></periodical><alt-periodical><full-title>Proceedings of the National Academy of Sciences of the United States of America</full-title><abbr-1>Proc Natl Acad Sci U S A</abbr-1></alt-periodical><pages>7755-60</pages><volume>93</volume><number>15</number><edition>1996/07/23</edition><keywords><keyword>Ascomycota/*classification/*genetics</keyword><keyword>Cell Nucleus/metabolism</keyword><keyword>DNA Fingerprinting</keyword><keyword>DNA, Fungal/chemistry/genetics</keyword><keyword>DNA, Ribosomal/chemistry/*genetics</keyword><keyword>*Evolution, Molecular</keyword><keyword>Genes, Fungal</keyword><keyword>Geography</keyword><keyword>Molecular Sequence Data</keyword><keyword>*Phylogeny</keyword><keyword>Polymerase Chain Reaction</keyword><keyword>RNA, Fungal/biosynthesis</keyword><keyword>Transcription, Genetic</keyword><keyword>Trichoderma/*classification/*genetics</keyword></keywords><dates><year>1996</year><pub-dates><date>Jul 23</date></pub-dates></dates><isbn>0027-8424 (Print)&#xD;0027-8424 (Linking)</isbn><accession-num>8755548</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/8755548</url></related-urls></urls><custom2>38820</custom2><language>eng</language></record></Cite></EndNote>	D<EndNote><Cite><Author>Mach</Author><Year>2003</Year><RecNum>169</RecNum><DisplayText>[3]</DisplayText><record><rec-number>169</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">169</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Mach, R. L.</author><author>Zeilinger, S.</author></authors></contributors><auth-address>Institute of Biochemical Engineering, Microbial Biochemistry and Gene Technology Group, Getreidemarkt 9/166, 1060 Vienna, Austria. rmach@mail.zserv.tuwien.ac.at</auth-address><titles><title><style face="normal" font="default" size="100%">Regulation of gene expression in industrial fungi: </style><style face="italic" font="default" size="100%">Trichoderma</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>515-22</pages><volume>60</volume><number>5</number><edition>2003/01/22</edition><keywords><keyword>Cellulase/biosynthesis/*metabolism</keyword><keyword>Enzyme Induction</keyword><keyword>*Gene Expression Regulation, Fungal</keyword><keyword>Hydrolases/biosynthesis/metabolism</keyword><keyword>*Industrial Microbiology</keyword><keyword>Models, Genetic</keyword><keyword>Promoter Regions, Genetic/genetics</keyword><keyword>Signal Transduction</keyword><keyword>Trichoderma/enzymology/*genetics</keyword><keyword>Xylan Endo-1,3-beta-Xylosidase</keyword><keyword>Xylosidases/biosynthesis/*metabolism</keyword></keywords><dates><year>2003</year><pub-dates><date>Jan</date></pub-dates></dates><isbn>0175-7598 (Print)&#xD;0175-7598 (Linking)</isbn><accession-num>12536250</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t&#xD;Review</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/12536250</url></related-urls></urls><electronic-resource-num>10.1007/s00253-002-1162-x</electronic-resource-num><language>eng</language></record></Cite></EndNote>�	D<EndNote><Cite><Author>Seiboth</Author><Year>2007</Year><RecNum>170</RecNum><DisplayText>[4]</DisplayText><record><rec-number>170</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">170</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Seiboth, B.</author><author>Gamauf, C.</author><author>Pail, M.</author><author>Hartl, L.</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, Austria. bseiboth@mail.zserv.tuwien.ac.at</auth-address><titles><title><style face="normal" font="default" size="100%">The D-xylose reductase of </style><style face="italic" font="default" size="100%">Hypocrea jecorina</style><style face="normal" font="default" size="100%"> is the major aldose reductase in pentose and D-galactose catabolism and necessary for beta-galactosidase and cellulase induction by lactose</style></title><secondary-title>Molecular microbiology</secondary-title><alt-title>Mol Microbiol</alt-title></titles><periodical><full-title>Molecular microbiology</full-title><abbr-1>Mol Microbiol</abbr-1></periodical><alt-periodical><full-title>Molecular microbiology</full-title><abbr-1>Mol Microbiol</abbr-1></alt-periodical><pages>890-900</pages><volume>66</volume><number>4</number><edition>2007/10/11</edition><keywords><keyword>Aldehyde Reductase/genetics/*metabolism</keyword><keyword>Cellulase/*biosynthesis</keyword><keyword>Enzyme Induction</keyword><keyword>Fungal Proteins/genetics/metabolism</keyword><keyword>Galactose/metabolism</keyword><keyword>*Gene Expression Regulation, Fungal</keyword><keyword>Hypocrea/*enzymology/genetics/growth &amp; development/metabolism</keyword><keyword>Lactose/metabolism</keyword><keyword>Molecular Sequence Data</keyword><keyword>Pentoses/metabolism</keyword><keyword>Sequence Analysis, DNA</keyword><keyword>beta-Galactosidase/*biosynthesis</keyword></keywords><dates><year>2007</year><pub-dates><date>Nov</date></pub-dates></dates><isbn>0950-382X (Print)&#xD;0950-382X (Linking)</isbn><accession-num>17924946</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/17924946</url></related-urls></urls><electronic-resource-num>10.1111/j.1365-2958.2007.05953.x</electronic-resource-num><language>eng</language></record></Cite></EndNote>�D<EndNote><Cite><Author>Gruber</Author><Year>1990</Year><RecNum>176</RecNum><DisplayText>[6]</DisplayText><record><rec-number>176</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">176</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Gruber, F.</author><author>Visser, J.</author><author>Kubicek, C. P.</author><author>de Graaff, L. H.</author></authors></contributors><auth-address>Abt. Mikrobielle Biochemie, Institut fur Biochemische Technologie und Mikrobiologie, TU Wien, Austria.</auth-address><titles><title><style face="normal" font="default" size="100%">The development of a heterologous transformation system for the cellulolytic fungus </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> based on a pyrG-negative mutant strain</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>71-6</pages><volume>18</volume><number>1</number><edition>1990/07/01</edition><keywords><keyword>Blotting, Southern</keyword><keyword>Chromatography, Thin Layer</keyword><keyword>Drug Resistance, Microbial/genetics</keyword><keyword>Genes, Fungal</keyword><keyword>*Mutation</keyword><keyword>Orotic Acid/analogs &amp; derivatives/pharmacology</keyword><keyword>Orotidine-5&apos;-Phosphate Decarboxylase/*deficiency/genetics</keyword><keyword>*Transformation, Genetic</keyword><keyword>Trichoderma/*genetics/isolation &amp; purification</keyword><keyword>Uridine/metabolism</keyword></keywords><dates><year>1990</year><pub-dates><date>Jul</date></pub-dates></dates><isbn>0172-8083 (Print)&#xD;0172-8083 (Linking)</isbn><accession-num>2245476</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/2245476</url></related-urls></urls><language>eng</language></record></Cite></EndNote>�	D<EndNote><Cite><Author>Mach</Author><Year>1994</Year><RecNum>185</RecNum><DisplayText>[7]</DisplayText><record><rec-number>185</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">185</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Mach, R. L.</author><author>Schindler, M.</author><author>Kubicek, C. P.</author></authors></contributors><auth-address>Abteilung fur Mikrobielle Biochemie, TU Wien, Austria.</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%">based on hygromycin B resistance using homologous expression signals</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>567-70</pages><volume>25</volume><number>6</number><edition>1994/06/01</edition><keywords><keyword>Bacterial Proteins/genetics</keyword><keyword>Base Sequence</keyword><keyword>Cellulose 1,4-beta-Cellobiosidase</keyword><keyword>Chromosomes, Fungal</keyword><keyword>Drug Resistance, Microbial/genetics</keyword><keyword>Escherichia coli/enzymology/genetics</keyword><keyword>Gene Expression Regulation, Fungal</keyword><keyword>Genes, Bacterial</keyword><keyword>Genes, Fungal</keyword><keyword>Genetic Vectors</keyword><keyword>Glycoside Hydrolases/genetics</keyword><keyword>Hygromycin B/*pharmacology</keyword><keyword>Molecular Sequence Data</keyword><keyword>Phosphotransferases (Alcohol Group Acceptor)/*genetics</keyword><keyword>Pyruvate Kinase/genetics</keyword><keyword>Recombinant Fusion Proteins/genetics</keyword><keyword>Selection, Genetic</keyword><keyword>Species Specificity</keyword><keyword>*Transformation, Genetic</keyword><keyword>Trichoderma/drug effects/*genetics</keyword></keywords><dates><year>1994</year><pub-dates><date>Jun</date></pub-dates></dates><isbn>0172-8083 (Print)&#xD;0172-8083 (Linking)</isbn><accession-num>8082210</accession-num><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/8082210</url></related-urls></urls><language>eng</language></record></Cite></EndNote>
D<EndNote><Cite><Author>Steiger</Author><Year>2011</Year><RecNum>289</RecNum><DisplayText>[10]</DisplayText><record><rec-number>289</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">289</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Steiger, M. G.</author><author>Vitikainen, M.</author><author>Uskonen, P.</author><author>Brunner, K.</author><author>Adam, G.</author><author>Pakula, T.</author><author>Penttilä, M.</author><author>Saloheimo, M.</author><author>Mach, R. L.</author><author>Mach-Aigner, A. R.</author></authors></contributors><auth-address>Gene Technology, Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, TU Wien, Vienna, Austria.</auth-address><titles><title><style face="normal" font="default" size="100%">Transformation system for </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%">) that favors homologous integration and employs reusable bidirectionally selectable markers</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>114-21</pages><volume>77</volume><number>1</number><edition>2010/11/16</edition><keywords><keyword>Gene Targeting/methods</keyword><keyword>*Gene Transfer Techniques</keyword><keyword>Genetic Engineering/methods</keyword><keyword>Genetics, Microbial/*methods</keyword><keyword>Humans</keyword><keyword>Hypocrea/*genetics</keyword><keyword>Selection, Genetic</keyword><keyword>*Transformation, Genetic</keyword></keywords><dates><year>2011</year><pub-dates><date>Jan</date></pub-dates></dates><isbn>1098-5336 (Electronic)&#xD;0099-2240 (Linking)</isbn><accession-num>21075888</accession-num><work-type>Research Support, Non-U.S. 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size="100%">Hypocrea jecorina</style><style face="normal" font="default" size="100%">)</style></title><secondary-title>Microbiology</secondary-title></titles><periodical><full-title>Microbiology</full-title><abbr-1>Microbiology</abbr-1></periodical><pages>46-57</pages><volume>158</volume><number>1</number><dates><year>2012</year><pub-dates><date>January 1, 2012</date></pub-dates></dates><urls><related-urls><url>http://mic.sgmjournals.org/content/158/1/46.abstract</url></related-urls></urls><electronic-resource-num>10.1099/mic.0.053132-0</electronic-resource-num></record></Cite><Cite><Author>Aro</Author><Year>2005</Year><RecNum>292</RecNum><record><rec-number>292</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">292</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Aro, N.</author><author>Pakula, T.</author><author>Penttilä, M.</author></authors></contributors><auth-address>VTT Biotechnology, Espoo, 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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 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1,4-beta-Cellobiosidase</keyword><keyword>Cloning, Molecular</keyword><keyword>Culture Media</keyword><keyword>Genetic Vectors</keyword><keyword>Glycoside Hydrolases/*metabolism</keyword><keyword>Immunoglobulin Fab Fragments/biosynthesis/*genetics</keyword><keyword>RNA, Messenger/genetics/metabolism</keyword><keyword>Recombinant Fusion Proteins/genetics/metabolism</keyword><keyword>Trichoderma/*genetics</keyword></keywords><dates><year>1995</year><pub-dates><date>Jun</date></pub-dates></dates><isbn>0172-8083 (Print)&#xD;0172-8083 (Linking)</isbn><accession-num>8536316</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/8536316</url></related-urls></urls><language>eng</language></record></Cite></EndNote>(	D<EndNote><Cite><Author>Vanhanen</Author><Year>1989</Year><RecNum>213</RecNum><DisplayText>[24]</DisplayText><record><rec-number>213</rec-number><foreign-keys><key app="EN" 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G.</author><author>Mach-Aigner, A. R.</author><author>Gorsche, R.</author><author>Rosenberg, E. E.</author><author>Mihovilovic, M. D.</author><author>Mach, R. L.</author></authors></contributors><auth-address>Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Gumpendorfer Str. 1a, A-1060 Wien, Austria.</auth-address><titles><title>Synthesis of an antiviral drug precursor from chitin using a saprophyte as a whole-cell catalyst</title><secondary-title>Microbial cell factories</secondary-title><alt-title>Microb Cell Fact</alt-title></titles><periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></periodical><alt-periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></alt-periodical><pages>102</pages><volume>10</volume><edition>2011/12/07</edition><keywords><keyword>Anabaena/enzymology/genetics</keyword><keyword>Antiviral Agents/*metabolism</keyword><keyword>Bacterial Proteins/*genetics/metabolism</keyword><keyword>Campylobacter jejuni/*enzymology/genetics</keyword><keyword>Carbohydrate Epimerases/genetics/metabolism</keyword><keyword>Carrier Proteins/genetics/metabolism</keyword><keyword>Chitin/*metabolism</keyword><keyword>Hexosamines/metabolism</keyword><keyword>Hypocrea/*genetics/*metabolism</keyword><keyword>Oxo-Acid-Lyases/genetics/metabolism</keyword><keyword>Protein Engineering</keyword></keywords><dates><year>2011</year></dates><isbn>1475-2859 (Electronic)&#xD;1475-2859 (Linking)</isbn><accession-num>22141613</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/22141613</url></related-urls></urls><custom2>3245449</custom2><electronic-resource-num>10.1186/1475-2859-10-102</electronic-resource-num><language>eng</language></record></Cite></EndNote>�D<EndNote><Cite><Author>Steiger</Author><Year>2011</Year><RecNum>186</RecNum><DisplayText>[39]</DisplayText><record><rec-number>186</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">186</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Steiger, M. G.</author><author>Mach-Aigner, A. R.</author><author>Gorsche, R.</author><author>Rosenberg, E. E.</author><author>Mihovilovic, M. D.</author><author>Mach, R. L.</author></authors></contributors><auth-address>Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Gumpendorfer Str. 1a, A-1060 Wien, Austria.</auth-address><titles><title>Synthesis of an antiviral drug precursor from chitin using a saprophyte as a whole-cell catalyst</title><secondary-title>Microbial cell factories</secondary-title><alt-title>Microb Cell Fact</alt-title></titles><periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></periodical><alt-periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></alt-periodical><pages>102</pages><volume>10</volume><edition>2011/12/07</edition><keywords><keyword>Anabaena/enzymology/genetics</keyword><keyword>Antiviral Agents/*metabolism</keyword><keyword>Bacterial Proteins/*genetics/metabolism</keyword><keyword>Campylobacter jejuni/*enzymology/genetics</keyword><keyword>Carbohydrate Epimerases/genetics/metabolism</keyword><keyword>Carrier Proteins/genetics/metabolism</keyword><keyword>Chitin/*metabolism</keyword><keyword>Hexosamines/metabolism</keyword><keyword>Hypocrea/*genetics/*metabolism</keyword><keyword>Oxo-Acid-Lyases/genetics/metabolism</keyword><keyword>Protein Engineering</keyword></keywords><dates><year>2011</year></dates><isbn>1475-2859 (Electronic)&#xD;1475-2859 (Linking)</isbn><accession-num>22141613</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/22141613</url></related-urls></urls><custom2>3245449</custom2><electronic-resource-num>10.1186/1475-2859-10-102</electronic-resource-num><language>eng</language></record></Cite></EndNote>�D<EndNote><Cite><Author>Steiger</Author><Year>2011</Year><RecNum>186</RecNum><DisplayText>[39]</DisplayText><record><rec-number>186</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">186</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Steiger, M. G.</author><author>Mach-Aigner, A. R.</author><author>Gorsche, R.</author><author>Rosenberg, E. E.</author><author>Mihovilovic, M. D.</author><author>Mach, R. L.</author></authors></contributors><auth-address>Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Gumpendorfer Str. 1a, A-1060 Wien, Austria.</auth-address><titles><title>Synthesis of an antiviral drug precursor from chitin using a saprophyte as a whole-cell catalyst</title><secondary-title>Microbial cell factories</secondary-title><alt-title>Microb Cell Fact</alt-title></titles><periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></periodical><alt-periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></alt-periodical><pages>102</pages><volume>10</volume><edition>2011/12/07</edition><keywords><keyword>Anabaena/enzymology/genetics</keyword><keyword>Antiviral Agents/*metabolism</keyword><keyword>Bacterial Proteins/*genetics/metabolism</keyword><keyword>Campylobacter jejuni/*enzymology/genetics</keyword><keyword>Carbohydrate Epimerases/genetics/metabolism</keyword><keyword>Carrier Proteins/genetics/metabolism</keyword><keyword>Chitin/*metabolism</keyword><keyword>Hexosamines/metabolism</keyword><keyword>Hypocrea/*genetics/*metabolism</keyword><keyword>Oxo-Acid-Lyases/genetics/metabolism</keyword><keyword>Protein Engineering</keyword></keywords><dates><year>2011</year></dates><isbn>1475-2859 (Electronic)&#xD;1475-2859 (Linking)</isbn><accession-num>22141613</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/22141613</url></related-urls></urls><custom2>3245449</custom2><electronic-resource-num>10.1186/1475-2859-10-102</electronic-resource-num><language>eng</language></record></Cite></EndNote>:D<EndNote><Cite><Author>Schuster</Author><Year>2010</Year><RecNum>291</RecNum><DisplayText>[2, 29]</DisplayText><record><rec-number>291</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">291</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Schuster, A.</author><author>Schmoll, M.</author></authors></contributors><auth-address>Research Area Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Getreidemarkt 9/166-5, 1060, Vienna, Austria. andre.schuster@tuwien.ac.at</auth-address><titles><title><style face="normal" font="default" size="100%">Biology and biotechnology of </style><style face="italic" font="default" size="100%">Trichoderma</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>787-99</pages><volume>87</volume><number>3</number><edition>2010/05/13</edition><keywords><keyword>Fungal Proteins/genetics/metabolism</keyword><keyword>Gene Expression Regulation, Fungal</keyword><keyword>*Industrial Microbiology</keyword><keyword>Trichoderma/classification/enzymology/*genetics/*metabolism</keyword></keywords><dates><year>2010</year><pub-dates><date>Jul</date></pub-dates></dates><isbn>1432-0614 (Electronic)&#xD;0175-7598 (Linking)</isbn><accession-num>20461510</accession-num><work-type>Research Support, Non-U.S. Gov&apos;t&#xD;Review</work-type><urls><related-urls><url>http://www.ncbi.nlm.nih.gov/pubmed/20461510</url></related-urls></urls><custom2>2886115</custom2><electronic-resource-num>10.1007/s00253-010-2632-1</electronic-resource-num><language>eng</language></record></Cite><Cite><Author>Nevalainen</Author><Year>2005</Year><RecNum>60</RecNum><record><rec-number>60</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">60</key></foreign-keys><ref-type name="Book Section">5</ref-type><contributors><authors><author>Nevalainen, Helena</author><author>Te&apos;o, Valentino</author><author>Penttilä, Mer ja</author><author>Pakula, Tiina</author></authors><secondary-authors><author>Dilip, K. Arora</author><author>Randy, M. Berka</author></secondary-authors></contributors><titles><title>Heterologous gene expression in filamentous fungi: A holistic view</title><secondary-title>Applied Mycology and Biotechnology</secondary-title></titles><pages>211-237</pages><volume>Volume 5</volume><dates><year>2005</year></dates><publisher>Elsevier</publisher><isbn>1874-5334</isbn><urls><related-urls><url>http://www.sciencedirect.com/science/article/pii/S1874533405800115</url></related-urls></urls><electronic-resource-num>10.1016/s1874-5334(05)80011-5</electronic-resource-num></record></Cite></EndNote>�D<EndNote><Cite><Author>Chen</Author><Year>2010</Year><RecNum>143</RecNum><DisplayText>[38, 39]</DisplayText><record><rec-number>143</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">143</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Chen, X.</author><author>Liang, Y.</author><author>Hua, J.</author><author>Tao, L.</author><author>Qin, W.</author><author>Chen, S.</author></authors></contributors><auth-address>State Key Laboratory for Agrobiotechnology and College of Biological Sciences, China Agricultural University, Beijing 100193, P. R. China.</auth-address><titles><title><style face="normal" font="default" size="100%">Overexpression of bacterial ethylene-forming enzyme gene in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> enhanced the production of ethylene</style></title><secondary-title>International journal of biological sciences</secondary-title><alt-title>Int J Biol Sci</alt-title></titles><periodical><full-title>International journal of biological sciences</full-title><abbr-1>Int J Biol Sci</abbr-1></periodical><alt-periodical><full-title>International journal of biological sciences</full-title><abbr-1>Int J Biol Sci</abbr-1></alt-periodical><pages>96-106</pages><volume>6</volume><number>1</number><edition>2010/02/13</edition><keywords><keyword>Aspergillus nidulans/genetics</keyword><keyword>Blotting, Southern</keyword><keyword>Cellulose 1,4-beta-Cellobiosidase/genetics</keyword><keyword>Cloning, Molecular</keyword><keyword>DNA, Fungal</keyword><keyword>Ethylenes/*metabolism</keyword><keyword>Gene Dosage</keyword><keyword>Genetic Vectors</keyword><keyword>Glyceraldehyde-3-Phosphate Dehydrogenases/genetics</keyword><keyword>Lyases/genetics/*metabolism</keyword><keyword>Polymerase Chain Reaction</keyword><keyword>Promoter Regions, Genetic</keyword><keyword>Pseudomonas syringae/enzymology/*genetics</keyword><keyword>Reverse Transcriptase Polymerase Chain Reaction</keyword><keyword>Time Factors</keyword><keyword>*Transformation, Genetic</keyword><keyword>Trichoderma/enzymology/*genetics/metabolism</keyword><keyword>Triticum/metabolism</keyword></keywords><dates><year>2010</year></dates><isbn>1449-2288 (Electronic)</isbn><accession-num>20150979</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/20150979</url></related-urls></urls><custom2>2820237</custom2><language>eng</language></record></Cite><Cite><Author>Steiger</Author><Year>2011</Year><RecNum>186</RecNum><record><rec-number>186</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">186</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Steiger, M. G.</author><author>Mach-Aigner, A. R.</author><author>Gorsche, R.</author><author>Rosenberg, E. E.</author><author>Mihovilovic, M. D.</author><author>Mach, R. L.</author></authors></contributors><auth-address>Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Gumpendorfer Str. 1a, A-1060 Wien, Austria.</auth-address><titles><title>Synthesis of an antiviral drug precursor from chitin using a saprophyte as a whole-cell catalyst</title><secondary-title>Microbial cell factories</secondary-title><alt-title>Microb Cell Fact</alt-title></titles><periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></periodical><alt-periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></alt-periodical><pages>102</pages><volume>10</volume><edition>2011/12/07</edition><keywords><keyword>Anabaena/enzymology/genetics</keyword><keyword>Antiviral Agents/*metabolism</keyword><keyword>Bacterial Proteins/*genetics/metabolism</keyword><keyword>Campylobacter jejuni/*enzymology/genetics</keyword><keyword>Carbohydrate Epimerases/genetics/metabolism</keyword><keyword>Carrier Proteins/genetics/metabolism</keyword><keyword>Chitin/*metabolism</keyword><keyword>Hexosamines/metabolism</keyword><keyword>Hypocrea/*genetics/*metabolism</keyword><keyword>Oxo-Acid-Lyases/genetics/metabolism</keyword><keyword>Protein Engineering</keyword></keywords><dates><year>2011</year></dates><isbn>1475-2859 (Electronic)&#xD;1475-2859 (Linking)</isbn><accession-num>22141613</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/22141613</url></related-urls></urls><custom2>3245449</custom2><electronic-resource-num>10.1186/1475-2859-10-102</electronic-resource-num><language>eng</language></record></Cite></EndNote>�D<EndNote><Cite><Author>Steiger</Author><Year>2011</Year><RecNum>186</RecNum><DisplayText>[38, 39]</DisplayText><record><rec-number>186</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">186</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Steiger, M. G.</author><author>Mach-Aigner, A. R.</author><author>Gorsche, R.</author><author>Rosenberg, E. E.</author><author>Mihovilovic, M. D.</author><author>Mach, R. L.</author></authors></contributors><auth-address>Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Gumpendorfer Str. 1a, A-1060 Wien, Austria.</auth-address><titles><title>Synthesis of an antiviral drug precursor from chitin using a saprophyte as a whole-cell catalyst</title><secondary-title>Microbial cell factories</secondary-title><alt-title>Microb Cell Fact</alt-title></titles><periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></periodical><alt-periodical><full-title>Microbial cell factories</full-title><abbr-1>Microb Cell Fact</abbr-1></alt-periodical><pages>102</pages><volume>10</volume><edition>2011/12/07</edition><keywords><keyword>Anabaena/enzymology/genetics</keyword><keyword>Antiviral Agents/*metabolism</keyword><keyword>Bacterial Proteins/*genetics/metabolism</keyword><keyword>Campylobacter jejuni/*enzymology/genetics</keyword><keyword>Carbohydrate Epimerases/genetics/metabolism</keyword><keyword>Carrier Proteins/genetics/metabolism</keyword><keyword>Chitin/*metabolism</keyword><keyword>Hexosamines/metabolism</keyword><keyword>Hypocrea/*genetics/*metabolism</keyword><keyword>Oxo-Acid-Lyases/genetics/metabolism</keyword><keyword>Protein Engineering</keyword></keywords><dates><year>2011</year></dates><isbn>1475-2859 (Electronic)&#xD;1475-2859 (Linking)</isbn><accession-num>22141613</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/22141613</url></related-urls></urls><custom2>3245449</custom2><electronic-resource-num>10.1186/1475-2859-10-102</electronic-resource-num><language>eng</language></record></Cite><Cite><Author>Chen</Author><Year>2010</Year><RecNum>143</RecNum><record><rec-number>143</rec-number><foreign-keys><key app="EN" db-id="zf225s0efpwz0uerrspprfpvzpw5v5pxrzae">143</key></foreign-keys><ref-type name="Journal Article">17</ref-type><contributors><authors><author>Chen, X.</author><author>Liang, Y.</author><author>Hua, J.</author><author>Tao, L.</author><author>Qin, W.</author><author>Chen, S.</author></authors></contributors><auth-address>State Key Laboratory for Agrobiotechnology and College of Biological Sciences, China Agricultural University, Beijing 100193, P. R. China.</auth-address><titles><title><style face="normal" font="default" size="100%">Overexpression of bacterial ethylene-forming enzyme gene in </style><style face="italic" font="default" size="100%">Trichoderma reesei</style><style face="normal" font="default" size="100%"> enhanced the production of ethylene</style></title><secondary-title>International journal of biological sciences</secondary-title><alt-title>Int J Biol Sci</alt-title></titles><periodical><full-title>International journal of biological sciences</full-title><abbr-1>Int J Biol Sci</abbr-1></periodical><alt-periodical><full-title>International journal of biological sciences</full-title><abbr-1>Int J Biol Sci</abbr-1></alt-periodical><pages>96-106</pages><volume>6</volume><number>1</number><edition>2010/02/13</edition><keywords><keyword>Aspergillus nidulans/genetics</keyword><keyword>Blotting, Southern</keyword><keyword>Cellulose 1,4-beta-Cellobiosidase/genetics</keyword><keyword>Cloning, Molecular</keyword><keyword>DNA, Fungal</keyword><keyword>Ethylenes/*metabolism</keyword><keyword>Gene Dosage</keyword><keyword>Genetic Vectors</keyword><keyword>Glyceraldehyde-3-Phosphate Dehydrogenases/genetics</keyword><keyword>Lyases/genetics/*metabolism</keyword><keyword>Polymerase Chain Reaction</keyword><keyword>Promoter Regions, Genetic</keyword><keyword>Pseudomonas syringae/enzymology/*genetics</keyword><keyword>Reverse Transcriptase Polymerase Chain Reaction</keyword><keyword>Time Factors</keyword><keyword>*Transformation, Genetic</keyword><keyword>Trichoderma/enzymology/*genetics/metabolism</keyword><keyword>Triticum/metabolism</keyword></keywords><dates><year>2010</year></dates><isbn>1449-2288 (Electronic)</isbn><accession-num>20150979</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/20150979</url></related-urls></urls><custom2>2820237</custom2><language>eng</language></record></Cite></EndNote>�# OJPJQJ_HmHnHsHtHZ`�ZZBXStandarddh�x�� CJOJQJ_HaJmHsHtHb b
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