title: A high performance Trichoderma reesei strain that reveals the importance of xylanase III in cellulosic biomass conversion.
abstract: The ability of the Trichoderma reesei X3AB1strain enzyme preparations to convert cellulosic biomass into fermentable sugars is enhanced by the replacement of xyn3 by Aspergillus aculeatus β-glucosidase 1 gene (aabg1), as shown in our previous study. However, subsequent experiments using T. reesei extracts supplemented with the glycoside hydrolase (GH) family 10 xylanase III (XYN III) and GH Family 11 XYN II showed increased conversion of alkaline treated cellulosic biomass, which is rich in xylan, underscoring the importance of XYN III. To attain optimal saccharifying potential in T. reesei, we constructed two new strains, C1AB1 and E1AB1, in which aabg1 was expressed heterologously by means of the cbh1 or egl1 promoters, respectively, so that the endogenous XYN III synthesis remained intact. Due to the presence of wild-type xyn3 in T. reesei E1AB1, enzymes prepared from this strain were 20-30% more effective in the saccharification of alkaline-pretreated rice straw than enzyme extracts from X3AB1, and also outperformed recent commercial cellulase preparations. Our results demonstrate the importance of XYN III in the conversion of alkaline-pretreated cellulosic biomass by T. reesei.
authors.affiliation: Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka 940-2188, Japan.
authors.forename: Hikaru
authors.initials: H
authors.lastname: Nakazawa
authors.affiliation: Japan Bioindustry Association, AIST Tsukuba Central 6, 1-1-1Higashi, Tsukuba, Ibaraki 305-8566, Japan.
authors.forename: Tetsushi
authors.initials: T
authors.lastname: Kawai
authors.affiliation: Japan Bioindustry Association, AIST Tsukuba Central 6, 1-1-1Higashi, Tsukuba, Ibaraki 305-8566, Japan.
authors.forename: Noriko
authors.initials: N
authors.lastname: Ida
authors.affiliation: Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka 940-2188, Japan.
authors.forename: Yosuke
authors.initials: Y
authors.lastname: Shida
authors.affiliation: Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka 940-2188, Japan.
authors.forename: Kouki
authors.initials: K
authors.lastname: Shioya
authors.affiliation: Japan Bioindustry Association, AIST Tsukuba Central 6, 1-1-1Higashi, Tsukuba, Ibaraki 305-8566, Japan.
authors.forename: Yoshinori
authors.initials: Y
authors.lastname: Kobayashi
authors.affiliation: Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka 940-2188, Japan.
authors.forename: Hirofumi
authors.initials: H
authors.lastname: Okada
authors.affiliation: Graduate School of Agriculture and Biological Sciences and Research Institute for Advanced Science and Technology, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, Osaka 599-8531, Japan.
authors.forename: Shuji
authors.initials: S
authors.lastname: Tani
authors.affiliation: Graduate School of Agriculture and Biological Sciences and Research Institute for Advanced Science and Technology, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, Osaka 599-8531, Japan.
authors.forename: Jun-Ichi
authors.initials: JI
authors.lastname: Sumitani
authors.affiliation: Graduate School of Agriculture and Biological Sciences and Research Institute for Advanced Science and Technology, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, Osaka 599-8531, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Kawaguchi
authors.affiliation: Japan Bioindustry Association, AIST Tsukuba Central 6, 1-1-1Higashi, Tsukuba, Ibaraki 305-8566, Japan.
authors.forename: Yasushi
authors.initials: Y
authors.lastname: Morikawa
authors.affiliation: Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka 940-2188, Japan. Electronic address: owataru@vos.nagaokaut.ac.jp.
authors.forename: Wataru
authors.initials: W
authors.lastname: Ogasawara
mesh_terms: D000818:Animals; D001230:Aspergillus / Q000201:enzymology / Q000235:genetics; D018533:Biomass; D002480:Cellulase / Q000235:genetics; D002482:Cellulose / Q000378:metabolism*; D043366:Cellulose 1,4-beta-Cellobiosidase / Q000235:genetics; D043364:Endo-1,4-beta Xylanases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D005656:Fungal Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D005800:Genes, Fungal; D005813:Genes, Synthetic; D006110:Grasshoppers; D006863:Hydrogen-Ion Concentration; D007218:Industrial Microbiology / Q000379:methods; D012275:Oryza; D018547:Plant Stems; D011134:Polysaccharides / Q000378:metabolism; D011401:Promoter Regions, Genetic; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013045:Species Specificity; D014242:Trichoderma / Q000145:classification / Q000201:enzymology* / Q000235:genetics; D001617:beta-Glucosidase / Q000235:genetics
chemical_list: D005656:Fungal Proteins; D011134:Polysaccharides; D011993:Recombinant Fusion Proteins; C007916:hemicellulose; D002482:Cellulose; C056374:endoglucanase 1; D001617:beta-Glucosidase; D002480:Cellulase; D043364:Endo-1,4-beta Xylanases; D043366:Cellulose 1,4-beta-Cellobiosidase
keywords: Biomass; Cellulase; GHF 10 xylanase; Trichoderma; β-Glucosidase