A high performance Trichoderma reesei strain that reveals the importance of xylanase III in cellulosic biomass conversion |
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| Institution: | 1. Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka 940-2188, Japan;2. Japan Bioindustry Association, AIST Tsukuba Central 6, 1-1-1Higashi, Tsukuba, Ibaraki 305-8566, Japan;3. 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;1. Metabolic Disorder Research Center, Golestan University of Medical Science, Gorgan, Iran;2. Department of Chemistry, Sharif University of Technology, Tehran, Iran;3. Department of Microbiology, School of Medicine, Golestan University of Medical Science, Gorgan, Iran;1. Department of Cell Biology, Institute of Biomedicine, College of Life Science and Technology, Jinan University, Guangzhou, Guangdong 510632, China;2. National Key Laboratory of Protein Engineering and Plant Gene Engineering, LSC, Peking University, Beijing 100871, China;1. Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, University of Southern California, CA, USA;2. Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, Magee-Womens Hospital, University of Pittsburgh, PA, USA;3. Department of Breast and Medical Oncology, National Cancer Center Hospital, Tokyo, Japan;4. Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, University of Kentucky, KY, USA;5. Department of Gynecology, Cancer Institute Hospital, Tokyo, Japan;6. Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, Albert Einstein College of Medicine, Montefiore Medical Center, NY, USA;7. The Gynecologic Oncology Center, Mercy Medical Center, Baltimore, MD, USA;8. Department of Obstetrics and Gynecology, Tottori University, Tottori, Japan;9. Department of Obstetrics and Gynecology, Kyoto University, Kyoto, Japan;10. Department of Obstetrics and Gynecology, The University of Tokyo, Tokyo, Japan;11. Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, Moffitt Cancer Center, University of South Florida, FL, USA;12. Department of Obstetrics and Gynecology, Saitama Medical University International Medical Center, Saitama, Japan;13. Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, University of Colorado, CO, USA;14. Department of Gynecology, Shizuoka Cancer Center, Shizuoka, Japan;15. Department of Obstetrics and Gynecology, Tokai University, Kanagawa, Japan;p. Department of Obstetrics and Gynecology, Tokushima University, Tokushima, Japan;q. Department of Obstetrics and Gynecology, Niigata University, Niigata, Japan;r. Division of Gynecologic Oncology, Department of Obstetrics and Gynecology, Oregon Health & Science University, OR, USA;s. Department of Obstetrics and Gynecology, Iwate Medical University, Morioka, Japan;t. Department of Obstetrics and Gynecology, Osaka Rosai Hospital, Osaka, Japan;u. Department of Obstetrics and Gynecology, Osaka University, Osaka, Japan;v. Department of Obstetrics and Gynecology, Aichi Medical University, Aichi, Japan;w. Department of Obstetrics and Gynecology, Kawasaki Medical School, Okayama, Japan;x. Department of Obstetrics and Gynecology, Kurashiki Medical Center, Okayama, Japan;y. Department of Obstetrics and Gynecology, Kitano Hospital, Osaka, Japan;z. Department of Obstetrics and Gynecology, Tohoku University, Miyagi, Japan |
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| 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. |
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| Keywords: | Cellulase GHF 10 xylanase β-Glucosidase Biomass |
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