Application of Trichoderma reesei cellulase and xylanase promoters through homologous recombination for enhanced production of extracellular β-glucosidase 1
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- RAHMAN Zinnia
- Department of Bioengineering, Nagaoka University of Technology
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- SHIDA Yosuke
- Department of Bioengineering, Nagaoka University of Technology
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- FURUKAWA Takanori
- Department of Bioengineering, Nagaoka University of Technology
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- SUZUKI Yota
- Department of Bioengineering, Nagaoka University of Technology
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- OKADA Hirofumi
- Department of Bioengineering, Nagaoka University of Technology
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- OGASAWARA Wataru
- Department of Bioengineering, Nagaoka University of Technology
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- MORIKAWA Yasushi
- Department of Bioengineering, Nagaoka University of Technology
書誌事項
- タイトル別名
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- Application of Trichoderma reesei Cellulase and Xylanase Promoters through Homologous Recombination for Enhanced Production of Extracellular .BETA.-Glucosidase I
- Application of Trichoderma reesei cellulase and xylanase promoters through homologous recombination for enhanced production of extracellular v glucosidase 1
- Application of<i>Trichoderma reesei</i>Cellulase and Xylanase Promoters through Homologous Recombination for Enhanced Production of Extracellular β-Glucosidase I
- Application of Trichoderma reesei cellulase and xylanase promoters through homologous recombination for enhanced production of extracellular β-glucosidase I
この論文をさがす
説明
One of the limiting factors for the application of Trichoderma reesei to degrade cellulosic biomass is its low β-glucosidase activity, required to convert cellobiose to glucose. The egl3 and the xyn3 promoters were used to express β-glucosidase 1 gene bgl1 through homologous recombination to improve the cellulose degradation ability of T. reesei. The recombinant strains expressing β-glucosidase 1 (BGLI) under the control of either the egl3 or the xyn3 promoter had 4.0 and 7.5 fold higher β-glucosidase activity than the native strain, which compares well to the finding that in wild-type T. reesei PC-3-7, the levels of egl3 and xyn3 mRNA expression were 6.0 and 12 fold higher respectively than that of bgl1. Matrix assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry analysis of proteins secreted by the recombinant strains demonstrated that BGLI was overproduced. The increase in the transcription of bgl1 and the concomitant elevated level of BGLI in these recombinant strains were sufficient to degrade the cellobiose and cellotriose formed during the degradation of pretreated cedar powder.
収録刊行物
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- Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ
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Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ 73 (5), 1083-1089, 2009
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681454125312
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- NII論文ID
- 10027540909
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 10234807
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- PubMed
- 19420722
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- 本文言語コード
- en
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- JaLC
- NDLサーチ
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- 使用不可
