Heterologous expression of Talaromyces emersonii cellobiohydrolase Cel7A in Trichoderma reesei increases the efficiency of corncob residues saccharification

Heterologous expression of Talaromyces emersonii cellobiohydrolase Cel7A in Trichoderma reesei... Biotechnol Lett (2018) 40:1119–1126 https://doi.org/10.1007/s10529-018-2564-x ORIGINAL RESEARCH PAPER Heterologous expression of Talaromyces emersonii cellobiohydrolase Cel7A in Trichoderma reesei increases the efficiency of corncob residues saccharification . . . . Ningning Sun Yuanchao Qian Weiwei Wang Yaohua Zhong Meixue Dai Received: 13 February 2018 / Accepted: 8 May 2018 / Published online: 19 May 2018 Springer Science+Business Media B.V., part of Springer Nature 2018 Abstract increase in filter paper activity relative to that of the Objective Improve the hydrolysis efficiency of the parental strain QP4. Moreover, the QTC14 cellulase Trichoderma reesei cellulase system by heterolo- system showed higher thermal stability than that of the gously expressing cellobiohydrolase Cel7A (Te- parental strain QP4. In the saccharification of delig- Cel7A) from the thermophilic fungus Talaromyces nified corncob residue, the cellulose conversion of emersonii. QTC14 showed 13.9% higher than that of QP4 at the Results Te-Cel7A was expressed in T. reesei under end of reaction. control of the cdna1 promoter and the generated Conclusions The thermophilic fungus-derived cel- transformant QTC14 could successfully secrete Te- lulases could be efficiently expressed by T. reesei and Cel7A into the supernatant using glucose as carbon the recombinant cellulases had potential applications source. The recombinant Te-Cel7A had a http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology Letters Springer Journals

Heterologous expression of Talaromyces emersonii cellobiohydrolase Cel7A in Trichoderma reesei increases the efficiency of corncob residues saccharification

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Publisher
Springer Netherlands
Copyright
Copyright © 2018 by Springer Science+Business Media B.V., part of Springer Nature
Subject
Life Sciences; Microbiology; Biotechnology; Applied Microbiology; Biochemistry, general
ISSN
0141-5492
eISSN
1573-6776
D.O.I.
10.1007/s10529-018-2564-x
Publisher site
See Article on Publisher Site

Abstract

Biotechnol Lett (2018) 40:1119–1126 https://doi.org/10.1007/s10529-018-2564-x ORIGINAL RESEARCH PAPER Heterologous expression of Talaromyces emersonii cellobiohydrolase Cel7A in Trichoderma reesei increases the efficiency of corncob residues saccharification . . . . Ningning Sun Yuanchao Qian Weiwei Wang Yaohua Zhong Meixue Dai Received: 13 February 2018 / Accepted: 8 May 2018 / Published online: 19 May 2018 Springer Science+Business Media B.V., part of Springer Nature 2018 Abstract increase in filter paper activity relative to that of the Objective Improve the hydrolysis efficiency of the parental strain QP4. Moreover, the QTC14 cellulase Trichoderma reesei cellulase system by heterolo- system showed higher thermal stability than that of the gously expressing cellobiohydrolase Cel7A (Te- parental strain QP4. In the saccharification of delig- Cel7A) from the thermophilic fungus Talaromyces nified corncob residue, the cellulose conversion of emersonii. QTC14 showed 13.9% higher than that of QP4 at the Results Te-Cel7A was expressed in T. reesei under end of reaction. control of the cdna1 promoter and the generated Conclusions The thermophilic fungus-derived cel- transformant QTC14 could successfully secrete Te- lulases could be efficiently expressed by T. reesei and Cel7A into the supernatant using glucose as carbon the recombinant cellulases had potential applications source. The recombinant Te-Cel7A had a

Journal

Biotechnology LettersSpringer Journals

Published: May 19, 2018

References

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