Alleviating product inhibition of Trichoderma reesei cellulase complex with a product-activated mushroom endoglucanase
| Autor: | Yinmei Wang, Dapeng Bao, Zhanshan Yang, Meili Xiao, Zhihua Zhou, Gen Zou, Sichi Zhou, Ying Wang |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
Environmental Engineering Bioengineering Cellulase 010501 environmental sciences 01 natural sciences Hydrolysis 010608 biotechnology Food science Saturated mutagenesis Waste Management and Disposal Trichoderma reesei 0105 earth and related environmental sciences Thermostability chemistry.chemical_classification Trichoderma biology Renewable Energy Sustainability and the Environment Substrate (chemistry) General Medicine biology.organism_classification Reducing sugar chemistry Product inhibition Mutagenesis biology.protein Agaricales |
| Zdroj: | Bioresource technology. 319 |
| ISSN: | 1873-2976 |
| Popis: | Product inhibition of cellulase is a challenging issue in industrial processes. Here, we introduced a product-activated mushroom cellulase, PaCel3A from Polyporus arcularius, into Trichoderma reesei. The filter paper activity, carboxymethyl cellulase activity, and saccharification efficiency (substrate: pretreated rice straw, PRS) of transformants increased significantly with this enzyme (by 18.4-26.8%, 13.8-22.8%, and 17.0%, respectively). A mutant of PaCel3A, PaCel3AM, obtained based on B-factor analysis, saturated mutagenesis, and residual activity assay, showed improved thermostability. The PRS saccharification efficiency using the cellulase complex from T. reesei transformants overexpressing pacel3am increased by 56.4%-63.0%. In addition, the T. reesei cellulase complex obtained by adding the purified recombinant PaCel3AM from T. reesei (rCel3aM-tr) to hydrolyze PRS resulted in increased reducing sugar yields at all sampling points, outperforming the cellulase complexes without rCel3aM-tr. These results suggest that introducing product-activated cellulase genes is a simple and feasible method to alleviate the product inhibition of cellulase. |
| Databáze: | OpenAIRE |
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