Protein disulfide isomerase homolog TrPDI2 contributing to cellobiohydrolase production in Trichoderma reesei |
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| Affiliation: | 1. Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, PR China;2. University of Chinese Academy Sciences, 19A, Yuquan Road, Beijing 100049, China;1. Section for Sustainable Biotechnology, Aalborg University Copenhagen, A. C. Meyers Vænge 15, DK-2450 Copenhagen SV, Denmark;2. Bioproducts, Sciences and Engineering Laboratory (BSEL), Washington State University Tri-Cities, 2710 Crimson Way, Richland 99354, WA, USA;1. Molecular Glyco-biotechnology Group, Discipline of Biochemistry, School of Natural Sciences, National University of Ireland Galway, Galway, Ireland;2. Departamento de Biologia Celular, Universidade de Brasília, Campus Universitário Darcy Ribeiro, Instituto de Ciências Biológicas, Brasília, DF, Brazil;3. Department of Biochemistry and Immunology, Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, Brazil;4. Department of Cell and Molecular Biology–Ribeirão Preto Medical School, University of São Paulo, Ribeirão Preto, SP, Brazil;5. Department for Biotechnology and Microbiology, Institute of Chemical Engineering, TU Wien, Wien, Austria;1. Tianjin Key Laboratory of Industrial Biosystem and Bioprocess Engineering, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, PR China;2. University of Chinese Academy Sciences, 19A, Yuquan Road, Beijing 100049, PR China;3. Department of Biological Systems Engineering, Washington State University, Pullman, WA 99164-6120, USA |
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| Abstract: | The majority of the cysteine residues in the secreted proteins form disulfide bonds via protein disulfide isomerase (PDI)-mediated catalysis, stabilizing the enzyme activity. The role of PDI in cellulase production is speculative, as well as the possibility of PDI as a target for improving enzyme production efficiency of Trichoderma reesei, a widely used producer of enzyme for the production of lignocellulose-based biofuels and biochemicals. Here, we report that a PDI homolog, TrPDI2 in T. reesei exhibited a 36.94% and an 11.81% similarity to Aspergillus niger TIGA and T. reesei PDI1, respectively. The capability of TrPDI2 to recover the activity of reduced and denatured RNase by promoting refolding verified its protein disulfide isomerase activity. The overexpression of Trpdi2 increased the secretion and the activity of CBH1 at the early stage of cellulase induction. In addition, both the expression level and redox state of TrPDI2 responded to cellulase induction in T. reesei, providing sustainable oxidative power to ensure cellobiohydrolase maturation and production. The results suggest that TrPDI2 may contribute to cellobiohydrolase secretion by enhancing the capability of disulfide bond formation, which is essential for protein folding and maturation. |
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| Keywords: | Cellobiohydrolase Cellulase Disulfide bond Protein disulfide isomerase |
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