Protein disulfide isomerase homolog TrPDI2 contributing to cellobiohydrolase production in Trichoderma reesei

被引：7

作者：

Wang, Guokun ^{[1
,2
]}

Lv, Pin ^{[1
]}

He, Ronglin ^{[1
]}

Wang, Haijun ^{[1
]}

Wang, Lixian ^{[1
]}

Zhang, Dongyuan ^{[1
]}

Chen, Shulin ^{[1
]}

机构：

[1] Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin 300308, PR, Peoples R China

[2] Univ Chinese Acad Sci, Beijing 100049, Peoples R China

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 2015年 / 77卷

基金：

国家高技术研究发展计划(863计划); 中国国家自然科学基金;

关键词：

Cellobiohydrolase; Cellulase; Disulfide bond; Protein disulfide isomerase; Trichoderma reesei; TRANSFORMATION SYSTEM; GENE; ENDOGLUCANASE; EFFICIENT; RUT-C30; STRESS;

D O I：

10.1016/j.enzmictec.2015.05.004

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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. (C) 2015 Elsevier Inc. All rights reserved.

引用

页码：21 / 28

页数：8

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