期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 117, 期 -, 页码 342-349出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2018.05.189
关键词
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资金
- National Key Technology R&D Program of China [2015BAD15B05]
- National Science Foundation of China [31671985]
- Natural Science Foundation of Shandong Province of China [ZR2018BC014]
- Funds of Taishan Scholar Construction Project [TS201712023]
- Shandong Provincial Key Laboratory of Agricultural Microbiology Open Fund [SDKL2017015]
A new endoglucanase encoding gene (ctendo7) was cloned from the thermophilic fungus Chaetomium thermophilum and heterologously expressed in Pichia pastoris. The recombinant CTendo7 enzyme was purified by Ni2+ affinity chromatography and subsequently characterized. CTendo7 belongs to glycoside hydrolase family 7, and exhibited considerable activity against sodium carboxymethyl cellulose (CMC-Na) and xylan of 1.91 IU/mg and 3.05 IU/mg at the optimum reaction condition of 55 degrees C, pH 5.0, respectively. The purified enzyme displayed relatively good thermostability. The residual endoglucanase and xylanase activities were 743% and 66.2% after a 60 min pre-incubation at 70 degrees C. Additionally, Ag+, Fe3+ and Cu2+ negatively affected the enzyme's activity, while the presence of 1 mM and 5 mM Mn2+ significantly enhanced both endoglucanase and xylanase activities. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production, and it is noteworthy that CTendo7 produced cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of CMC-Na and xylan, respectively. This is the first detailed report on a novel bifunctional endoglucanase/xylanase enzyme from C. thermophilum. Furthermore, the excellent properties of CTendo7 distinguish it as a promising candidate for industrial lignocellulosic biomass conversion. (C) 2018 Elsevier B.V. All rights reserved.
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