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Applied Microbiology and Biotechnology
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A thermophilic endo-1,4--glucanase from Talaromyces emersonii CBS394.64
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with broad substrate specificity and great application potentials
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Kun Wang, Huiying Luo1, Yingguo Bai, Pengjun Shi, Huoqing Huang, Xianli Xue,
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Bin Yao1
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Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research
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Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, People’s
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Republic of China
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Corresponding authors. Address: Key Laboratory for Feed Biotechnology of the
Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun South Street, Beijing 100081, P. R. China. Tel.: +86 10 82106053; fax: +86 10 82106054. E-mail addresses:
[email protected] (H. Luo),
[email protected] (B. Yao).
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Fig. S1 Amino acid sequence alignment of TeEgl5A from Talaromyces emersonii
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with GH5 endoglucanases from Thermoascus aurantiacus (1GZJ), Trichoderma
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reesei (3QR3), and Piromyces rhizinflata (3AYR) using the ClustalW program. The
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highly conserved residues and catalytic residues are indicated with black asterisks and
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pounds, respectively. The conserved motifs used for degenerate primer design are
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boxed.
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