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Figure 1 | Biotechnology for Biofuels

Figure 1

From: Contribution of a family 1 carbohydrate-binding module in thermostable glycoside hydrolase 10 xylanase from Talaromyces cellulolyticus toward synergistic enzymatic hydrolysis of lignocellulose

Figure 1

Amino acid sequence of Xyl10A with predicted secondary structural elements. The putative signal sequence is shown in italics. The putative domains in mature Xyl10A are as follows: catalytic domain (amino-acid residues 20 to 335); Ser/Thr-rich linker region (336 to 372), underlined; CBM1 (373 to 407), double underlined. C-terminal residues of Xyl10AdLC (Leu334), Xyl10AdC (Gly372), and Xyl10Awt (Leu407) are enclosed in a box. The predicted catalytic residues are shown in filled black boxes. The predicted secondary structural elements (α-helices and β-strands) based on the structure of a GH10 xylanase from Fusarium oxysporum (FoXyn10a, sequence identity, 50%, PDB ID, 3U7B) as template [50] are indicated above the sequence.

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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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