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Fig. 2 | Biotechnology for Biofuels

Fig. 2

From: A novel thermostable GH10 xylanase with activities on a wide variety of cellulosic substrates from a xylanolytic Bacillus strain exhibiting significant synergy with commercial Celluclast 1.5 L in pretreated corn stover hydrolysis

Fig. 2

Multiple sequence alignment of XynA with selected GH10 enzymes. The CLUSTAL W and GENEDOC program were used for multiple sequence alignment. The enzymes and GenBank accession numbers used were xylanases from Bacillus sp. KW1 [XynA, MK064556 (this study)], Bacillus sp. HJ14 (rXynAHJ14, AHH02587), Streptomyces lividans (XlnA32kDa, 1XAS), and Caldicellulosiruptor bescii DSM 6725 (CbXyn10C, 5OFJ_A). Among them, XynA (this study) and CbXyn10C are GH10 enzymes with both xylanase and cellulase activities, while rXynAHJ14 and XlnA32kDa are two GH10 xylanases without reported cellulase activity. The 2 catalytic Glu residues are marked with open triangles, while the 12 conserved residues responsible for interplaying with both cello-oligosaccharides and xylo-oligosaccharides identified in CbXyn10C are denoted with solid diamonds. The sequences enclosed in blue square brackets are the GH10 domains of XynA and rXynAHJ14; the 15 different amino acids between XynA and rXynAHJ14 in GH10 domains are denoted with the blue inverted arrows

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